Title of Invention

ALKALINE MANNANASES FROM BACILLUS SP

Abstract

ABSTRACT INVPCT/2000/00787/CHE "ALKALINE MANNANASES FROM BACILLUS SP" The present invention relates to an isolated mannanase which is (a) a polypeptide encodable by the mannanase enzyme encoding part of the DNA -sequence cloned into the plasmid present in Escherichia coli DSM 12197, or (b) a polypeptide comprising an amino acid sequence as shown in positions 31-330 of SEQIDNO:2,or (c) a polypeptide encodable by the DNA sequence as shown in positions 91-990 or positions 91-1470 of SEQ ID NO:I, or (d) an analogue of the polypeptide defined in (a) or (b) which is at least 65% homologous with said polypeptide, or a fragment of (a), (b) or (c).

Full Text

The present invnetion relates to alkaline raannases from Bacillus Sp specifically to microbial enzymes exhibiting mannanase activity as their major enzymatic activity in the neutral ar;c alkaline cH ranges; to a method of producing such enzymes; and tc net.-.cds for using such enzymes in the paper and pulp, textile, cii drilling, cleaning, laundering, detergent and cellulose finer processing industries. BACKGROUND OF THE INVENTION Mannar, containing polysaccharides are a major component cf cne hemice.lulose fraction in woods and endosperm m many leguminous seeds and in some ma:ure seeds of non-leguminous plants. Essentially unsubstituted linear beta-1,4-mannan is found in some r.-r,-leguminous plants. Unsubstituted beta-1,4-mar.nan which is present e.g. in ivory nuts resembles cellulose in the conformation cf the individual polysaccharide chains, and is water-insoluble. In leguminous seeds, water-scluble galactcmannan is the main storage carbohydrate comprising up to 20% cf the total dry weight. Galactcmannans have a linear beta-1,4-m.anna.n backbone substituted with single alpha-1, 6-galactcse, optionally substituted with acetyl groups. Mannans are also found in several monoootyledonous plants and are the most abundant polysaccharides in the cell wail material in palm kernel meal. Glucomannans are linear polysaccharides with a backbone of beta-1,4-linked mannose and glucose alternating in a more or less regular manner, the backbone optionally being substituted with galactose and/or acetyl groups. Mannans, galactcmannans, glucomannans and galactoglucomannans ;i.e. glucomannan backbones with branched galactose) contribute to more than 50% of the softwood hemicellulose. Moreover, the cellulose of many red algae certains a significant amount of mannose. Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, Nc. 11, pp. 3505-3510 (1990) describes a. beta-mannanase derived from Bacillus stearothermophilics in dimer form having molecular weight of 162 kDa and an optimum pH of 5.5-7.5. Mendcza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-manr.anase derived from Bacillus subcilis having a molecular weight of 3S kDa, an optimum activity at pH 5.0 and 55°C and a pi of 4.8. JP-A-03047076 discloses a beta-rr.ar.nanase derived from Bacillus sp., having a molecular weight of 37±3 kDa measured by gel filtration, an optimum pH of 8-10 and a pi of 5.3-5.4. J?-A-63056289 describes the production of an alkaline, thermostable beta-mannanase which hydrolyses beta-1,4-D-mannopyranoside bonds of e.g. mannans and produces manno-oligosaccharides. JP-A- ■ 63036775 relates to the Bacillus microorganism FERM P-8356 which produces beta-mannanase and beta-mannosidase at an alkaline pK. JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001 having molecular weights of 43±3 kDa and 57±3 kDa and optimum pH of 8-10. A purified mannanase from Bacillus amylcliquafaciens useful in the bleaching of pulp and paper and a method of preparation thereof is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active at an extreme pH and temperature. WO 94/25576 discloses an enzyme from Aspergillus aculaatus, CBS 101.43, exhibiting mannanase activity which may be useful for degradation or modification of plant or algae cell wall materiali WO 93/24622 discloses a mannanase isolated from Trichoderma reseei useful for bleaching iignocellulosic pulps. WG 95/35362 discloses cleaning compositions containing plan- cell wall degrading enzymes having pectinase ar.d/cr hemicellulase and optionally cellulase activity for the re-oval of stains of vegetable origin and further discloses an alkaline mannanase fro™ the strain C11SB.G17. It is an object of the present invention to provide a novel and efficient enzyme exhibiting mannanase activity also in the alkaline pH range, e.g. when applied in cleaning compositions or different industrial orocesses. SUMMARY OF THE INVENTION The -inventors have now found novel enzymes having substantial mannanase activity, i.e. enzymes exhibiting mannanase activity which may be obtained from a bacterial strain of the genus Bacillus and have succeeded in identifying DNA sequences encoding such enzymes. The DNA sequences are listed in the sequence listing as SEQ in Nc. 1, 5, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29 ana 31; and the deduced amino acid sequences are listed in the sequence listing as SEQ ID No. 2, 6, 10, 12, 14, 16, 16, 20, 22, 24, 26, 28, 30 and 32, respectively. It is believed that the novel enzymes will be classified according to the Enzyme Nomenclature in the Enzyme Class EC 3.2.1.7S. In a first aspect, the present invention relates to a mannanase which is i) a polypeptide produced by Bacillus sp. 1633, ii) a polypeptide comprising an amino acid sequence as shown in positions 31-330 of SEQ ID N0:2, or iiil an analogue of the polypeptide defined in i) or ii) which is at least 651 homologous with said polypeptide, is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal antibody raised against said polypeptide in purified f o rir.. Within one aspect, the present invention provides an iso¬lated polynucleotide molecule selected from the group consisting of (a) polynucleotide molecules encoaing a polypeptide having mannanase activity anc comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from nucleotide 91 to nucleotide 990; (b) species hcmologs of fa); (c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 31 to amino acid residue 330; (d) molecules complementary tc (a), ib) cr (c); and (e) degenerate nucleotide sequences of (a), (b), (c) cr (d) . The piasmid pBXM3 comprising the polynucleotide molecule (the DMA sequence) encoding a mannanase of the present invention has been transformed into a strain of the Escherichia coli which was deposited by the inventors according to the 3udapest Treaty on the International Recognition, of the Deposit of Microorganisms for the Purposes of Patent Procedure at Che Deutsche Sammlung von Kikroorgar.ismen una Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, en 29 May 1998 under the deposition number DSM 12197. Within another aspect of the invention there is provided an expression vector comprising the following operably linked elements: a transcription promoter; a DNA segment selected from the group consisting of (a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from nucleotide 91 to nucleotide 990; (b) species homologs of (a); (c) polynucleotide molecules tnat encode a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 31 to amino acid residue 330; and (ci) degenerate nucleotide sequences cf la), (b;, cr (c); and a transcription terminator. Within yet another aspect cf the present invention there is provided a cultured cell into which has beer, introduced an expression vector as disclosed above, wherein said cell ex¬presses the polypeptide encoded by the DNA segment. Further aspects cf the present invention provide an iso¬lated polypeptide having mannanase activity selected from the group consisting of (a) polypeptide molecules comprising a sequence of amino acid residues as shown in SEQ ID NO:2 from amine acid residue 31 to amino acid residue 330; (b) species homologs of (a;; and a fusion protein having mannanase activity comprising a first polypeptide part exhibiting mannanase activ¬ity and a second polypeptide part exhibiting cellulose binding function, the second polypeptide preferably being a cellulose oinding domain (CBD), such as a fusion protein represented by SEQ ID NO:4. Within another aspect cf the present invention there is provided a composition comprising a purified polypeptide accord¬ing to the invention in combination with other polypeptides. Within another aspect of the present invention there are provided methods for producing a polypeptide according to the Invention comprising culturing a cell into which has been intro-iuced an expression vector as disclosed above, whereby said cell expresses a polypeptide encoded by the DNA segment and recover¬ing the polypeptide. The novel enzyme cf the present invention is useful for the reatment of cellulosic material, especially cellulose-■ontaining fiber, yarn, woven or non-woven fabric, treatment of Lechanical paper-making pulps, kraft pulps cr recycled waste >aper, and for retting cf fibres. The treatment can be carried out during the processing of cellulosic material into a material ready for manufacture c: paper or of Garment or fabric, the Latter e.g. in the desizing cr securing step; or during industrial or household laundering of such fabric or garment. Accordingly, in further aspects the present invention relates to a cleaning or detergent composition comprising the enzyme of the invention; and to use of the enzyme of the invention for the treatment, eg cleaning, of cellulose-containing fibers, yarn, woven or non-woven fabric, as well as synthetic or partly synthetic fabric. It is conzempiated that the enzyme of the invention is useful in ar. enzymatic scouring process and/or desizing (removal of mannan size) in the preparation of ceiluiosic material e.g. for proper response in subsequent eyeing operations. The enzyme is also useful for rerroval of mannan containing print paste. Further, detergent compositions comprising the novel enzyme are capable of removing cr bleaching certain soils or stains present en.laundry, especially soils and spots resulting from mannan containing food, plants, and the like. Further, treatment with cleaning or detergent compositions comprising the novel enzyme can improve whiteness as well as prevent binding cf certain soils to the ceiluiosic material. Accordingly, the present invention also relates to clean¬ing compositions, including laundry, dishwashing, hard surface cleaner, personal cleansing and oral/dental compositions, com¬prising the mannanase of the invenntion. Further, the present invention relates to such cleaning compositions comprising a mannanase and an enzyme selected from cellulases, proteases, lipases, amylases, pectin degrading enzymes and xyioglucanases, such compositions providing superior cleaning performance, i.e. superior stain removal, dingy cleaning or whiteness mainte¬nance. DEFINITIONS Prior to discussing this invention in further detail, the following terir.s will first be defined. The tern*. v,ortholog" (or "species homolog") denotes s polypeptide or protein obtained from one species that has homol¬ogy to an analogous polypeptide or protein from a'different species. The term "paraloc" denotes a polypeptide cr protein obtained from a given species that has homology to a distinct polypeptide or protein from that same species. The term "expression vector" denotes a DNA molecule, linear or circular, that comprises a segment encoding a polypeptide cf interest operably linked to additional segments that provide for its transcription. Such additional segments may include promoter and terminator sequences, and may optionally include one or mere origins of replication, one or more selectable markers, an enhancer, a poiyadenylation signal, and the like. Expression sectors are generally derived from plas-rdd or viral DHA, cr may contain elements cf both. The expression vector of the invention nay be any expression vector that is conveniently subjected to recombinant DNA procedures, and the choice of vector will often lepend on the host ceil into which the vector is to be ntroduced. Thus, the vector may be an autonomously replicating ector, i.e. a vector which exists as an extrachrcmosomal ntity, the replication of which is independent cf chromosomal eplication, e.g. a plasmid. Alternatively, the vector may be ne which, when introduced into a host ceil, is integrated into he host cell genome and replicated together with the hrornosome (s) into which it has been integrated. The term "recombinant expressed" or "recombinantly expressed" used herein in connection with expression cf a polypeptide or crcte:r: is defined according no the standard definition in the art. Re conic inantly expression cf a protein is generally performed oy using an expression vector as described immediately abcve. ; The term "isolated", when applied to a polynucleotide mole¬cule, denotes that tr.e polynucleotide has been removed from its natural genetic milieu and is thus free of other extraneous or unwanted coding sequences, and is in a form suitable for use within genetically engineered orotein production systems. Such isolated molecules are those that are separated from their natural environment and include cDNA and genomic clones. Iso¬lated DMA molecules cf the present invention are free of other genes with which they are ordinarily associated, but may include naturally occurring 5' and 3' untranslated regions such as promoters and terminators. The identification of associated regions will be evident to one of ordinary skill in the art (see for example, Dynan and Tijan, Nature 316_:114-78, 1985). The term "an isolated polynucleotide" may alternatively be termed "a cloned polynucleotide". When applied to a protein/polypeptide, the term "isolated" indicates that the protein is found in a condition other than its native environment. In a preferred form, the isolated pro¬tein is substantially free cf other proteins, particularly other homologous proteins (i.e. "homologous impurities" (see below)). It is preferred to provide the protein in a greater than 40% pure form, more preferably greater than 60% pure form. Even more preferably it is preferred to provide the protein in a highly purified form, i.e., greater than 8G% pure, more preferably greater than 95% pure, and even more preferably greater than 99% pure, as determined by SDS-PAGE. The term "isolated protein/polypeptide may alternatively be termed "purified protein/polypeptide". Tiie term "homologous impurities" means any invcurity (e.g. an¬other polypeptide zr.ar- tne pelypeotide of the ir.vendor) which originate from the homologous ceil where the polypeptide of the invention is originally obtained from. The terrr. "obtained from" as used herein in connection with a specific microbial source, means that the polynucleotide and/or polypeptide is produced by the specific source (homologous expression), or by a cell in which 3 gene from the source have beer, inserted (heterologous expression) . The term "cperably linked", when referring to DMA segments, denotes that the segments are arranged so that they function in concert for their intended purposes, e.g. transcription initi¬ates in the promoter and proceeds through the coding segment to the terminator The term, "polynucleotide" denotes a single- or dcuble-stranded polymer of ceoKVribonucleotide cr ribonucleotide bases read from the 5' to tne 3' end. Polynucleotides include RNA and DNA, and may be isolated from natural sources, synthesized in vitro, or prepared from a combination of natural and synthetic molecules. The term "complements' of polynucleotide molecules" denotes polynucleotide molecules having a complementary base sequence and reverse orientation as compared to a reference sequence. For example, the sequence 5' ATGCACGGG 3' is complementary to 5' CCCGTGCAT 3'. The term "degenerate nucleotide sequence" denotes a sequence of nucleotides that includes one or more degenerate codons (as compared to a reference polynucleotide molecule that encodes a polypeptide). Degenerate codons contain different triplets of nucleotides, but encode the same amino acid residue (i.e., GAU and GAC triplets each encode Asp) . The ;srn "promoter" denotes a portion cf a gene contair.ir.a DMA sequences that provide fcr the binding of RNA polymerase and initiation of transcription. promoter sequences are commonly, but not always, four.d in the 51 nor.-coding regions of genes. \ The tern "secretory signal sequence" denotes a DK'A sequence that encodes a polypeptide (a "secretory peptide") that, as a component of a larger polypeptide, directs the larger polypep¬tide through a secretory pathway cf a ceil in whicn. it is syn¬thesized. The larger peptide is commonly cleaved to remove the secretory peptide during transit through the secretory pathway. The term "enzyme core" denotes a single domain enzyme which may or may not have been modified, or altered, but which has retained its original activity; the catalytic domain as known in the art has remained intact and functional. By the term "linker" or "spacer" is meant a polypeptide comprising at least two amino acids which may be present between the domains of a nvuitiaomain protein, for example.an enzyme comprising an enzyme core and a binding domain such as a cellulose binding domain (CBD) or any other enzyme hybrid, or between two proteins or polypeptides expressed as a fusion polypeptide, for example a fusion protein comprising two core enzymes. For example, the fusion protein cf an enzyme core with a CBD is provided by fusing a DNA sequence encoding the enzyme core, a DNA sequence encoding the linker and a DNA sequence encoding the CBD sequentially into one open reading frame and expressing this construct. The term "manr.sr.ase" or "galactomar.r.anase" denotes a rran-nanase enzyme defined according to the art as officially being named mar.nan endc-1,4-beta-mannosidase and having the alterna¬tive names beta-mannanase and endo-1,4-mannanase and catalysing hydrolyses of 1,4-beta-D-mannosidic linkages in mannans, galac-tomannans, glucomannans, and galactoglucomannans which enzyme is classified according tc the enzyme Nomenclature as EC 3.2.1.73 (bttp: //www. expasy. ch 'enzyme) . DETAILED DESCRIPTION CF THE INVENTION HOW TO USE h SEQUENCE OF THE INVENTION TO GET OTHER RELATED SEQUENCES: The disclosed sequence information herein relating tc a polynucleotide sequence encoding a mannanase of the invention can be used as a tool to identify other homologous raarr.ar.ases. For instance, polymerase chain reaction (PC?) car. be used to amplify sequences encoding other homologous mannanases from a variety of microbial sources, in particular of different Bacii-lus species. ASSAY FOP. ACTIVITY TEST A polypeptide of the invention having mannanase activity may be tested for mannanase activity according tc standard test procedures known in the art, such as by applying a solution to be tested tc 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan jcarob), i.e. substrate for ■the assay of er.do-1,4-beta-D-ir.ar.nanase available as CatNc. I-A2GMA from the company Megazyme (Megazyme's Internet address: http://www.mecazyme.com/Purchase/index,html). POLYNUCLEOTIDES Within preferred embodiments of the invention an isolated polynucleotide of the invention will hybridize to similar sized regions of SEQ ID NO: 1, or a sequence complementary thereto, under at Least medium stringency conditions. In particular polynucleotides of the invention will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:l or a partial sequence comprising the segment shown in positions 91-990 of SEQ ID rJO:i which segment encodes fcr the cstalytically active domain or enzyme cere of the nannanase of trie invention or any probe comprising a subsequence shewn in positions 91-990 cf SEQ ID N0:1 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as Described m detail below. Suitable experimental conditions for Determining hybridization at medium, or high stringency between a nucleotide probe and a homologous DNA cr RNA sequence involves presoaking of the filter containing the DNA fragments or RNA to hybridize in 5 x SSC (Sodium chloride/Sodium citrate, Sambrcok et =1. 1989) fcr 10 rr.in, and prehybridizaticn cf the filter in a solution of 5 x SSC, 5 x Denhardt's solution (SambrooK et al. 1939), 0.5 % SDS and ICC pg/ml cf denatured sonicated salmon sperm DMA (Sarr.brook et al. 1989), followed by hybridization in the same solution containing a concentration of lOng/mi of a random-primed (Feinberg, A. P. and Vcgelstein, B. (1983) Anal. Biochem. 132:6-13), 32F-dCT?-labeled (specific activity higher than 1 x 109 cpm/ug) probe for 12 hours at ca. 45aC. The filter is then washed twice for 30 minutes in 2 x SSC, 0.5 % SDS at least 60°C (medium stringency), still more preferably at least 65°C (medium/high stringency), even more preferably at least 70°C (high stringency), and even more preferably at least 75°C (very high stringency). Molecules tc which the oligonucleotide probe hybridizes under these conditions are detected using a x-ray film. Other useful isolated polynucleotides are those which will hybridize to similar sized regions of SEQ ID NO: 5, SEQ ID NO: S, SEQ ID NO: 11, SEQ ID NO: 13, SEQ ID NO: 15, SEQ ID NO: 17, SEQ ID NO: 19, SEQ ID NO: 21, SEQ ID NO: 23, SEQ ID NO: 25, SEQ ID NO: 27, SEQ ID NO: 29 cr SEQ ID NO: 31, respectively, or a sequence complementary thereto, under at least medium stringency conditions. Particularly useful are polynucleotides which will hybridize to a denatured double-stranded DMA probe comprising eit.ner the full sequence shown in SEQ ID NO: 5 cr a partial sequence comprising the segment shown in positions 94-1032 of SEQ ID NO:5 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 94-1032 cf SEQ ID NO:5 which subsequence has a length of at least aeon: 100 base pairs under at least .medium stringency conditions, but preferably at high stringency conditions as described :r. detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DtCA probe comprising either the full sequence shown in SEQ ID NO: 9 or a partial sequence comprising the segment shown in positions 94-1086 of SEQ ID NO:9 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 94-1086 of SEQ ID KO:9 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:II cr a partial sequence comprising the segment shown in positions 97-993 of SEQ ID NO:11 which segment encodes for the catalytically active domain or enzyme core cf the mannanase of the invention or any probe comprising a subsequence shown in positions 97-933 cf SEQ ID NC:I1 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double- stranded DNA probe comprising either the full seauer.ce sncwn in SEQ ID NO:13 cr a partial sequence comprising the segment shown in positions 438-146^ cf SEQ ID NO:13 whrcn segment encodes for the catalytically active domain or er.zyrr.e core of the nannanase of the invention or any probe comprising a subsequence shown in positions 498-1^64 cf SEQ ID NO:13 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in derail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising eitner the full sequence shown in SEQ ID N0:15 or & partial sequence comprising che segment shewn in positions 204-1107 cf SEQ ID NO:15 which segment encodes for the catalytically active domain or enzyme core cf the mannanase of the invention or any probe comprising a subsequence shown in positions 204-1107 of SEQ ID NO:15 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the sequence'shown in SEQ ID NO;17 or any probe comprising a subsequence of SEQ ID NO:17 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA. probe comprising either the sequence shown in SEQ ID NO:19 or any probe comprising a subsequence of SEQ ID NO:19 which subsequence has a length of at least about 1C0 base pairs under at least medium stringency conditions, but preferably at : high stringency conditions as described in detail'above; as well as polynucleotides which will hybridize to a denatured double- strands a CNA prcbe comprising either tr.e f uil ssauer.ce s.ioun in SEQ ID N0:21 or a part.al sequence- comprising the segment s.town m positions SS-96C of SEQ ID NO:21 which segment encodes for the catalytically active domain or enzyme core of the mannanase ci the invention or any probe comprising a subsequence shown m positions 88-960 of SEQ ID NO: 21 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shewn, in SEQ ID NO:23 or any probe comprising a subsequence of SEQ ID NO:23 which subsequence has a length cf at lease about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:25 or a partial sequence comprising the segment shown in positions 904-1874 of SEQ ID NO:25 which segment encodes for the catalytically active domain or enzyme core of the mannanase cf the invention or any probe comprising a subsequence shown in positions 904-1874 of SEQ ID NO:25 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either the full sequence shown in SEQ ID NO:27 or a partial sequence comprising the segment shewn in positions 498-1488 of SEQ ID NO:27 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 498-14SS of SEQ ID NO;27 which subsequence has a length cf at least abc.it 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above; as well as DOlynucleotides which will hybridize to a denatured double-stranded DNA probe comprising either ohe full sequence shown in jSQ ID NO:29 or a partial sequence comprising the segment shown j.n positions 13-1083 of SEQ ID NO;29 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions "79-1063 of SEQ ID NO:29 which subsequence has a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at hign stringency conditions as described in detail above; as well as polynucleotides which will hybridize to a denatured double-stranded DKA probe comprising either the full sequence shown in SEQ ID NO:31 or a partial sequence comprising the segment shown ir. positions 1779-2709 of SEQ ID NO: 31 which segment encodes for the catalytically active domain or enzyme core of the mannanase of the invention or any probe comprising a subsequence shown in positions 1779-2709 cf SEQ ID NO:31 which subsequence has a lengoh of at least about 100 base pairs under at least medium stringency conditions, but preferably at high stringency conditions as described in detail above. As previously noted, the isolated polynucleotides of the present invention include DNA and RNA. Methods for isolating DNA and RNA are well known in the art. DNA, and RNA encoding genes of interest can be cloned in Gene Banks or DNA libraries by means cf methods known in the art. Polynucleotides encoding polypeptides having mannanase activity of the invention are then identified and isolated by, for example, hybridization or PCR. The preser.' invention further pre ■.■ides counterpart: polypeptides and polynucleotides frorr different bacterial strains (ort.nclogs cr paralogs;. Of particular interest are mannanase polypeptides from gram-positive alkalophilic strains, including species of Bacillus such as Bacillus sp., Bacillus agaradhaerens, Bacillus halodurans, Bacillus clausii and Bacillus lichanifonais; and mannanase polypept ides from Thermoanaerabactsr group, including species of Caldicellulcsiruptor. Also mannanase polypeptides from the fungus Humicols or Scyzalidium, in particular the species Humicola ir.sclens cr S~yzalidium thermophiluni, are of interest. Species ncmciogues of a polypeptide with mannanase activity cf the invention can he cloned using information and compositions provided by the present invention in combination with conventional cloning techniques. For example, a DNA sequence of the present invention can be cloned using chromosomal DNA obtained from a cell type that expresses the protein. Suitable sources of DNA can be identified by probing Northern, or Southern blots with probes designed from the sequences disclosed herein. A library is then prepared from chromosomal DNA of a positive cell line. A DNA sequence of the invention encoding an polypeptide having mannanase activity can then be isolated by a variety cf methods, such as by probing with probes designed from the sequences disclosed in the present specification and claims or with one or mere sets of degenerate probes based on the disclosed sequences. A DNA sequence cf the invention can also be cloned using the polymerase chain reaction, or PCR (Muliis, U.S. Patent 4,683,202), using primers designed fron the sequences disclosed herein. Within an additional method, the DNA library can be used to transform or transfect host cells, and expression of the DNA cf interest can be detected with an antibody (nonc-clonal or polyclonal) raised against the nar.nanass cloned from E.sc, expressed and purified as described in Materials and Methods and Example 1, cr bv an activity test relating to a polypeptide having mannanase activity. The mannanase encoding part cf the DNA sequence fS~C_ Z2 M0:1} cloned into piasrrid pBXM3 present in Escherichia cell DSM 12197 ar.d/cr an analogue DNA sequence of the invention may be cloned from a strain cf the bacterial species Bacillus s-. 1633, or another cr related organism as described herein. The mannanase encoding part cf the polynucleotide molecule (the DNA sequence of SEQ ID NC:5; was transformed a strain cf the Escherichia coli which was deposited by che inventors according to the Eudapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammiung von Mikroorgar.ismen end Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 18 May 1998 under the deposition number DSM 121SC; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:5) and/or an analogue DNA sequence thereof may be cloned from a strain cf the bacterial species Bacillus agaradhaerens, for example from the type strain DSM 8721, or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:9) was transformed a strain of the Escherichia eeli which was deposited by the inventors according to the 3udapest Treaty on the International Recognition of the Deposit cf Microorganisms for the Purposes of Patent Procedure at the Deutsche Sam.lung von Mik.roorganisn.en und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic cf Germany, on 7 October 1998 under the deposition number DSM 12433; this mannanase encoding part of the polynucieccice molecule (the DMA sequence or SEQ ID NO: 9 ;■ and/or at. analogue DHA sequence thereof nay be cloned from a strain of the bacterial species Bacillus sp. AAI12 cr another or related organism as described herein. The mannanase encoding part cf the polynucleotide molecule (the DNA sequence of SEQ ID NO:11) was transformed a strain of tne Escherichia cell wnich was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit cf Microorganisms for the Purposes of Patent Procedure at the Deutsche Saratlung von Mikrcorgar.ismer. und Zellkuituren GmbH, Hascherocer Wee lb, D-38124 Eraunsohwetg, Federal Republic of Germany, en 9 October 1998 under the deposition number DSM 124 41; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO: 11) ar.d/or an analogue 3KA sequence thereof may be cloned from a strain of the bacterial species Bacillus haloduzar.s cr another cr related organism, as described herein". The mannanase encoding part of the polynucleotide molecule (the DMA sequence cf SEQ ID NO:13} was transformed a strain of the Escherichia coli which was deposited by the inventors according to tne Budapest Treaty on the International Recognition of the Deposit of Kicroorganisms for the purposes of Patent Procedure at the Deutsche Sammlung von Mikroorgar.ismen und Zellkuituren GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 11 May 1995 under the deposition number DSM 998 4; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:13) and/or an analogue DKA sequence thereof may be cloned from a strain of the fungal species Humicola inscdens cr another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID N0:15) was transformed a strain, cf the Escherichia ccii wnich was deposited by the inventors accessing to the Budapest Treaty en "he In-grnauonal Recognition of the Deposit: cf Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorganismer. | una ZeUkulturer. GmbH, Mascheroder Weg lb, D-3S124 Braunschweig, Federal Republic cf Germany, on 5 October 1998 under the deposition number DSM 124 32; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:15} and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. AA349 or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DHA sequence of SEQ ID NO: 17) was transformed a strain of the Escherickia ccii which was deposited by the inventors according to the Eudapest Treaty en the International Recognition of the Deposit cf Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung ven Mikroorgar.ismen und Zellkulturer. GmbH, Mascheroder Weg lb, D-38124 Eraur.sehweig, Federal Republic cf Germany, on 4 June 1999 under the deposition number DSM 1284'/; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:IV) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:19) was transformed a strain of the Escherichia eeli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikroorgar.ismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 4 June 1999 under the deposition r number DSM 12 34 6; this rtannanase encoding part cf the polynucleotide molecule (the- OKA sequence of SEQ' ID NO:19: and/cr an analogue DMA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding pare of the polynucleotide molecule (the DNA sequence of SEQ ID N0:21) was transformed a strain cf the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition cf the Deposit of Microorganisms for the Purposes cf Patent Procedure at the Deutsche Sammlunc von Mikroorganismen una Zellkulturen GmbH, Mascheroder Weg lb, D-3S124 Eraunscoweig, Federal Republic of Germany, on 4 June 1999 under the deposition number DSM 1284 9; this mannanase encoding part cf the polynucleotide molecule (the DKA sequence of SEQ ID N0:21) and/or an analogue DNA sequence thereof may be cloned from, a strain cf the bacterial species Bacillus clausii cr another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:23) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the 3udapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Samrnlung von Mikroorga.nismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic cf Germany, on 4 June 1999 under the deposition number DSM 12850; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:23) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding par- cf the polynucleotide molecule (che DMA sequence of SEQ ID MO: 25} was transformed a strain cf the Escherichia, coli which was deposited by the inventors according to the Budapest Treaty on the International | Recognition cf the Deposit of Microorganisms for the Purposes of Patent Frocedure at the Deutsche Sammlung von Mikrcorganisrfien unci Zellkulcuren GmbH, Mascheroder Weg lb, D-38124 Braunschv;e _g, Federal Republic of Germany, on 4 June 1999 under.the deposition number DSM 12846; this mannanase encoding part cf the polynucleotide molecule (the DKA sequence or SEQ ID KO:25j and/cr an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:27) was transformed a strain cf the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes cf Patent Procedure at the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic cf Germany, on 4 June 1999 under the deposition number DSM 12851; this mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:27) and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Bacillus sp. or another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DNA sequence of SEQ ID NO:29) was transformed a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty en the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikrocrganismer. and Zelikuituren GmbH, Mascheroder Weg lb, D-3S124 Eraur.schweig, Federal Republic of Germany, en 4 June 1999 under the deposition number DSM 12S52; this mannanase encoding part: cf the polynucleotide molecule (the DMA sequence cf SEQ ID MO: 29.) and/or an analogue DNA sequence thereof rtay be clor.ee from a strain of the bacterial species Bacillus lichenifcrnns cr another or related organism as described herein. The mannanase encoding part of the polynucleotide molecule (the DMA ssquer.ee cf SEQ ID N0:31) was transformed a strain cf the Escherichia coli which was deposited by the inveutcrs according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlur.g von Miicroorganismen una Zeilkuituren GmbH, Mascheroder Weg lb, D-38I24 Braunschweig, Federal Republic cf Germany, or. 5 October 199S under the deposition number DSM 12436; this mannanase encoding part of the polynucleotide molecule (the DMA sequence of SEQ ID N0:3i! and/or an analogue DNA sequence thereof may be cloned from a strain of the bacterial species Caldicellulosiruptcr sp. or another or related organism as described herein. Alternatively, the analogous sequence may be constructed on the basis cf the DNA sequence obtainable from the plasrr.id present in Escherichia coli DSM 12197 (which is believed to be identical to the attached SEQ ID MO-.l), the plasmid present in Escherichia coli DSM 12180 (which is believed tc be identical to the attached SEQ ID NO:5), the plasmid present in Escherichia coli DSM 12433 (which is believed to be identical to tne attached SEQ ID NO:9), the plasmid present in Escherichia coli DSM 12441 (which is believed to be identical to the attached SEQ ID NO:11), the plasmid present in Escherichia coli DSM 9384 (which is believed to be identical to the attached SEQ ID NO:13), the plasmid present in Escherichia coli DSM 12432 (which is believed to be identical :o tne attached SEQ ID MC:!;;, the plasmid present in Escherichia coii DSM 128-57 (which is believed to be identical to the attaches SEQ ID MO:17;, the plasmid present in Escherichia coli DSM 12843 (which is believes tc be identical to the attached SEQ ID NO: 19), the plasmid present in Escherichia coii DSM 12849 (which is believed to be identical to the attached SEQ ID N0:21), the plasmid present in Escherichia coli DSM 1285C (which is believed to be identical to the attached SEQ ID NC:23), the plasmid present in Escherichia coii DSM 12846 (which is believed to be identical to the attached SEQ ID NO:25), the plasmid present in Escherichia cell DSM 12251 (which is believed to be identical to the attached SEQ ID NO:27), the plasmid present in Escherichia coli DSM 12552 (which is believed to be identical to the attached SEQ ID NO:29) or the plasmid present in Escherichia coii DSM 12436 (which is believed to be identical to the attached SEQ ID N0:31), e.g be a sub¬sequence thereof, anri/cr by introduction of nucleotide substitutions which dc not give rise to another amine acid sequence of the mannanase encoded by the DMA sequence, but which corresponds to the coden usage of the host organism intended for production of the enzyme, or by introduction of nucleotide substitutions which may give rise to a different amino acid sequence (i.e. a variant of the msnnan degrading enzyme of the invention). POLYPEPTIDES The sequence of amino acids in positions 31-49C of SEQ ID \T0: 2 is a mature mannanase sequence. The sequence of amine acids nos. 1-30 of SEQ ID NO: 2 is the signal peptide. It is teiieved that the subsequence of amino acids in positions 31-330 of SEQ ID NO: 2 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises a linker in positions 331-542 and at least one C-terninal domain of unknown function in positions 343-^90. Since the object cf the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids ncs. 31-330 of SEQ ID NO: 2, ie a catalytical domain, optionally cperably iir.kec, either N-terminally cr C-terrr.inally, to one or two or more than two-other domains cf a different functionality. The domain having the subsequence of amino acids nos. 343-49C of SEQ ID K'D: 2 is a domain of the mannanase enzyme of unknown function, this domain being highly homologous with similar domains in known mannanases, cf. example 1. The sequence cf amino acids in positions 32-494 cf SEC I-1 NO:6 is a mature mannanase sequence. The secuence cf ammo acids nos. 1-31 cf SEQ ID NO:6 is the signal peptide. It is believed that the subsequence cf amino acids in positions 32-34 4 of SEQ ID NO:6 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least one C-terminel domain of unknown function in positions 345-494. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 32-344 of SEQ ID NO: 6, ie a catalytical domain, optionally operably linked, either N-terminally or Oterminally, to one or two or more than two other domains of a different functionality. The sequence of amino acids in positions 32-586 cf SEQ ID NO:10 is a mature mannanase sequence. The sequence of amino acids nos. 1-31 of SEQ ID NO:10 is the signal peptide. It is believed that the subsequence of amino acids in positions 32-362 of SEQ ID NO:10 is the catalytic domain cf the mannanase enzyme and that the mature enzyme additionally comprises at least one C-terminal domain of unknown function in positions 363-586. Since tne or^ect of t.ne prese:.: invention is to cbtain a polypeptide which exhibits mar.nar.ase activity, the present invention relates to ar.y mannanase enzyme comprising the sequence of amino acids nos. 22-362 of SEQ ID NO': 10, ie a 1 catalytical domain, optionally operably linked, either K-terminally or C-terminaliy, tc one or tvjo or more than two other aomair.s or a different functionality. The sequence of amino acids in positions 33-331 of SEQ ID MO: 12 is a nature manr.anase sequence. The seauer.ce of snino acids ncs. 1-22 of SEQ ID MO:12 is the signal peptide. It is believed that the subsequence of amino acids in positions 33-331 of SEC; 33 l'0:il is the catalytic domain of the mannanase enzyme. This mannanase enzyme core comprising the sequence of ammo acids nos. 33-331 of SEQ 13 NO: 12, ie a catalytical domain, may or may not be cperably linked, either N-terminally cr C-terminally, to one or two or more than two other domains of a different functionality, ie being part of a fusion protein. The sequence of amino acids in positions 22-436 of SEQ 10 NO: 14 is a mature manr.anase sequence. The sequence of amine acids nos. 1-21 of SEQ ID NO:14 is the signal peptide. It is believed that tne subsequence of amino acids in positions 166-488 of SEQ ID M0:14 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least one N-terminal domain of unknown function in positions 22-164. Since the object of the present invention is tc cbtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 166-488 of SEQ ID MO: 14, ie a catalytical domain, optionally operably linked, either N-terminaliy or C-terminally, to one or two or more than two other domains of a different functionality. The sequence of amino acids in positions 26-369 c: SEQ ID NO: 16 is a mature mannanase sequence. The sea'je.ice cf amino acids nos. 1-23 cf SEQ ID NO:16 is the signal pep-ice, It is believed that the subsequence of amino acids in positions 63-3 59 | of SEQ ID NO: 16 is the catalytic domain of the mannanase er.zyrce and that the mature enzyme additionally comprises at least one ^'terminal domain of unknown function in positions 26-6". Since the object of the present invent ion is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence cf amine acids ncs. 68-369 of SEQ ID MO:16, ie a catalytical domain, optionally operably linked, either N-terrr.rnally cr C-termir.al ly, to one or two or more than two ether domains cf a different functionality. The sequence of amino acids of SEQ ID MO:18 is a partial sequence forming part cf a mature mannanase sequence. The present invention relates to any mannanase enzyme comprising the sequence of amino ecias nos. 1-305 of SEQ ID HO: 18. The sequence cf amino acids of SEQ ID NO:20 is a partial sequence forming part cf a mature mannanase sequence. The present invention relates to any mannanase enzyme comprising the sequence cf amino acids nos. 1-132 of SEQ ID NO:20. The sequence of amino acids in positions 29-320 of SEQ ID NO:22 is a mature mannanase sequence. The sequence of amino acids nos. 1-23 cf SEQ ID NO:22 is the signal peptide, it is oelieved that the subsequence cf amino acids in positions 29-320 zt SEQ ID NO:22 is the catalytic domain of the mannanase enzyme. This mannanase enzyme cere comprising the sequence of amino acids nos. 29-320 cf SEQ 10 NC:22, ie a catalytical domain, may )r may not be operably linked, either N-terminaxly cr C-".erminally, to one or two or more than two other domains cf a different functionality, ie being part of a fusion protein. The sequence of amino acids of SEQ ID NO: 24 is a Dartial sequence forming part c: a mature ir.anr.anase sequence. The present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 29-183 of SEQ ID NO:24. The sequence of ammo acids in positions 30-815 of SEQ ID NO:26 is a mature mannanase sequence. The sequence of amine acids r.os. 1-29 cf SEQ ID NO:26 is the signal peptide. It is believed that the subsequence of amine acids in positions 301-625 of SEQ ID NO: 26 is the catalytic domain of the manr.anase enzyme and that the mature enzyme additionally comprises at least two N-terrr.inai domain of unknown function in positions 44-166 and 195-300, respectively, and a C-terrr.inel domain of unknown function in positions 626-815. Since the object of the present invention is to obtain a polypeptide which exhibits mannar.ase activity, the present invention relates to any raannanase enzyme comprising the sequence of amino acids ncs. 301-625 cf SEQ ID NG:25, ie a catalytical domain, optionally operably linked, either N-termir.ally or C-terminally, to one or two or more than two ether domains of a different'functionality. The sequence of amino acids in positions 38-496 of SEQ ID NO:28 is a mature mannanase sequence. The sequence of ammo acids nos. 1-37 of SEQ ID NO:23 is the signal peptide. It is believed that the subsequence of amino acids in positions 166-496 of SEQ ID NO:23 is the catalytic domain of the mannanase enzyme and that the mature enzyme additionally comprises at least one N-terninal domain of unknown function in positions 38-165. Since the object of the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amino acids nos. 166-496 of SEQ ID NO:28, ie a catalytical domain, optionally operably linked, either M-terminally or C-terminally, to one or two or more than two other domains of 3 different functionality. The sequence of ax.ir.c acids in positions 26-361 cf SEQ ID K0:30 is a mature mannanase sequence. The sequence cf amino acids nos. i-25 of SEQ ID KC:30 is -he signal peptide. It is believed that the subsequence cf amino acids in positions 26-361 of SEQ ID NO:30 is the catalytic domain of the mannanase enzyme. This mannanase enzyme core comprising the sequence cf amino acids nos. 26-361 of SEQ ID NQ;3Q, ie a catalytical domain, may¬or may not oe optionally operably linked, either N-terminallv or C-terminally, to one or two or more than two other domains cf a different: functionality. The sequence cf amino acids in positions 23-9C3 cf SEQ ID NO:32 is a mature mannanase sequence. The sequence cf amino acids nos. 1-22 of SEQ ID KO:32 is the signal peptide. It is believed that the subsequence of amino acids in positions 553-903 of SEQ ID NO:32 is the catalytic domain of the mannanase enzyme and that the mature enzyme" additionally comprises at least three N-terminal domains cf unknown function in positions 23-214, 224-424 and 434-592, respectively. Since the object cf the present invention is to obtain a polypeptide which exhibits mannanase activity, the present invention relates to any mannanase enzyme comprising the sequence of amine.acids nos. 593-903 of SEQ ID NO:32, ie a catalytical domain, optionally operably linked, either N-terminally or C-terminally, to one or two or mere than two ether domains of a different functionality. The present invention also provides mannanase polypeptides that are substantially homologous to the polypeptides of SEQ ID NC:2, SEQ ID N0:6, SEQ ID N0:1C, SEQ ID NO:12, SEQ ID KO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO: 24, SEQ ID NO:26, SEQ ID NO-.28, SEQ ID N0-.3Q and SEQ ID NO:32, respectively, and species homologs (paralogs or orthologs) thereof. The term "substantially homologous" is used herein to denote polypeptides having 65%, crefer^Iy at least 70%, more preferably at least 75%, m0re preferably at least 80%, mere preferably at least 85%, ar.d even more preferably at least 90%, sequence identity to the sequence shown in amine acids nos. 33-340 cr nos. 33-490 of SEQ ID MO:2 or their crtholcgs cr paraiogs; or to the sequence shown in amino acids ncs. 32-54-3 cr nos. 32-494 of SEQ ID NO; 6 cr their orthologs or paraiogs; or to the sequence shown in amino acids nos. 32-362 or nos. 22-586 of SSQ ID NO:10 cr their orthclogs or paraiogs; cr tc the secuence shown in amino acids ncs. 33-331 of SEQ ID NO:12 or its orthologs or paraiogs; cr to the sequence shown in amino acids nos. 166-488 or nos. 22-433 of SEQ ID NO:14 or their orthologs cr paraiogs; or to the sequence shown in amine acids ncs. 66-369 or nos. 32-369 of S2Q ID NO:16 or their orthologs cr paraiogs; or to the sequence shewn m amino acids nos. 2-30 5 of SEQ ID NO:18 or its orthologs cr paraiogs; cr to the sequence shown in amino acids ncs. 1-132 cf SEQ ID NO:20 or its orthologs cr paraiogs; or tc the sequence shown in amino acids nos. 29-320 cf SEQ ID NO:22 or its orthologs cr paraiogs; or to the sequence shown in amino acids nos. 29-188 of SEQ ID NO:24 or its orthologs or paraiogs; or to the sequence shown in amino acids nos. 301-625 cr nos. 30-625 of SEQ ID N0:26 or their orthclogs or paraiogs; or to the sequence shown in amino acids nos. 166-496 or nos. 38-496 of SEQ ID NO:28 or their orthologs or paraiogs; or to the sequence shown in amino acids nos. 26-361 of SEQ ID NO:30 or its orthclogs or paraiogs; or to the sequence shown in amino acids nos. 593-903 or nos. 23-903 of SEQ ID NO:32 or their orthclogs or paraiogs. Such polypeptides will more preferably be at least 95% identical, and most preferably 98% or more identical to the sequence shown in amine acids nos. 31-330 or nos. 31-490 cf SEQ ID N0:2 cr its crtholcgs or paraiogs; or tc the sequence shown in amine acids nos. 22-344 or ncs. 32-494 o = SEQ ID MO:6 cr its orthologs cr paralogs; or cr the sequence shown j..n amine acids nos. 32-362 or ncs. 22-556 of SEQ ID NO:10 or its orthologs cr paralogs; or to the sequence shown in amino acids ncs. 33-331 of 1 SEQ ID NO:12 Cr its crtholcgs or paraiegs; or to the sequence shown in amino acids ncs. 166-488 or nos. 22-433 cf SEQ ID NO:14 or its orthologs or paralogs; cr to the sequence shown in amino acids nos. 68-369 or nos. 32-369 of SEQ ID NO:I6 or its orthologs or paralogs; cr to the sequence shewn in amino acids nos. 1-3C5 of SEQ ID ;;0:18 cr its orthologs cr paralogs; cr tc the sequence shewn in amine acids ncs. 1-132 of SEQ 2D NO:20 cr its orthologs cr paralogs; or to tne sequence shown in amine acids nos. 29-320 of SEQ ID N0:22 or its orthologs or paralogs; or tc the sequence shown in amino acids nos, 29-188 of SEQ ID NO:24 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 301-625 or nos. 30-625 of SEQ ID NO.-26 or its orthologs or paralogs; cr to the sequence shown in amino acids nos. 166-496 or nos. 38-496 cf SEQ ID NO:23 or its orthologs or paralogs; or to the sequence shown in amino acids-ncs. 26-361 of SEQ ID NO:30 or its orthologs or paralogs; or to the sequence shown in amino acids nos. 593-903 or nos. 23-903 cf SEQ ID N0:32 or its orthologs or paralogs. Percent sequence identity is determined by conventional nethods, by means of computer programs known in the art such as GAP provided in the GCG program package (Program Manual for the Wisconsin Package, Version 8, August 1994, Genetics Computer 3roup, 575 Science Drive, Madison, Wisconsin, USA 53711) as iisclosed in Keedleman, S.B. and Wunsch, CD., (1S7C), Journal Df Molecular Biology, 4S, 443-453, which is hereby incorporated uy reference in its entirety. GAP is used with the following settings for polypeptide sequence comparison: GAP creation penalty of 3.0 and GAP extension penalty of 0.1. Sequence identity of polynucleotide molecules is cetermmed by similar methods using GA? with the following settir.cs for DKA sequence comparison: GA? creation penalty of 5.0 and GA? exten¬sion penalty of C.3. The enzyme preparation of the invention is preferably de¬rived from a microorganism, preferably from a bacterium, an archea or a fungus, especially from a bacterium such as a bac¬terium belonging to Bacillus, preferably to a Bacillus strain which may be selected from the group consisting of the species Bacillus sp. and highly related Bacillus suedes in whicn ail species preferably are at least 951, even mere preferably at least 98%, homologous to Bacillus sp. 1633, Bacillus haiodurans or Bacillus sp. AAI12 based on aligned 165 rDNA sequences. These species are claimed based en phylogenic relation¬ships identifed from aligned 16S rDNA sequences from RD? (Ribosomal Database Project) (Bonne L. Maidak, Neils Larson, Michael J. McCaughey, Ross Overbeek, Gary J. Olsen, Karl Togel, James Blandy, and Carl R. Woese, Nucleic Acids Reasearch, 1994, Vol. 22, Nol7, p. 3485-3487, The Ribosomal Database Project;. The alignment was based on secondary structure. Calculation of sequence simularities were established using the "Full matrix calculation" with default settings of the neighbor joining method integrated in the ARB program package (Oliver Strunk and Wolfgang Ludwig, Technical University of Munich, Germany). Information derived from table II ate the basis for the clain for all family 5 mannanases frorr. the highly related Ba¬cillus species in which all species over 93% homologous to Ba¬cillus sp. 1633 are claimed. These include: 3acillus sporother-modurans, Bacillus acalcphilus, Bacillus pseudoalcalcphilus and Bacillus clausii. See Figure 1: Phylogenic tree generated from ARP program relating closest species to Bacillus sp. 1633. The 16S RNA is shown in SEQ ID NO:33. Table II: 163 nocsomai RNA homology :ndei: foe select Ea-cill'js species BaiSpor2 EaiAlcal BaiSpec3 BaiSpecS B.sp.lS32 BaiSpor2 92.75% 92.98% 92.41% 93.43% BaiAlcal 98.11% 94.55% 97.03% BaiSpec3 94.49% ■96.39% BaiSpec5 93.67% BaiSpor2 - B sporothermodurans, u49079 BaiAlcal = 5. B. aicalophilus, x7S436 BaiSpec3 = 5. pseudoalcalophilus, X76449 BaiSpecS = B clausii, x76440 Other useful family 5 mannanases are those derived from the highly related Bacillus species in which all species show more than 93% homology to Bacillus halodurans based or. aligned 16S sequences. These Bacillus species include; Spcrolactobacil-lus laevis, Bacillus agaradhaerens and Marinccoccus ha.loph.ilus. See Figure 2: Phylogenic tree generated from AR? program relat¬ing closest species to Bacillus halodurans. Table III: 16S ribosomal RNA homology index for selected ^ Bacillus species SplLaev3 Bai3pec6 BaiSpell MaoKalo2 NN SplLaev3 90.98% 87.96% 85.94% 91,32% BaiSpec6 91.63% 87.96% 99.46% BaiSpell 89.04% 92.04% 1 MaoHalo2 88.17% NN SplLaev3 = Sporolactobacillus laevis, D162 6 7 BaiSpec6 = B. halodurans, X76442 BaiSpell = B. agaradhaerens, X76445 MaoHalo2 = Marinccoccus halophilus, X62171 NN = donor organism of the invention (B. halodurans) Other useful family 5 mar.nanases are those derived frcm a strain selected from the group consisting cf the soe;ies Bacil¬lus agaradhaerens and highly related Bacillus species in which all species preferably are at lease 95cc, even more preferably at » least 98%, homologous to Bacillus sgaradhaerep.s, DSt-: 6721, based on aligned IBS rDNA sequences. Useful family 26 nannanases are for examcle those derived from the highly related Bacillus species in which ail species over 93% homologous to Bacillus sp. AA112 are claimed. These include; Bacillus spcrotherxoduzans, Bacillus acaiopnilus, Ba¬cillus pseudozlcalophiius and 3acillus clausii. See Figure 3; Phyiogenic tree aenerated from ARP program relating closest species to Bacillus sp. AAI 12. The 163 RNA is showr. ir. SEQ ID NO:34. Table IV: ISS ribosomal RNA homology index for selected Ba¬cillus species BaiSpor2 BaiAlcai BaiSpec3 BaiSpecS S.sp.AAI12 BaiSpor2 92.75% 92.98% 92.41% 32.24% BaiAlcai 98.11% 94.6 9% 3 7.2 8% BaiSpec3 94.49% 96.10% BaiSpec5 33.83% 3aiSpor2 = B sporothermodurans, u49079 3aiAlcal = B. B. alcalophilus, x76436 iaiSpec3 = B. pseudoalcalophilus, X76449 3aiSpec5 = B clausii, x76440 Other useful family 26 marmanases are those derived from a :train selected from the group consisting of the species Bacil-.us licheniformis and highly related Bacillus species in which 11 species preferably are at least 95%, even more preferably at east 98%, homologous tc Bacillus licheniformis based on aligned 6S rDNA sequences. Substantially homologous proteins and polypeptides are char¬acterized as having one or more amino acid substitutions, dele¬tions or additions. These changes are preferably of a minor nature, that is conservative ammo acid substitutions (see Table 2) and other substitutions that do not significantly affect the folding or activity of the protein or polypeptide; small dele-tions, typically of one to about 3C amir.o acids; and small amino- or carboxyl-terminal extensions, such as an ammo-terminal methionine residue, a small linker peptide of up to about 20-25 residues, or a small extension that facilitates purification (an affinity tag), such as a pcly-histidine tract, protein A (Nilsson et ai., EMEO J, j_:1075, 1955; Nilsson et a!., Methods Enzymol. 198;3, 1991. See, in general Ford et ai., Protein Expression and Purification 2_: 95-107, 1991, which is incorporated herein by reference. DMAs encoding affinity tags are available from commercial suppliers {e.g., Pharmacia Bio¬tech, Piscataway, NJ; New England Eiclabs, Beverly, MA). However, even though the changes described above preferably are of a minor nature, such changes may also be of a larger nature such as fusion of larger polypeptides of up to 300 amino acids or more both as amino- or carboxyl-terminal extensions to a Mannanase polypeptide of the invention. Table 1 Conservative amino acid substitutions Basic: arginine lysine histidine Acidic: glutamic acid aspartic acid Polar: glutamine asparagine Hydrophobic; leucine isoleucine valine Aromatic: phenylalanine tryptophan tyrosine Small: glycine alanine ssrine threonine methionine In addition to the 20 standard amino acids, non-standard amino acids {such as 4-hydroxyproIine, 6-ltf-methyl lysine, 2-amincisobutyric acid, isovaline and a-methyl serine) may be substitutec fcr amine acid residues of a polypeptide according to the invention. A limited number of non-conservative amino acids, amino acids that are net encoded by the genetic code, and unnatural amino acids may be substituted for amino acid resi¬dues. "Unnatural amino acids" have been modified after protein synthesis, and/cr have a chemical structure in their side chain{s) different from that of the standard amino acids. Unnatural amino acids can be chemically synthesized, or prefera¬bly, are commercially available, and include pipecolic acid, thiazolidine carboxylic acid, dehydroproline, 3- and 4-methylproline, and 3,3-dimethylproline. Essential amino acids in the mannanase polypeptides cf the present invention can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, Science 244: 1081-1065, 1989). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resul- tant mutant molecules are tested :or biclccica. activity (i.e mannanase activity) to identify a^ino acio residues that are critical to the activity of the molecule. See also, Hilton et al" J- Bic'^Cnenu 2^1:4699-4 708, 1996. The active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron dif¬fraction or phoccaffinity labeling, in conjunction with mutation of putative contact site ammo acias. See, for example, de Vos et al., Science 2J^:3C6-212, 1992; Smith et al. , J. Mel. Biol. 22_4_:899-9G4, 1992; Wlccaver et al . , FEBS Lett. 309:59-64, 1992. The identities of essential amino acids can also be inferred from analysis of homologies with polypeptides which are related to a polypeptide according to the invention. Multiple an-inc acio substitutions car. be made and tested us¬ing known methods of mutagenesis, recombination and/cr shuffling followed by a relevant screening procedure, such as those dis¬closed by Reidhaar-Olscr. and Sauer (Science 241:53-57, 1988), Bowie and Sauer (Proc. Natl. Acad. Sci. USA £6:2152-2156, 1989), W095/17413, or WO 95/22625. Briefly, these authors disclose methods for simultaneously randomizing two or more positions in a polypeptide, or recombination/shuffling of different mutations (W095/17413, W095/22625/, followed by selecting for functional a polypeptide, and then sequencing the mutagenized polypeptides to determine the spectrum of allowable substitutions at each posi¬tion. Other methods that can be used include phage display (e.g., Lowman et al., Ei^cher^ 30_: 10832-108 37, 1991; Ladner et al., U.S. Patent No. 5,223,409; Huse, WIPO Publication WO 92/06204) and region-directed mutagenesis (Derbyshire et al., 3ene 15:145, 1986; Ker et al., DNA 7:127, 1988) . ' Mutagenesis/shuffling methods as disclosed above can be com¬bined with high-throughput, automated screening methods to aezecz activity cf cloned, mutagemzed polypeptides in host cells. Mu-age-ized DMA molecules chat encode ac:ive polypeptides can be recovered frorr, the host cells and rapidly sequenced usina modern equipment. These methods allow the rapic ae:er^nat::or. of the importance cf individual ammo acid residues :r. ~ polypep¬tide of interest, ana can be applied to polypeptides cf unknown structure. Using the methods discussed above, one of crdinarv sstill in the art can identify ar.c/or prepare a variety of polypeptides that are substantially homologous to residues 23-340 cr 33-490 of SEQ ID NO:2; cr to residues 32-344 or 32-494 of SEQ ID NO: 6; or tc residues 32-362 cr32-5S6 of SEQ ID MO:10; or to residues 33-331 of SEQ ID N0:12; or to residues 166-488 or.22-483 cf SEQ' ID MO:14; cr to residues 63-369 cr 32-369 of SEQ ID NO:16; cr tc residues 1-305 of SEQ ID NO:18; cr to residues 1-132 cf SEQ ID NO:20; or to residues 29-320 of SEQ ID K0:22; cr to residues 29-188 of SEQ ID NO:24; or to residues 301-625 or 30-625 of SEQ ID -]0:26; or to residues 166-496 cr 38-496 of SEQ ID NO:28; or tc residues 26-361 of SEQ ID NO:30; cr to residues 593-903 or 23-303 of SEQ ID NO:32 and retain the mannanase activity of the jiId-type protein. The mannanase enzyme of the invention may, in addition to the enzyme core comprising the catalytically domain., also com¬prise a cellulose binding domain (CBD), the cellulose binding domain and enzyme core (the catalytically active domain) of the enzyme being operably linked. The cellulose binding domain (CBD) may exist as an integral part of the encoded enzyme, or a CBD from another origin may be introduced into the msr.nan de¬grading enzyme thus creating an enzyme hybrid. In this context, the tern "cellulose-binding domain" is intended to be under¬stood as defined by Peter Tomme et ai. '■'Cellulose-Bindirig Do-mains: Classification and Properties" in "Enzymatic Degradation cf Insoluble Carbohydrates", John K. Saddler and Michael K. Penner (Eds.), ACS Symposium Series, No. 613, 1996. This defi¬nition classifies more t.nan 120 cellulose-binding dorrains ;ntc 10 families ji-X), and demonstrates 'hat CBDs are found in various enzymes such as cellulases, xylanases, j.annar.ases, arabinofurancsidases, acetyl esterases and chitinases. CBCs have also beer, found in algae, e.g. the red alga Porphyra cur-pursa as a non-hydrolytic poiysaccharide-binding protein, see Tomme en al., cp.cit. However, most of the CBDs are from cellu-lases and xyiar.ases, CEDs are found at the N and C termini of proteins cr are internal. Enzyme hybrids are known in the art, see e.g. WC 90/CC60S and "WC 95/16782, and may be prepared by transforming into a host cell a DMA construct comprising at least a fragment of DMA encoding the cellulose-binding domain ligated, with or without a linker, to a DMA sequence encoding the mannan degrading enzyme and growing the host cell to ex¬press the fused gene. Enzyme hybrids may be described by the following formula: C3D - MR - X ■wherein CBD is the N-terminal or the C-termir.al region of an amino acid sequence corresponding to at least the cellulose-binding domain; MR is the middle region (the linker), and may be a bond, or a short linking group preferably cf from about 2 to about 100 carbon atoms, more preferably of from 2 to 40 carbon atoms; or is preferably from about 2 to to about 100 amino acids, more preferably cf from 2 to 4 0 amino acids; and X is an N-terminal or C-terminal region of the mannanase of the invention. SEQ 13 NO:4 discloses the amino acid sequence or an enzyme hybrid of a mannanase enzyme core and a CBD. Preferably, the mannanase enzyme of the present invention has its maximum catalytic activity at a pH of at least 7, mere preferably of at least 8, more preferably of at least 8.£f more preferably of at least 9, mere preferably of at least 9.5, mere preferably of at least 10, even rr.ore preferably of a- least 10.5, especially cf at least 11; and preferably the maximum activity of the enzyme is obtained at a temperature of at least 5 4C°C, more preferably of at least 50DC, even more preferably cf at least 55Dc. Preferably, the cleaning composition of the present inven¬tion provides, eg when uses for treating fabric during a washing cycle of a machine washing process, a washing solution having a pH typically between accut 3 and acout 10.5. Typically, such a washing solution is used at temperatures between about 2 0°C and about 95CC, preferably oatween about 20°C and about 6C°C, pref¬erably between about 2C°C and about 5C°C. ■ PROTEIN PRODUCTION: The proteins and polypeptides of the present invention, in¬cluding full-length proteins, fragments thereof and fusion proteins, can be produced in genetically engineered host ceils according to conventional techniques. Suitable host cells are those ceil types that car. be transformed or transfected with exogenous DNA and grown in culture, and include bacteria, fungal cells, and cultured higher eukaryotic cells. Bacterial cells, particularly cultured cells of gram-positive organisms, are preferred. Gram-positive cells from the genus of Bacillus are especially preferred, such as from, the group consisting of Bacillus subtiiis, Bacillus lentus. Bacillus clausii, Bacillus agaradhaerens, Bacillus Jbrevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus icoagulans, Bacillus circulars, Bacillus lautus, Bacillus thuringiensis. Bacillus licheniformis, and Bacillus sp., in particular Bacillus sp. 1633, Bacillus sp. AAI12, Bacillus clausii, Bacillus agaradhaerer.s and Bacillus lichsnz forms. In another preferred embodiment:, the host cell is 5 fungal cell. "Fungi" as used herein includes the phyla Ascorr.ycota, Basidiomycota, Chytridiomycota, and Zygomycots (as defined by Hawksworth et al. , In, Ainsworth and Bisby's Dictionary cf The Fungi, 8th edition, 199E, CAB International, University Press, Cambridge, UK} as well as the Oomycota (as cited in Hawksworth et al., 1955, supra, page 171} and all mitosporic fungi (Hawksworth et al., 1995, supra). Representative groups of Asccmycota include, e.g., Neurospcra, Eupenicillium (=Penicillium) , Emericella (=Aspergillus) , Eurotium (=Aspargillus) , and rhe true yeasts listed above. Examples of Easidiomyccta include mushrooms, rusts, and smuts. Representative groups of Chytridiomycota include, e.g., Allomyces, Blastociadialla, Coelomomyces, and aquatic fungi. Representative groups cf Oomycota include, e.g., Saprolegniomycetous aquatic fungi iwater molds) such 'as Achlya. Examples of mitosporic fungi include Aspergillus, Penicillium, Candida, and Alternaria. Representative groups of Zygomycota include, e.g., Rhizopus and Mucor. In yet another preferred embodiment, the fungal host cell is a filamentous fungal cell. "Filamentous fungi" include all filamentous forms of the subdivision Eumycota and Oomycota (as defined by Hawksworth et al., 1995, supra). In a more preferred embodiment, the filamentous fungal host cell is a cell of a species of, but not limited to, Acremonium, Aspergillus, Fusarium, Humicola, Muccr, Myceliophthora, Neurospora, Penicillium, Thielavia, Tolypocladium, and Trichoderma or a teleomorph. or synonym thereof. In particular, the cell may belong to a species of rrichodenna, preferably Trichoderma harzianum or Trichcderma reesei, or a species of Aspergillus, most preferably Aspergillus regeneration of the cell wall in a manner known per se. Suitable procedures for transformation of Aspergillus host ceils are described in E? 238 023 and Yeiton et al. , 1984, Proceeding of the National Academy of Sciences USA 81:1470-1474. A suitable method of transforming Fusarium species is described by Malardier et al., 1983, Gene 73:147-156 or in copending US Serial No. 08/269,44 9. Yeast may be transformed using the procedures described by Eecker and Gusrente, In Abelson, J.N. and Simon, M.I., editors, Guide to yeast Genetics and Molecular Bicloav, Methods in Enzymology, Volume 194, pp 182-187, Academic Press, Inc., New York; Ito et al., 1983, Journal of Bacteriology 153:163; and Hinnen et al., 1978, Proceedings cf the National Academy of Sciences USA 75:192C. Mammalian cells may be transformed by direct uptake using the calcium phosphate precipitation method of Graham and Van der Eb (1978, Virology 52:546). Techniques for manipulating cloned DNA molecules and intro¬ducing exogenous DNA into a variety of host cells are disclosed by Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989; Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley and Sons, Inc., NY, 198"; and "Bacillus subtilis and Other Gram-Positive Bacteria", Sonensheim et al., 1993, American Society, for Microbiology, Washington D.C., which ire incorporated herein by reference. In general, a DNA sequence encoding a mannanase cf the pres¬ent invention is operabiy linked to other genetic elements required for its expression, Generally including a transcripticr. promoter and terminattr within an expression vector. The vectc-will also commonly contain one or more selectable markers and one cr more origins cf replication, althougn those skilled in the art will recognize that within certain systems selectable markers may be provided on separate vectors, and replication of the exogenous DMA may be provided by integration into the host cell genome. Selection of promoters, terminators; selectable markers, vectors and ether elements is a matter of routine design within the level cf ordinary skill in the art. Many such elements are describee in the literature and are available through commercial supoiiers. To direct a polypeptide into the secretory pathway of a host cell, a secretory signal sequence (also known as a leader se- i ; quence, prepro sequence cr pre sequence) is provided in the expression vector. The secretory signal sequence may be that ox the Doiypeptide, or mav be derived from another secreted protein or synthesized de novo. Numerous suitable secretory signal sequences are known in the art and reference is made to "Bacillus subtilis and Other Gram-Positive Bacteria", Soner.sheim et al., 1993, American Society for Microbiology, Washington D.C.; and Cutting, S. M.(eds.) "Molecular Biological Methods for Bacillus", John Wiley and Sons, 1990, for further description of suitable secretory signal sequences especially fcr secretion in a Bacillus host cell. Tne secretory signal sequence is joined to the DNA sequence in the correct reading frame. Secretory signa_ sequences are commonly positioned 51 to the DMA sequence encod¬ing the polypeptide of interest, although certain•signal se¬quences may be positioned elsewhere in the DNA sequence cf interest (see, e.g., Welch et al., U.S. Patent No. 5,037,743; Holland et al., u.S. Patent No. 5,143,830). The expression vector cf the invention may be any expression vector that is conveniently subjected to recombinant DNA procedures, and the choice of vector will often depend on the host cell into which the vector it is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e. a vector which exists as an extrachromosomai entity, the replication of which is independent of chromosomal replication, e.g. a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host ceil genome and replicated together with the chromosome(si into which it has been integrated. Examples cf suitable promoters for use in filamentous fungus host cells are, e.g. the ADK3 promoter (McKnight et al., The EMBO J. 4, (1985), 2053 - 2099) or the tpiA promoter. Examples of other useful promoters are those derived from, the gene encoding Aspergillus cryzae TARA amylase, Rhizcmucor miekei aspartic proteinase, Aspergillus niger neutral a-amylase, Aspergillus niger acid stable a-amylase, Aspergillus niger or Aspergillus a.wamori glucoamylase (giuA) , Rhizomucor miehei lipase, Aspergillus cryzae alkaline protease, Aspergillus oryzae triose phosphate isomerase or Aspergillus nidulans acetamidase. Transformed or transfected host cells are cultured according to conventional procedures in a culture medium containing nutri¬ents and other components required for the growth cf the chosen host cells. A variety of suitable media, including defined media and complex media, are known in the art and generally include a carbon source, a nitrogen source, essential amino acids, vita¬mins and minerals. Media may also contain such components as growth factors or serum, as required. The growth medium will generally select for cells containing the exogenously added DNA by, for example, drug selection or deficiency in an essential nutrient which is complemented by the selectable marker carried en the expression vector cr co-trar.sf ected intc the host cell. PROTEIN ISOLATION 5 When the expressed reccmoir.ant polypeptide is secreted the polypeptide may be purified from the grow-!-, media. Preferably the expression host cells are removed from the media before purification of the polypeptide (e.g. by centrifugation!. When the expressed recombinant polypeptide rs nor secreted ' from the host ceil, the host cell are preferably disrupted and the polypeptide released into an aqueous "extract" which is the first stage of such purification techniques. Preferably the expression host cells are collected from the media before the cell disruption (e.g. by centrifugaticn). The cell disruption may be performed by conventional tech¬niques such as by iysczyme digestion or by forcing the cells through high pressure. See (Robert K. Scobes, Protein Purifica¬tion, Second edition, Springer-Verlag) for further description of such cell disruption techniques. Whether or not the expressed recombinant polypeptides (or chimeric polypeptides) is secreted or not it can be purified using fractionation and/or conventional purification methods and media. Ammonium sulfate precipitation and acid or chaotrope extrac¬tion may be used for fractionation of samples. Exemplary purifi¬cation steps may include hydroxyapatite, size exclusion, F?LC and reverse-phase high performance liquid chromatography. Suit¬able anion exchange media include derivatized dextrar.s, agarose, cellulose, polyacrylamide, specialty silicas, and the like. PEI, DEAE, QAE and Q derivatives are preferred, with DEAE Fast-Flow Sepharose [Pharmacia, Piscataway, NJ) being particularly pre¬ferred. Exemplary chromatographic media include those media derivacizeo with phenyl, butyl, c: cctyi groups, sue:, as Pnsr.yl-Sepharose FF (Pnarmacia. , Toycpearl butyl E5C (Tcsc Haas, Mont¬gomery-vine, FA;, Cctyi-Sepharose [Pharmacy] and-the like; or poiyacrylic resins, such as Amberchrom CG 71 (Toso Haas; and the like. Suitable solid supports include glass beads, silica-based resins, celiulosic resins, agarose beads, cross-linked agarose beads, polystyrene beads, cross-linked poiyacrylamide resins and the like that are insoluble under the conditions in which they are tc be usee. These supports may be modified with reactive groups that allow attachment of proteins by amino groups, car-boxyl groups, sulfhydryl groups, hydroxyl groups and/or carbohy¬drate moieties. Examples of coupling chemistries include cyano¬gen bromide activation, N-r.ycrcxysuccinimide activation, epoxide activation, sulfhydryl activation, hydrazide activation, and carboxyi and ammo derivatives fcr carbodiimide coupling chemis¬tries. These and other solid media are well known and widely used in the art., and are available from commercial suppliers. Selection of a particular method is a matter of routine de¬sign and is determined in part by the properties of the chosen support. See, for example, Affinity Chromatography: Principles S Methods, Pharmacia LKB Biotechnology, Uppsala, Sweden, 1988. Polypeptides of the invention or fragments thereof may also be orepared through chemical synthesis. Polypeptides of the invention may be monomers cr multimers; glycosylated or non-Glycosylated; pegylated or non-pegylated; and may or may not include an initial methionine amino acid residue. Based on the sequence information disclosed herein a full length DNA sequence encoding a mannanase of the invention and comprising the DNA sequence shown in SEQ ID No 1, at least the DNA sequence from position 94 to position 990, or, alterna¬tively, the DNA sequence from position 34 to position 1410, may be cloned. Likewise rr-y ce cloned a full length DNA sequence encoding a mannanase cf tr.e : r/enuo: and comprising the DMA sequence showr. ir. SEQ ID tic 5, at lease the DMA sequer.ee frci position 94 to position 1031, cr, alternatively, the DNA se-' quence iron position 94 to position 1482; and a full length DNA, sequence encoding a mannanase c: the invention ana comprising the DNA sequence shown in SEQ ID No 9, at least the DMA se¬quence from position 94 tc position 1086, or, alternatively, the DNA sequence from position 94 to position 17 61; and a full length DNA sequence encoding a mannanase cf the invention and comprising the DMA sequence snewr. in SEQ ID No 11, at least the DNA sequence from position 9" tc position 993; and a full length DNA sequence encoding a mannanase cf the invention and comprising the DNA. sequence shown in SEQ ID No 13, at least the DNA sequence from position 498 to Dosition 1464, cr, alterna¬tively, the DNA sequence from position 64 to position 1464; and a full length DNA sequence encoding a mannanase of the inven¬tion and comprising the- DNA. ssquer.ee shown in SEQ ID No IS, at least the DNA sequence from position 2G4 to position 1107, cr, alternatively, the DNA. sequence from position 76 to position 1107; and a DNA sequence partially encoding a mannanase of the invention and comprising the DMA sequence shown in SEQ ID No 17; and a DNA sequence partially encoding a mannanase of the invention and comprising the DNA. sequence shown in SEQ ID No 19; and £ full length DKA sequence encoding a mannanase of the invention and comprising the DMA sequence shown in SEQ ID No 21, at least the DNA. sequence from position 88 to position 960; and a DMA sequence partially encoding a mannanase.cf the inven¬tion and comprising the DNA. sequence shown in SEQ ID No 23; and a full length DMA sequence encoding a mannanase cf the inven¬tion and comprising the DNA. sequence shown in SEQ ID No 25, at least the DNA sequence from position 904 to position 1875, or, alternatively, me DUA sequence from position 88 to position 2445; and a full length DMA sequence encoding a mannanase cf the invention end comprising the D11A sequence shown an SE^ ID No 27, at ieest the DNA sequence from position 493 to position 1488, or, alternatively, the DNA sequence from position 112 to position 1488; and a full length DNA sequence encoding a man¬nanase of the invention and comprising the DNA sequence shewn in SEQ ID No 29, at leest the DtiA sequence from position ~9 to position 2083; and a full length DNA sequence encoding a man¬nanase of the invention and comprising the DNA sequence shown in SEQ ID Ho 31, at least the DNA sequenae from position 1~7$ to position 2"?09, or, alternatively, the DKA sequence from position 6~ to position 2709. Cloning is performed by standard procedures known m the = art such as by, ■ preparing a genomic library from a Bacillus strain, espe¬ cially a strain selected from B. sp. 1633, B. sp. AAI12, B. sp. AA349. Bacillus agaradhaarens, Bacillus halodurans, Ba¬ cillus clausii and Bacillus licheniformis, or from a fungal strain, especially the strain Humicola insolens; ■plating such a library on suitable substrate plates; ■ identifying a clone comprising a polynucleotide sequence of the invention by standard hybridization techniques using a probe based on any of the sequences SEQ ID Nos. 1, 5, 9, ±1, 13, 15, 17, 19, 21, 23, 25, 27, 29 or 31; or by ■ identifying a clone from said genomic library by an Inverse PCR strategy using primers based on sequence information from SEQ ID No 1, 5, 9, 11, 13, 15, 17, 19, 21, 23, 25, 27, 29 or 31. Reference is made to M.J. MCPherscn et al. ("PCR A prac¬tical approach" Information Press Ltd, Oxford England) for further details relating to Inverse PCR. =asea on _r.e s-qience information cis:icjed herein. ! SE2 ID NOS l, 2, ~, e, 9, :o, ::, 12, 13, u, 15, ie, 17, :S, 19, 20, 21, 22, 22, 24, 25, 26, 27, 23, 29, 3C, 31, 32) is it rou¬tine work for a person skilled in the art to isolate homologous 5 polynucleotide sequences encoding homologous mannanase of the invention by a similar strategy using genomic libraries from related microbial organisms, in particular from genomic librar¬ies from other strains of the genus Bacillus such-as aikaio-philic species of Bacillus sp., or from fungal strains such as ■ species of Humiccla . Alternatively, the DMA encoding the mar.nan or galactoman-nan-degrading enzyme of the invention may, in accordance with well-known procedures, conveniently be cloned from a suitable source, such as any cf the above mentioned organises, by use of synthetic oligonucleotide probes prepared on the basis cf the W.A sequence obtainable from, the plasmid present ar.y of the strains Escherichia cclx DSM 12191, DSM 12160, DSM 12432, DSM 12441, DSM 99S4, DSM 12432, DSM 12436, DSM 12846,.DSM 12847, DSM 12848, DSM 12849, DSM 12350, DSM 12851 and DSM 12852. Accordingly, the polynucleotide molecule of the invention may be isolated from any of Escherichia coli, DSM 12197, DSM 12180, DSM 12433, DSM 12441, DSM 9984, DSM 12432, DSM 12436, DSM 12846, DSM 12847, DSM 12848, DSM 12849, DSM 12850, DSM 12851 and DSM 12852, in which the plasmid obtained by cloning such as described above is deposited. Also, the present inven¬tion relates to an isolated substantially pure biological cul¬ture of any of the strains Escherichi3 coli, DSM 12197, DSM 12180, DSM 12433, DSM 12441, DSM 9984, DSM 12432,.DSM 12436, DSM 12846, DSM 12847, DSM 12848, DSM 12849, DSM 12850, DSM 12851 and DSM 12352. In the present context, the term "enzyme preparation" is intended to mean either a conventional enzymatic fermentation product, possibly isolated ar^ purified, from a single specie; of a microorganism, such preparation usually comprising a number of different enzymatic activities; cr a fixture of mcnoccmconent enzyir.es, preferably enzymes derived from bacterial cr fungal species by using conventional recombinant techniques, wr.ich enzymes have been fermented and possibly isolated and purified separately and which may originate frcm different species, preferably fungal or bacterial species; or the fermentation product of a microorganism which acts as a host cell fcr expression of a recombinant mannanase, but which microorganism simultaneously produces other enzymes, e.g. pectin degrading enzymes, proteases, or cellulases, being naturally occurring fermentation products of the microorganism, i.e. the enzyme complex conventionally produced by the corresponding naturally occurring microorganism. The mannanase preparation of the invention may further comprise one or more enzymes selected from the group consisting of proteases, cellulases (endo-p-1, 4-giucanases; , (3-glucanases (endo-p-1, 3(4) -glucana.sesi , lipases, cutinases, peroxidases, laccases, amylases, glucoamyiases, pectinases, reductases, oxidases, phenoioxidases, iignir.ases, pullulanases, hemiceilulases, pectate lyases, xyloglucanases, xylanases, pectin acetyl esterases, rhamnogalacturonan acetyl esterases, polygalacturonases, rhar.nogalacturonases, pectin lyases, pectin methylesterases, ceilobiohydrolases, transglutaminases; or mixtures thereof. In a preferred embodiment, one or more or all enzymes in the preparation is produced by using recombinant techniques, i.e. the enzyme(s) is/are mono-component enzyme!s) rfhich is/are mixed with the other enzyme(s) to form an enzyme ^reparation with the desired enzyme blend. In another aspect, the present invention also relates to a method of producing the enzyme preparation of the invention, the method comprising cul::nng a microorganism, eg a wild-type strain, capable or producing the mannanase under conditions permitting the production o: the enzyme, and recovering the enzyme from the culture. Culturing may be carried out using conventional fermentation techniques, e.g. culturing in shake flasks or fermentors with agitation to ensure sufficient aeration on a growth medium inducing production of the mannanase enzyme. The growth medium may contain a conventional K1-source .such as peptone, yeast extract or casamino acids, a reduced amount of a conventional C-source such as dextrose or sucrose, and an inducer such as guar gum cr locust bean gum. The recovery may be carried out using conventional techniques, e.g. separation c: bio-mass and supernatant by cer.trifugetion or filtration, recovery c; the supernatant or disruption of cells if the enzyme cf interest is intracellular, perhaps followed by further purification as described in EP 0 406 314 or by crystallization as described in WO 9T/15660. Examples cf useful bacteria producing the enzyme or the enzyme preparation of the invention are Gram positive bacteria, preferably from the Bacillus/Lactobacillus subdivision, preferably a strain from the genus Bacillus, more preferably a strain of Bacillus sp. In yet another aspect, the present invention relates to an isolated mannanase having the properties described above and which is free from homologous impurities, and is produced using conventional recombinant techniques. IMMUNOLOGICAL CROSS-REACTIVITY Polyclonal antibodies to be used in determining immunological cross-reactivity may be prepared by use of a purified mannanase enzyme. More specifically, antiserum against Use in the detergent industry In further asoects, the present invention relates to a deter¬gent composition comprising the mannanase or mannanase prepara¬tion of the invention, to a process for machine treatment of fabrics comprising treating fabric during a washing cycle cf a machine washing process with a washing solution containing the mannanase or mannanase preparation of the invention, and to cieanina compositions, including laundry, dishwashing, hard surface cleaner, personal cleansing and oral/aental composi¬tions, comprising a mannanase and optionally another enzyme selected among cellulases, amylases, pectin degrading enzymes and xyloglucanases and providing superior cleaning performance, i.e. superior seain removal, dingy cleaning and whiteness main¬tenance . such soilings or spots. The cleaning compositions cf the invention must; contain at least one additional detergent component. The crecise nature or these additional components, and levels of incorporation thereof will depend on the physical form of the composition, and the nature cf the cleaning operation for which it is to be usee. The cleaning compositions cf the present invention crefera-bly further comprise a detergent inaredient selected from e selected surfactant, another enzyme, a builder and/or a bleach system. The cleaning compositions according to the invention can be liquid, paste, gels, bars, tablets, spray, foam, powder or granular. Granular compositions can also be in "compact" form and the liquid compositions car. also be in a "concentrated" form. The compositions of the invention may for example, be formulated as hand and machine dishwashing compositions, hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics, rinse added fabric softener compositions, and compositions for use in gen¬eral household hard surface cleaning operations. Compositions containing such carbchydrases can also be formulated as sensiti¬zation products, contact lens cleansers and health and beauty rare products such as oral/dental care and personal cleaning compositions. When formulated as compositions for use in manual dishwash¬ing methods the compositions of the invention preferably contain a surfactant and preferably otr.er detergent compounds selected from organic polymeric compounds, suds enhancing agents, croup, il metal ions, solvents, hydrctropes and additional enzymes. When formulated as compositions suitable for use in a z laundry machine washing method, the compositions of the inven¬tion preferably contain bctn a surfactant and a builder compound and additionally one or more detergent components preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersar.es, lime-soap dispersants, soil suspension and ar.ti-redeposition agents and corrosion inhibitors. Laundry compositions can also contain softening agents, as additional detergent components. Such compositions containing carbohydrase can provide fabric clean¬ing, stain removal, whiteness maintenance, softening, colour , appearance, dye transfer inhibition and sanitization when formu¬lated as laundry detergent compositions. The compositions of the invention can also be used as detergent additive products in solid or liquid form. Such addi¬tive products are intended to supplement or boost the perform¬ance of conventional detergent compositions and car. be added at any stage of the cleaning process. If needed the density of the laundry detergent compositions herein ranges from 400 to 1200 g/litre, preferably 500 to 950 g/litre of composition measured at 20°C. The "compact" form of the compositions herein is best re¬flected by density and, in terms of composition, by the amount of inorganic filler salt; inorganic filler salts are conven¬tional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are pres¬ent in substantial amounts, typically 17-35% by weight of the total composition. In the cempact compositions, the filler salt is present in amounts not exceeding 15% of the total composi- tion, preferably net exceeding 10%, mCst preferably nc: exceeci-ing 5% by weigh- of the composition. Tne inorganic filler salts, sucn as meant in the present, compositions are selected from the alkali and alkaline-earth-metal salts of sulphates and chlo¬rides. A preferred filler salt is sodium sulphate. Liquid detergent compositions according tc the present invention can also be m a "concentrated form", in such case, the liquid detergent compositions according the present inven¬tion will contain a lower amount of water, compared to conven¬tional liquid detergents. Typically the water content of the concentrated liquid detergent is preferably less than 40%, more preferably less than 3C%, most preferably less than 20% by weight of the detergent composition. The cleaning or detergent compositions according to the oresent invention comprise a surfactant system, wherein the surfactant can be selected from nonionic and/or anionic and/or rationic and/or amphoiytic and/or zwittericnic and/or semi-polar surfactants. The surfactant is typically present at a level from 0.1% .o 60% by weight. The surfactant is preferably formulated to be :ompatible with enzyme hybrid and enzyme components present in he composition. In liquid or gel compositions the surfactant is ost preferably formulated in such a way that it promotes, or at east does not degrade, the stability of any enzyme hybrid or nzyme in these compositions. Suitable systems for use according to the present nvention comprise as a surfactant one or more of the nonionic and/or anionic surfactants described herein. Polyethylene, polypropylene, and pciybutylene cxide conder.-sates of alky! phenols are suitable for use as the nonionic surfactant of the surfactant systems cf the present invention, with the polyethylene oxide condensates being | preferred. These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 3 to about 14 carbon atoms, in either a straight chain or branched-chain con¬figuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to from about 2 to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkyl phenol. Commercially available nonionic surfactants of this type include Igepal™ C0-630, marketed by the GA.F Corporation; and Triton™ X-45, K-114, X-100 and X-102, all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol slkoxylates (e.g., alkyl phenol ethoxylates). The condensation products of primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most preferably from 2 to 5 moles of ethylene oxide per mole of alcohol are present in said condensation pro¬ducts. Examples cf commercially available nonionic surfactants of this type include Tergitol™ 15-S-9 (The condensation product : 5 mcles of ethylene oxide) marketed by Koechst. Preferred range of HLE in these products is from 8-11 and most preferred from 8-10. Also useful as the nonionic surfactant of the surfactant systems of the present invention are alkylpolysaccharides disclosed in US 4,565,647, having a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units. Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties (optionally the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside). The intersaccharide bonds can be, e.g., between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- alkylphenyl, hydroxyalky1, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, pre-ferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpoLyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1-position). The additional glycosyl units can then be attached between their 1-position and the preceding glycosyl units 2-, 3-, 4-, and/or 6-position, preferably predominantly the 2-position. The condensation products of ethylene oxide with a hydrophobic base formed by the condensation of propylene oxide } with propylene glycol are also suitable for use as the additional ncnionic surfactant systems of the present invention. The hydrophobic portion of these compounds will preferably have a molecular weight from about 1500 to about 1800 and will exhibit water insolubility. The addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% o£ the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain of the commercially available Pluronic™ surfactants, marketed by BASF. Also suitable for use as the nonionic surfactant cf the nonionic surfacianc system of the present invention, are the condensation products of ethylene oxide with the product resulting from the reaction of propylene cxide and 5 ethylenediamine. The hydrophobic moiety of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000. This hydrophobic moiety is condensed with ethylene cxide to the extent that the condensation product contains from about 40% to about 80% by weight of polycxyethylene and has a molecular weight of from about 5,000 to about 11.00C. Examples of this type cf nonionic surfactant include certain of the commercially available Tetronic™ compounds, marketed by BASF. Preferred for use as the nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethyleneoxide, alkylpolysaccharides, and mixtures hereof. Most preferred are CB-C, alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and Ce-Cia alcchol ethoxylates (preferably C10 avg.) having from 2 to 10 ethoxy groups, and mixtures thereof. Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula wherein R1 is K, or R: is CiM hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl or a mixture thereof, R2 is Cs.3l hydrocarbyl, and S is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at leas- 3 hydroxy Is directly connected to the chain, or ar. alkoxylated derivative thereof. Preferably, R: is methyl, R: is straight C1W5 alkyl cr C,e_ie alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived frcm a reducing sugar such as glucose, fructose, maltose or lactose, in a reductive amination reaction. Highly preferred anionic surfactants include alkyl alkoxylated sulfate surfactants. Examples hereof are water soluble salts or acids of the formula R0(A)mS03M wherein R is ar. msubstituted C,0-C-24 alkyl or hydroxyalkyl group having a C.0-C,, ilkyl component, preferably a C^-C^ alkyl or hydro-xyalkyl, more preferably C1;-C.S alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about □, more preferably between about 0.5 and about 3, and M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium cation. Alkyl echoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and those derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary surfactants are C:2-C1S alkyl polyethoxylate (1.0) sulfate (Cia-C1BE (1. 0) M) , C,rC,9 alkyl polyethoxylate 12.25) sulfate (C12-ClB (2.25>M, and C,a-Cia alkyl polyethoxylate (3.0) sulfate (C1S-C1BE Suitable anionic surfactants to be used are alkyl ester sulfonate surfactants including linear esters of CB-C2a carboxylic acids (i.e., fatty acids) which are sulfonated with gaseous S0: according to "The Journal of the American Oil Chemists Society", 52 (1375), pp. 323-329. Suitable starung materials would include natural fatty substances as derived from tallow, palm oil, etc. The preferred alkyi ester sulfonate surfactant, especially for laundry applications, comprise alkyi ester sulfonate surfactants of the structural formula: wherein R3 is a Ch-C2a hydrocarbyl, preferably an alkyi, or combination thereof, Ra is a C^-C^ hydrocarbyl, preferably an alkyi, or combination thereof, and M is a cation which forms a water soluble salt with the alkyi ester sulfonate. Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethonolamine, and triethanolamine. Preferably, R3 is C.i0-Ci4 alkyi, and R1 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonates wherein R3 is C10-C16 alkyi. Other suitable anionic surfactants include the alkyi sulfate surfactants which are water soluble salts or acids cf the formula ROS03M wherein R preferably is a Cl0-CS4 hydrocarbyl, preferably an alkyi or hydroxyalkyl having a C-_0-C2G alkyi com¬ponent, more preferably a Cis-Cia alkyi or hydroxyalkyl, ana M is H or a cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or ammonium or substituted ammonium (e.g. methyl-, dimethyl-, and trimethyl ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and quaternary ammonium est ions derived from alkylamines such as echylamine, diethyla^ine, triethylamine, and mixtures thereof, and the like!. Tvricailv alkyl chains of C12-C:e are preferred for lower wash temperatures (e.g. below about 50°C) and C.6-C:a alkyl chains are preferred for higher wash temperatures (e.g. above about 50°C). Other anionic surfactants useful for detersive purposes can also be included in the laundry detergent compositions of the present invention. Theses can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono- di- and triethanolamine salts) of soap, Ca-C22 primary or secondary alkanesulfonates, Ca-C-j, olefinsulfcnates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No. 1,082,179, Ca-C2, alkyipolyglycolethersulfates (containing up to 10 moles of ethylene oxide]; alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates, alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C.--C18 monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated Cs-C2 diesters), acyl sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsulfated compounds being described below), branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as those of the formula RO(CHaCH3O)k-CHiC00-M+ wherein R is a Ce~C22 alkyl, k is an integer from 1 to 10, and M is a soluble salt forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil. Alkylber.zene sulfonates are highly preferred. Especially preferred are linear (straight-chain) alky! benzene sulfonates (LAS) wherein the alkyl group Dreferably contains from 10 to 18 f ■> carbon atoms. Further examples are described in "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perrry and Berchi . A variety of such surfactants are also generally disclosed in u"S 3,929,678, (Column 23, line 53 through Column 29, line 23, herein incorporated by reference). When included therein., the laundry detergent compositions of the present invention typically comprise from abcu.- l% to about 40%, preferably from about 3% tc about 2C% by weight of such anionic surfactants. The cleaning or laundry detergent compositions of the present invention may also contain cationic, amphclytic, zwitterionic, and sew.i-pclar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein. Cationic detersive surfactants suitable for use in the laundry detergent compositions of* the present invention are those having one long-chain hydrocarbyl group. Examples of such cationic surfactants include the ammonium surfactants such as alkyltrimethylammonium halogenides, and those surfactants having the formula: has a value from 2 Co 5, and X is an anion. Not: more than one of R,, R3 or R4 should be benzyl. The preferred alkyl chair, length for R± is C.,-C1S, particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or 0X0 alcohols synthesis. Preferred groups for R2R; and R4 are methyl and hydroxyechyl groups and the anion X may be selected from halide, methosulphate, acetate and phosphate ions. Examples of suitable quaternary ammonium compounds of formulae (i) for use herein are: coconut: trimechyl ammonium chloride or bromide; coconut methyl dihydroxyethyl ammonium, chloride or bromide; decyl triethyl ammonium chloride,- decyl dimethyl hydroxyethyi ammonium chloride or brcmide; ci2-is dimethyl hydroxyethyi ammonium chloride or bromide; coconut dimethyl hydroxyethyi ammonium chloride or bromide; myristyl trimethyi ammonium methyl sulphate; lauryl dimethyl benzyl ammonium chloride or bromide,- lauryl dimethyl (ethenoxy). ammonium chloride or brcmide; choline esters (compounds of formula (i) wherein Rx is di-alkyl imidazolines [compounds of formula fi)]. Other cationic surfactants useful herein are also described in US 4,223,044 and in EF 00G 224. When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 25%, preferably from about 1% to about 8% by weight of such cationic surfactants. Ampholycic surfactants are also suitable for use in the laundry detergent compositions of the present invention. These surfactants csu be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight- or branched-chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water-solubilizing group, e.g. carbcxy, sulfonate, sulfate. See US 3,929,678 (column 19, lines 18-35) for examples of ampholytic surfactants. included tnerein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such ampholytic surfactants. Zwitterionic surfactants are also suitable for use in laundry detergent compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphor.ium or tertiary sulfonium compounds. See US 3,929,678 (column 19, line 38 through column 22, line 48) for examples of zwitterionic surfactants. When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight cf such zwitterionic surfactants. Semi-polar ncnionic surfactants are a special category of. nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; watersoluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and 5 hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms. Semi-polar ncnionic detergent surfactants include the amine oxide surfactants having the formula: ' wherein R- is an alkyl, hydroxyalkyl, or alkyl ?n=r;,-: urouc cr mixtures thereof containing fr;~i about 8 to about 22 carbon, atoms; R4 is an alkylene or hydroxyalkyieue group containing from about: 2 tc about 3 carbon atoms or mixtures thereof; x is from 0 to about 3: an: each Ru is an alkyl cr hydroxyalkyl group containing from about '_ oo about .; carbon a COTS or a polyethylene oxide group cor.tairiinc from, about i cc an cut 3 ethylene oxide groups. The R: groups can he atcacned tc each eerier, e.g., through an oxygen cr nitrogen a::r., cc fcrrr. a ring structure. These amine oxide surfactants in particular include ~-_-~ie alkyl dimethyl amine oxides and Cs-C. alkcxy ethyl dihydroxy ethyl amine cxides. When included therein, the laundry detergent coicpos ioi ens of the present invention typically comprise from 0.2% to aoout 15%, preferably from about 1% cc about 10% by weight cr such semi-polar nor.ionic surfactants . Builder system The comoositiens according to the present invention may further comprise a builder system. Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, poiycarboxyiates and fatty acids, materials such as ethyienediamine tetraacetate, metal icr. seauestrants such as aminopclyphosphonates, particularly ethyienediamine tetramethylene phosp'nonic acid and diethylene triamine pentamethyienephosphonic acid. Though less preferred for obvious environmental reasons, phosphate builders car. also be used herein. Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated alumincsilicsce material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MA?. Another suitable inorganic builder material is layered silicate, e.g. SKS-6 (Hoechst}. SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na:Si:Os) . Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and enher derivatives thereof as disclosed in Belgian Patent Ncs. 831,363, 821,369 and 821,370. Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic acid, malonic acid, (ethyienedioxy! diacetic acid, maleic acid, diglycollic acid, tartaric acid, tartronic acid and furnaric acid, as well as the ether carboxylates described in German Offenle-enschrift 2,446,686, and 2,446,487, US 3,935,257 and the sulfinyl carboxylates described in Belgian Patent No. 840,623. Polycarboxylates containing three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconatzes as well as succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1,379,241, laccoxysuccinates described in Netherlands Application 7205873, and the oxypolycarboxylate materials such as 2-oxa-l,l,3-propane tricarboxylates described in British Patent No. 1,387,447. Polycarboxylates containing four carboxy groups include oxydisuccinates disclosed in Eritish Patent No. 1,261,829, 1,1,2,2,-ethane tetracarboxylates, 1,1,3,3-propane tetracarboxylaces containing sulfo substituents include the sulfosuccinate derivatives disclosed in British Patent Nos. 1,398,421 and 1,398,422 and in US 3,936,448, and the sulfonated pyrciysed citrates described in British Patent No. 1,082,179, while polycarboxylates containing phosphcne substituents are disclosed in British Patent No. 1,439,000. Alicyclic and heterocyclic polycarboxylates include ■ cyclopentane-cis,cis-cis-tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-furan - cis, cis, ;;s-tetracarboxylates, 2,5-tetrahydro-furan-cis, discarboxylaces, 2,2,5,5, -tetrahydrofuran - tetracarboxylates , 1,2,3,4,5, S-hexane - hexacarboxylates and carboxymethyl derivatives of pclvhyaric alcohols such as sorbitol, mann.itol and xylitol. Aromatic polycarboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent Kc. 1,425,343. Of the above, the preferred polycarboxylates are hydroxy-carboxylates containing up to three carboxy groups per molecule, more particularly citrates. Preferred builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a'layered i silicate (SKS-6), and a water-soluble carboxylate chelating agent such as citric acid. A suitable chelant for inclusion in the detergent corr.posi-ions in accordance with the invention is ethylenediamine-R,Nl-disuccinic acid (EDDS) or the alkali metal, alkaline earth metal, ammonium, or substituted ammonium salts thereof, or mixtures thereof. Preferred EDDS compounds are the free acid form and the sodium or magnesium salt thereof. Examples cf sucr. preferred sodium salts of EDDS include Na3EDDS and Na,EDDS. Examples of such preferred magnesium salts cf EDDS include MgEDDS and Mg2EDDS. The magnesium salts are the most preferred for inclusion in compositions in. accordance with the invention. Preferred builder systems include a mixture of a water-insoluble aiurr.mosilicate builder such as zeolite A, and a water soluble carboxyiate chelating agent such as citric acid. Other builder materials that can form part of the builder J. system for use in granular compositions include inorganic materials such as alkali metal carbonates, bicarbonates, silicates, and organic materials such, as the organic phosphonates, amino polyalkylene phosphonates and amino polycarboxylates. ' Other suitable water-soluble organic salts are the horao-or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carbcxyl radicals separated form each other by not more than two carbon atoms. I Polymers cf this type are disclosed in GB-A-1,596,75€. Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of frcra 20,000 to 70,000, especially about 40,000. Detergency builder salts are normally included in amounts of from 5% zo 80% by weight of the composition. Preferred levels of builder for iiouid detergents are from. 5% to 30%. Kannanase is incorporated into the cleaning or detergent compositions in accordance with the invention preferably at a level of from O.0C01% tc 21, more preferably from 0.0005% to 0.5%, most preferred from 0.001% to 0.1% pure enzyme by weight of the composition. The cleaning compositions of the present invention may further comprise as an essential element a carbohydrase selected from the group consisting of cellulases, amylases, pectin ae-grading enzymes and xylogiucanases. Preferably, the cleaning compositions of the present lr.venncn will comprise a ms.nnanase, an amylase ana another tiosccurir.g-type of enzyme seieoueo from the group consisting of celluloses, pectin degradir.c er.:\r.es 2nd xyloglucanases. 5 The cellulases usable in the present invention include both bacterial or fungal cellulases. Preferably, they will have a pH optimum of between 5 and 12 and a specific activity above 50 CEVU/mg (Cellulose Viscosity Unit). Suitable cellulases are disclosed in U.S. Patent 4,435,307, J6I0783S4 and'W096/C26£3 which discloses fungal cellulase produced from Humicola ir.so-lens, Trichoderma, Thislavia and Spcrocrichuw, respectively. Ep 739 982 describes cellulases isolated from novel Bacillus soe-cies. Suitable cellulases are also disclosed in GE-A-2075025; GB-A-2095275; DE-OS-22 47 832 and W095/26398. Examples of such cellulases are cellulases produced by a strain of Humicola insclens (Humicola grisaa var, thezn\zidea) , particularly the strain Humicola insclens, D3.M 1800. Other suitable cellulases are cellulases originated from Humicola insolens having a ir.olecular weight of about 50kD, ■ an isoelectric point of 5.5 and containing 415 amino acids; and a ~43kD endo-beta-1,4-glucanase derived from Humicola insoler.s, DSM 13C3; a preferred cellulase has the amino acid sequence disclosed in PCX Patent Application Ho. WO 91/17243. Also suitable cellulases are the EGIII cellulases from Trichoderma 1 ongibrachia turn described in WO94/21801. Especially suitable cellulases are the cellulases having color care benefits. Examples of such cellulases are the cellulases described in W096/29397, EP-A-0495257, WO 91/17243, /J091/17244 and WO91/21S01. Other suitable cellulases for fabric care and/or cleaning properties are described in W096/34Q92, ^096/17994 and W095/24471. Said cellulases are normally incorporated in the detergent composition at levels from 0.0001% to 2% of pure enzyme by weight of the deterge::- composition. Preferred celluiases for the purpose cf the present inven¬tion are alkaline cslluiases, i.e. enzyme having at least 25%, more preferably a: least 40% of their maximum activity at a pH ranging from 7 tc 12. More preferred celluiases are enzymes having "heir maximum activity at a PK ranging from 7 tc 12. A preferred alkaline cellulase is the cellulase sold under the tradename Carezyme® by Novo Ncrdisk A/S. Amylases fa sr.d/cr £) car. be included for removal of carbc-' hydrate-based stains. WO94/02597, Novo Nordisk A/S published February 03, 1994, describes cleaning compositions which incor¬porate mutant amylases. See also WO95/10S03, Novo Mcrdisk A/S, published April 20, 1995. Other amylases known for use in clean¬ing compositions induce both a- and p-amylases. 'a-Anyiases are known in the art and include those disclosed in US Pat. no. 5,003,257; E? 252,666; WO/91/00353; FR 2,676,456; E? 285,123; EP 525,610; E? 366,341; and British Patent specification no. 1,296,839 (Novo). Other suitable amylases are stability-enhanced amylases described in W094/18314, published August 18, 1994 and WO96/05295, Ger.enccr, published February 22, 1996 and amylase variants having additional modification in the immediate parent available from Hove Nordisk A/S, disclosed in WO 95/10603, published April 95. Also suitable are amylases described in E? 277 216, W095/26397 and W096/23872 (all by Ncvc Nordisk). Examples of commercial a-amyiases products are Purafect Ox Am® from Genenccr and Termamyl®, Ban® , Fungaroyl® and Duramyl®, all available from Novo Nordisk A/3 Denmark. W095/26397 de¬scribes other suitable amylases : a-amylases characterised by having a specific activity at least 25% higher than the specific activity of Termamyl® at a temperature range of 25°C to 55°C and at a pH value in the range of S to 10, measured by the Phadebas a-amyiase activity assay. Suitable are variants of the above enzymes, descrioed ir. WOS6/233~3 (Move Nordisk) . Cther amy-iolytic enzymes with improved properties witn respect to the activity level and the combination of thermostability and a higher activity level are described in W095/35362. Preferred amylases fcr the purpose of the present invention are the amylases sold under the tradename Termamyl, Duramyl and Maxamyi and or the a-amyiase variant demonstrating increased thermostability disclosed as SEQ ID J-;o. 2 in WOS6/23S73. Preferred amylases for specific applications are alkaline amylases, ie enzymes having an enzymatic activity of at least 10%, preferably at least 25%, mere preferably at least 40% of their maximum activity at a pH ranging frarr. 7 to 12. More pre¬ferred amylases are enzymes having their maximum activity at a j pH ranging from 7 to 12. The amylolytic enzymes are incorporated in the detergent compositions of the present invention a level of from 0.0001% to 2%, preferably from 0.00018% to C.06%, more preferably from. 0.00024% to C. 04B% pure enzyme by weight of the composition. The term "pectin degrading enzyme" is intended to encompass arabinanase {EC 3.2.1.99), galactanases (EC 3.2.1.8S), polyga¬lacturonase (EC 3.2.1.15) exo-poLygalacturoaase (EC 2.2.1.67), exo-poiy-alpha-galaczuromdase (EC 3.2.1.32), pectin lyase (EC 4.2.2.10), pectin esterase (EC 3.2.1.11), pectate lyase (EC 4.2.2.2), exc-polygalacturonate lyase (EC 4.2.2.9)and hemicellu-lases such as endc-I,3-P-xylosfdase (EC 3.2.1.32), xyian-1, 4-(3-xylosidase (EC 3.2.1-37)and a-L-arabinofuranosidase {EC 3.2.1.55). The pectin degrading enzymes are natural mixtures of the above mentioned enzymatic activities. Pectin enzymes there¬fore include the pectin methylesterases which hydrclyse the pectin methyl ester linkages, polygalacturonases which cleave the giycosidic bonds between galacturonic acid molecules, and the pectin cranselimmasss or lyases which act or, t.te peccic acids to bring about ncn-nydroiytic cleavage of a-;-»-J glycosi¬de linkages to form unsaturated derivatives of galscturonic acid. Pectin' degrading enzymes are incorporated into the composi¬tions in accordance with the invention preferably at a level of from 0.0001 I tc 2 I, more preferably from G.0005% to 0.5%, most preferred from 0.001 % to C.l % pure enzyme by weight of the total composition. i Preferred pectin degrading enzymes for specific apciica-tions are alkaline pectin degrading enzymes, ie enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40^ c: their maxim-urn activity at a pH ranging from 7 to 12. More preferred pectin degrading enzymes are enzymes having their maximum activity at a pH ranging from 7 to 12. Alkaline pectin degrading enzymes are produced by alkalo-philic microorganisms e.g. bacterial, fungal and yeast microor¬ganisms such as Bacillus species. Preferred microorganisms are Bacillus firmus, Bacillus circulans and Bacillus subtilis as described m J? 56131376 and JP 55068393. Alkaline pectin decom¬posing enzymes include galacturan-1,4-a-galacturonase (EC 3.2-1.67), pciy-gaiacturonase activities [EC 3.2.1.15, pectin esterase (EC 3.1.1.11), pectate lyase (EC 4.2.2.2} and their iso enzymes and they can be produced by the Erwinia species. Pre¬ferred are E. chrvsanthami, E. carotovora, E. amylovora, E. herbicola, E. dissclvans as described in JP 59066538, J? 63042988 and in World J. Microbiol. Microbiotechncl. (S, 2, 115-120) 1992. Said alkaline pectin enzymes can also be produced by Bacillus species as disclosed in J? 730Q6557 and Agr. Biol. :hem. (1972;, 26(2) 265-93. The term xyloglucanase encompasses the family of enzymes described bv Vincken and Vcragen at Wageningen University [Vir.cker, er al ;1994; Plant Physiol., 104, 99-107] and are able ro degrade xyicglucans as oescribec in Hayashi et al (1939) Plant. Physiol. Plant Mol. Bid., 40, 139-168. Vincken ec al demonstrated the removal of xylogiucan coating from cellulose of the isolated apple ceil wail by a xyloglucanase purified from Trichoderma vicide (er.dc-17-giucar.ase) . This enzyme enhances the enzymatic degradation of ceil wall-embedded cellulose and work in synergy with peccic enzymes. Rapidase L1Q+ from Gist-Erocades contains ar, xyioglucanase activity. This xylcgiucar.ase is incorporated ir.tc the cleaning compo¬sitions in accordance with the invention preferably at a level of from C.00G1% to 2r;, sic re preferably from 0.0005% to C.5%, most preferred from C.C 01 % tou.l % pure enzyme by weight of the composition. Preferred xylogiucanases for specific applications are alkaline xyloglucanases, ie enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% cf their maximum activity at a pH ranging from 7 to 12. More preferred xyloglucanases are enzymes having their maximum activity at a pH ranging from 7 to 12. The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrctrophic, thermophilic, barophilic, aika-lophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / ge¬netic engineering techniques m order to optimise their perform¬ance efficiency in the cleaning compositions of the invention. For example, the variants may be designed such that the compati¬bility of the enzyme tc commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that the optimal PH, bleach or cneiant stability, catalytic activity and the like, of the entyme variant is tai¬lored to suit the particular cleaning application. Ir: particular, attention should be focused on amino acios f sensitive to oxidation m the case of bleach stability anc or. surface charges for the surfactant compatibility. The isoelec¬tric point of such enzymes may be modified by the substitution of some charged anino acids, e.g. an increase in isoelectric point may help to improve compatibility with anionic surfac¬tants. The stability c£ the enzymes may be further enhanced by the creation of e.g. additional salt bridges and enforcing metal binding sites to increase cheiant stability. R1 eaching aggros ; Additional optional detergent ingredients that can be included in the detergent compositions of the present invention include bleaching agents such as PB1, PB4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components can include one or more oxygen bleaching agents and, depending upon the bleaching agent chosen, one or more bleach activators. When present oxygen bleaching compounds will typically be present at levels of from about 1% to about 25%. In general, bleaching compounds are optional added components in ion-liquid formulations, e.g. granular detergents. A bleaching agent component for use herein can be any of :he bleaching agents useful for detergent compositions including >xygen bleaches, as well as others known in the art. A bleaching agent suitable for the present invention can >e an activated or non-activated bleaching agent. One category of oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include magnesium mor.opercxyphthaiate hexahydrate, the magnesia salt of meta-chloro perbenzoic acid, 4-ncnylamino-4-oxoperoxybutyric acid and diperoxydodecanedicic acid. Such bleaching age—3 are disclosed in US 4,483,781, US 740,446, EP 0 133 354 and US 4,412,934. Highly preferred bleaching agents also include 6-nonylaminc-6-cxcpercxycaproic acid as described in US 4,634,551. Another category of bleaching agents that can be used encompasses the halogen bleaching agents. Examples of hypohalite bleaching agents, for example, include trichloro isocyanuric ) acid and the sodium and potassium dichloroisocyanurates and N-chloro and N-bromo alkane sulphonamides. Such materials are nor¬mally added at C.5-10% by weight cf the finished product, preferably 1-5% by weight. The hydrogen peroxide releasing agents can be used in combination with bleach activators such as tetra- acetylethyienediamine (TAED), nonanoyloxybenzenesulfcnate (NOBS, described in US 4,412,934), 3,5-trimethyl- hexsanoloxybenzenesulfonate (ISONOBS, described in E? 120 591) or pentaacetylglucose (PAG), which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. In addition, very suitable are the bleach activators C8(6-octanamido-caproyl} oxybenzene-sulfonate, C9 (6-nonanamido caproyl) oxybenzenesulfonate and ClO (6-decar.amido caproyl) oxybenzenesulfonate or mixtures thereof. Also suitable activators are acylated citrate esters such as disclosed in European Patent Application No. 91870207.7. Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in cleaning compositions according to the invention are described in application USSN 08/136,625. The hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generation cf hydrogen peroxide ac the beginning or during the washing and/or rinsing process. Such enzymatic systems are disclosed in European Patent Application EP 0 53? 381. r Bleaching agents other -nan oxygen bleaching agents are also known in the art and can be utilized herein. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated zinc and-/or aluminium phthalocyanines. These materials can be deposited upon the substrate during the washing process. Upon irradiation with light, in the presence cf oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is activated and, consequently, the substrate is bleached. Preferred zinc phthalocyanine and a photoactivated bleaching process are described in US 4,033,718. Typically, detergent composition will contain about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine. Bleaching agents may also comprise a manganese catalyst. The manganese catalyst may, e.g., be one of the compounds described in "Efficient manganese catalysts for low-temperature bleaching", Majors 2£2, 1994, pp. 637-639- Sud? Repressors: Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-silicone mixtures. Silicones can generally be represented by alkylated polysiloxane materials, while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. Theses materials can be incorporated as particulates, in which the suds suppressor is advantageously releasably incorporated in a water-soluble or water-dispersible, substantially non surface-active detergent impermeable carrier. Alternatively the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or mere of the other components. A preferred silicone suds controlling agent is disclosed ■ in US 3,933,672. Other particularly useful suds suppressors are the self-emulsifying Silicone suds suppressors, described in German Patent Application DTOS 2,64 5,126. An example of such s compound is D0544, commercially available form Dow Corning, which is a siloxane-glycol copolymer. Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alkanols. Suitable 2-alkyi-alkanols are 2-butyl-ocnanol which are commercially available under the trade name Isofol 12 R. Such suds suppressor system are described in European Patent Application EP 0 553 841. Especially preferred silicone suds controlling agents are described in European Patent Application No. 92201649.8. Said compositions can comprise a silicone/ silica mixture in combination with fumed nonporous silica such as Aerosil*. The suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% tc 1% by weight. ^t-.he.r components: Other components used in detergent compositions may be employed, such as soil-suspending agents, soil-releasing agents, optical brig&teners, abrasives, bactericides, tarnish .nhibitors, coloring agents, and/or encapsulated or lonencapsulated perfumes. Especially suitable encapsulating materials are water soluble capsules which consist of a matrix of polysaccharide and polyhydrcxy compounds such as described in GB 1,464,616. Other suitable water soluble encapsulating materials comprise dextnns derived from ungelatinized starch acid esters of substituted dicarbcxylic acids such as described in US 3,455,838. These acid-ester dextrins are, preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said encapsulation materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modified by adding mcnofunctional substituted groups such as octenyl succinic acid anhydride. Antiredepcsition and soil suspension agents suitable herein include cellulose derivatives such as methylceilulose, carboxymethylcellulose and hydroxyethyicellulose, and homo- cr co-polymeric pclycarboxylic acids or their salts..Polymers of i this type include the pclyacryiates and maleic anhydride-acrylic acid copolymers previously mentioned as builders, as well as copolymers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of frcm 0.5% to 10% by weight, more preferably form 0.75% to 8%, most preferably from 1% to 6% by weight of the composition. Preferred optical brighteners are anionic in character, examples of which are disodium 4,4■-bis-(2-diethanolamino-4-anilino -s- tria2in-6-ylami.no) stilbene-2 :2 ( disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino-stilbene-2:2' - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin-6-ylamino)stilbene-2:2' - disulphonate, monosodium 4',411 - bis-(2,4-dianilino-s-tri-azin-6 ylamino)stilbene-2-sulphonate, disodium 4,4' -bis-(2-anilino-4-(N-methyl-N-2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2' - disulphonate, di-sodium 4,4' -bis-(4-phenyl-2,1,3- triazol-2-yl)-scilbene-2,2' disulphonate, di-so-dium 4,4'bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-£-ylami-no)stilbene-2,2'disulphonate, sodium 2(stilbyl-4' '- inaphtho-I1 ,2l :4,5)-1,2,3, - triazoie-2' '-sulphonate and 4,4'-bis(2-sulphostyryl)biphenyl. Other useful polymeric materials are the polyethylene glycols, particularly those of molecular weight IDCO-IODOO, more particularly 2Q0Q to 8Q0O and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight. These polymers and the previously mentioned homo- or co-polymeric poly-carboxylase salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proceir.aceous and oxidizable soils in the presence of transition me^ai impurities. Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are disclosed in US 4,116,885 and 4,711,730 and cP C 272 033. A particular preferred polymer in accordance with EP 0 272 033 has the formula: (CH3 (PEG)43) 0.7S (POH) c.25 [T-PO) ,.3 (T-PEG) 0. where PEG is -(OC3H,)0-, PO is (OC3H60) and T is (pOOC6H,CO) . Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1,2-propanediol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or 1,2-propanediol. The target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of saad copolymers herein will be endcapped by sulphobenzoate groups. However, some copolymers will be less Chan fully capped, and therefore their er.d groups may consist of monoester of ethylene glycol and/cr 1,2-propanediol, thereof consist "secon-3 darily" of such species. The selected polyesters herein contain about 45% by weight of dimethyl terephthalic acid, about 16% by weight of 1,2-propanediol, about 10% by weight ethylene glycol, about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of Sulfoisophthalic acid, and have a molecular weight of about 3.000. The polyesters and their method of preparation are described in detail in EP 311 342. Softening agent,s ; fabric softening agents can also be incorporated into laundry detergent compositions in accordance with the present invention. These agents may be inorganic or organic in type. Incrganic softening agents are exemplified by the smectite clays disclosed in GE-A-1 400898 and in US 5,019,252. Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP 0 oil 340 and their combination with mono C:,-C14 quaternary ammonium salts are disclosed in EP-B-Q 026 528 and di-lang-chain amides as disclosed in EP 0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP 0 299 575 and C 313 146. Levels of smectite clay are normally in the range from 5% to 15%, more preferably from 8% to 12% by weight, with the material being added as a dry mixed component to the remainder of the formulation. Organic fabric softening agents such as the water-insoluble tertiary amines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight, normally from 1% to 3% by weight whilst the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight. These materials are normally added to the spray dried portion of the composition, although in some instances it may be more convenient to add them as a dry mixed particulate, or spray them as molten liquid or. to other solid components of the composition. Polymeric dye-transfer inhabiting agents; The detergent compositions according to the present invention may also comprise from 0.001% to 10%, preferably from 0.01% to 2%, mere preferably form 0.05% to 1% by weight of polymeric dye- transfer inhibiting agents. Said polymeric dye-transfer inhibiting agents are normally incorporated into detergent compositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability of complexing or adsorbing the fugitive dyes washed out of dyed fabrics before the dyes have the opportunity to become attached to other articles in the wash. Especially suitable polymeric dye-transfer inhibiting agents are polyamine N-cxide polymers, copolymers of N-vinyl-pyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. Addition of such polymers also enhances the performance of the enzymes according the invention. Use in the paper pulp industry Further, it is contemplated that the mannanase of the present invention is useful in chlorine-free bieacning processes for paper pulp (chemical pulps, semichenrcal pulps, mechanical pulps or kraft pulps) in order to increase the brightness f thereof, thus decreasing cr eliminating the need for hydrogen peroxide in the bleaching process. Use in the textile and cellulosic fiber processing industries The mannanase cf the present invention can be used in com¬bination with other carbohydrate degrading enzymes (for instance xyiogiucanase, xylanase, various pectinases) for preparation of fibers cr for cleaning of fioers in combination with detergents. In the present context, the term "cellulosic material" is intended to mean fibers, sewn and unsewn fabrics,'including knits, wover.s, denims, yarns, and toweling, made from cotton, cotton blends cr natural or manmade cellulosics (e.g. orig¬inating from xylan-containing cellulose fibers such as from wood pulp) or blends thereof. Examples of blends are blends of cotton or rayon/viscose with ere cr more companion material such as wool, synthetic fibers (e.g. poiyamide fibers, acrylic fibers, polyester fibers, polyvinyl alcohol fibers, polyvinyl chloride fibers, polyvinyiidene chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and cellulose-containing fibers (e.g. rayon/viscose, ramie, hemp, flax/linen, jute, cellulose acetate fibers, lyoceli). The processing of cellulosic material for the textile industry, as for example cotton fiber, into a material ready for garment manufacture involves several steps: spinning of the fiber into a yarn; construction of woven or knit fabric from the yarn and subsequent preparation, dyeing and finishing operations. Woven goods are constructed by weaving a filling yarn between a series of warp yarns; the yarns could be two different types. Desizmg: polymeric size like e.g. mannan, starch, CMC cr PVA is added before weaving m order to increase the warp speed; This material must be removed before further processing. Tne enzyme of the invention is useful fcr removal of mannan contain¬ing size. Degradation of thickeners Galactomanr.ans such as guar gum and locust bean gu~ are widely used as thickening agents e.g. in food and print paste for textile printing such as prints on T-shirts. The enzyme or enzyme preparation according re the invention can be used for reducing the viscosity of eg residual food in processing equip¬ment and thereby facilitate cleaning after processing. Further, it is contemplated that the enzyme or enzyme preparation is useful for reducing viscosity of print paste, thereby facilitat¬ing wash out of surplus print paste after textile printins. Degradation or modification of plant material The enzyme or enzyme preparation according to the invention is preferably used as an agent fcr degradation or modification of mannan, galactcmannan, glucomannan or galactoglucomannan containing material originating from plants. Examples of such material is guar gum and locust bean gum. The mannanase of the invention may be used in modifying the physical-chemical properties of plant derived material such as the viscosity. For instance, the mannanase may be used to reduce the viscosity of feed or food which contain mannan and to promote processing of viscous mannan containing material. ' Coffee extraction r The enzyme or enzyme preparation ct the invention may also be used for nyarciysmg gslsctomannar.s present in a liquid coffee extract, preferably in. order to inhibit gel formation ourir.a freeze drying of the (instant) coffee. Preferably, ' the .T.ar.r.anase of the invention is immobilized in order to reduce enzyme consumption and avoid contamination of the coffee. This use is further disclosed in EP-A-676 145. Use in the fracturing of a subterranean formation (oil drilling) Further, it is contemplated that the enzyme cf the present invention, is useful as an enzyme breaker as disclosed in US patent nos. 5,8C6,5S7, 5,562,160, 5,201,370 and 5,067,5S5 to BJ Services Company (Houston, TX, U.S.A.), all of which are hereby incorporated by reference. Accordingly, the mannanase of the present invention is use¬ful in a method of fracturing a subterranean formation in a well bore in which a gellable fracturing fluid is first formed by blending together an aqueous fluid, a hydratable polymer, a suitable cross-linking agent for cross-linking the hydratable polymer to form a polymer gel and an enzyme breaker, ie the enzyme of the invention. The cross-linked polymer gel is pumped into the well bore under sufficient pressure to fracture the surrounding formation. The enzyme breaker is allowed to degrade the cross-linked polymer with time to reduce the viscosity or the fluid so that the fluid can be pumped from the formation back to the well surface. The enzyme breaker may be an ingredient of a fracturing fluid or a breaker-crosslinker-polymer complex which further comprises a hydratable polymer and a crosslinking agent, The fracturing fluid or complex may be a gel or may be gellaole. The complex is useful in a method for using the complex in a rrac-curing fluid to fracture a subterranean formation that surrounds a well bore by pumping the fluid to a desired location within the well bore under sufficient pressure to fracture the sur¬rounding subterranean formation. The complex may be maintained in a substantially non-reactive state by maintaining specific conditions cf pH and temperature, until a time at which the fluid is in place m the well bore and the desired fracture is completed. Once the fracture is completed, the specific condi¬tions at which the complex is inactive are no longer maintained. When the conditions change sufficiently, the complex becomes active and the breaker begins to catalyze polymer degradation causing the fracturing fluid to become sufficiently fluid to be pumped from the subterranean formation to the well surface. MATERIALS AND METHODS Assay for activity test A polypeptide of the invention having mannanase activity may be tested for mannanase activity according to standard test procedures known in the art, such as by applying a solution to be tested to 4 mm diameter holes punched out in agar plates containing 0.2% AZCL galactomannan (carob), i.e. substrate for the assay of endo-1,4-beta-D-mannanase available as CatNo.I-AZGMA from the company Megazyme (Megazyme's Internet address: http://www.megazyme.com/Purchase/index.html). Determination of catalytic activity (ManU) of mannanase "oloriraetric Assay Substrate: 0.2% AZCL-Galactomannan (Megazyme, Australia) from carob in 0.1 M Glycin buffer, pH 10.0- The assay is carried out in an Eppendorf Micro tube 1.5 mi :>n a thermomixer with stirring and temperature control of 40°C. [ncubstion of 0.750 ml substrate with 0.05 ml enzyme for 20 rnin, stop by cer.trifugation for 4 minutes at 15000 rpm. The colour of the supernatant Ls measured a- 600 nm in a 1 cm cu-vette. One Ma.nU {Mannanase units) gives 0.24 abs in 1 cr,, i Strains and donor organism The Bacillus sp. 1633 mentioned above comprises the beta-1, 4-mannanase encoding DMA sequence shown in SEQ. ID. NO: I. E.coli DSM 12197 comprises the plasmid containing the DNA encoding the beta-1, 4~manriar.ase of the invention (SEQ. ID, NO: 1; . The Bacillus agaradhaeraris NCTM3 40482 mentioned above com¬prises the beta-i,4-mannanase encoding DNA sequence shown in SEQ.ID.NO:5. E.coli DSM 12180 comprises the plasmid containing the ONA er.codir.g the beta-1, 4-manr.a.nase of the invention t SEQ. ID . NC: 5 ) . The Bacillus sp. AAI12 mentioned above comprises the beta-1, 4-mar.nanase encoding DNA. sequence shown in SEQ,ID.NO:9. E.'ccli DSM 12433 comprises the plasmid containing the DNA encoding the beta-1,4-mannanase of the invention (SEQ.ID.NO:9). The Bacillus haloduzans mentioned above comprises the beta-1,4-mannanase encoding DNA sequence shown in SEQ.ID.NO:11. E.coli DSM 12441 comprises the plasmid containing the DNA encoding the beta-1,4-mannanase of the invention (SEQ.ID.NO:11). The Humiccla insolens mentioned above comprises the beta-L,4-mannanase encoding DNA sequence shown in SEQ.ID.NO:13. E.coli DSM 9984 comprises the plasmid containing the DNA encoding the beta-1,4-mannanase of the invention (SEQ.ID,NO:13). The Bacillus sp, AA.349 mentioned above comprises the beta-.,4-mannanase encoding DNA sequence shown in SEQ.ID.NO:15. E.coli DSM 12432 comprises the plasmid containing the DNA ■needing the beta-1,4-mannanase of the invention (SEQ.ID.NO:15). E.coli DSM 12847 comprises the plasmid containing the DNA encoding the beta-1,4-mannanase of the invention (SEQ.ID.NO:17). E.cc^i DSM 126-5 3 comprises one plasmid containing the DNA encoding tr.e beta-1,4-marmanase cf the invention (SEQ. ID. NC: IS) . Trie 5acj.iiu5 cia i^so i mentioned above comprises the beta-1,4-mannanase encoding DMA sequence shown in SEQ. ID.NO:21. E.coli DSM 1284 9 comprises the plasmid containing the DNA encoding the beta-1,4-mannanase of the invention (SEQ.ID.NC:21). E.coli DSM 12350 comprises the plasmid containing the DNA encoding the beta-i, 4-mar.nanase cf the invention (SEQ. ID.NO: 23) . Bacillus so. comprises the beta-1,4-mannanase encoding DNA sequence shown in SEQ. ID. NC : 25 . E.coli DSM 12846 comprises the■plasmid containing the DNA encoding the beta-1,4-mannanase of the invention (SEQ.ID.KG:25). Bacillus sp, comprises the beta-1,4-mannanase encoding DMA sequence shewn in SEQ . ID . NO: 27. E.ccli DSt The Bacillus lichenifcrmis mentioned above comprises the beta-1,4-mannanase encoding DNA sequence shown in SEQ.ID,NO:29. E.coli DSM 12352 comprises the plasmid containing the DNA. encoding the beta-I,4-mannanase of the invention (SEQ.ID.NC:29) . 3acilius so. comprises the beta-1,4-mannanase encoding DNA sequence shown in SEQ.ID.NO:31. E.coli DSM 12436 comprises the plasmid containing the DMA encoding the beta-1,4-mannanase of the invention (SEQ.ID-NO:31). E. coli strain: Cells of E. coli SJ2 (Diderichsen, B., Wedsted, \J. , Hedegaard, L., Jensen, B. R., Sjaholm, C. (1990) Oioning of aldE, which encodes alpha-acetolactate decarboxylase, an exoenzyme from Bacillus brevis. J. Bacterid., 172, 4315-4321), were prepared for and transformed by electrocoration ising a Gene PulserTM electroporator from EIO-RAD as described zy the supplier. E.sutzilis P1.23G6. This strain is the E.subzilis U1U88 5 with disrupted apr and r.pr ger.es (Diderichsen, B., Wedsted, U., Hedegaard, 1., Jer.sen, 5. R., 5je>hclm, C. {1950; Cloning of aldB, which encodes alpha-acetolactace decarboxylase, ar. exoen-i zyme from Bacillus brevis. J. Bacterid., 172, 4315-4321) dis¬rupted in the transcriptional unit of the known Bacillus sub-tilis celluiase gene, resulting in cellulase negative cells. The disruption was performed essentially as described in ( Eds. A.L. Sonenshein, J.A. Hoch and Richard losick (1993) Bacillus sub-tills and ether Gram-Positive Bacteria, American Society for microbiology, p.616) . Competent cells were prepared and transformed as described by Yasbin, ?..£., Wilson, G.A. and Young, F. El. (197t) Transforma¬tion and transfection in lyscgenic strains of Bacillus subtilis: evidence for selective induction of prophage in competent cells. J. Bacterid, 121:296-304. General molecular biology methods: Unless otherwise stated all the DNA manipulations and transformations were performed using standard methods of molecu¬lar biology (Sambrook et al. (1989) Molecular cloning: A labora¬tory manual. Cold Spring Harbor lab., Cold Spring Harbor, NY; Ausubel, F. M. et al. (eds.) "Current protocols in Molecular Biology". John Wiley and Sons, 1995; Harwood, C. P,., and Cut¬ting, S. K. (eds.) "Molecular Biological Methods for Bacillus". John Wiley and Sons, 1990). Enzymes for DNA manipulations were used according to the manufacturer's instructions (e.g. restriction endonucleases, ligases etc. are obtainable from New England 3iolabs, Inc.). Plasm!ds PSJ1678: (see International Patent Application published as WO 94/19454)- pBK-CMV (Stratager.e inc., La Jolla Ca.i pMOL944. This plasmid 15 a p'JBHO derivative essentially containing elements making the plasmid prcpagacable in Bacillus subtiiis, kanamycin resistance gene and having a strong promoter and signal peptide cloned from the amyL gene cf B. liche^iforxiis ATCC14580. The signal peptide contains a SacII site ma-;ing it convenient to clone the DMA encoding the mature part cf a pro¬tein in-fusion with the signal peptide. This results in the expression of a Pre-prctein which is directed towards the exte¬rior of the cell. The plasrr.id was constructed by means cf ordinary genetic engineering and is briefly describee in the following. Construction cf PMQL944: The pUBllO plasmid [McKenzie, T. et al. , 1966, Flasmid 15:93-103) was digested with the unique restriction enzyme Neil. A PCP. fragment amplified from the amy! promoter encoded on the plasmid pDN1981 (P.L. Jargensen et al.,1990, Gene, 96, p37-41.) 1 was digested with Neil and inserted in the Neil digested pUBllC to give the plasmid pSJ2624. The two PCR Drimers used have the following sequences: # LWN5494 5'-GTCGCCGGGGCGGCCGCTATCAATTGGTAACTGTATCTCAGC -3' # LWN54 9 5 5'-GTCGCCCGGGAGCTCTGATCAGGTACCAAGCTTGTCGACCTGCAGAA TGAGGCAGCAAGAAGAT -3' The primer #LWN5494 inserts a NctI site in the plasmid. The plasmid pSJ2624 was then digested with SacI and NotI and a new PCR fragment amplified on amy! promoter encoded on the PDN1981 was digested with SacI and NctI and this DMA fragment was inserted in the SacI-NotI digested pSJ2624 to give the plasmid pSJ26"70. This cloning repiacas the first amy! promoter cloning wizr. the same promoter but in the opposite direction. The two primers used for PCR amplification have the following sequences; i #LWN5938 5 " -GTCGGCGGCCGCTGATCACGTACCAAGCTTGTCGACCTGCAGAATG ' AGGCAGCAAGAAGAT -3' W1WN5939 5 ' -GTCGGAGCTCTATCAATTGGTAACTGTATCTCAGC -3 ' The plasrr.id pSJ2670 was digested with the restriction en¬zymes PstI and Bell and a PCS fragment amplified from a cloned DNA sequence encoding the alkaline amylase SP722 (Patent *f W09525397-A1) was digested with PstI and Bell and inserted to give the piasmid pMOL94 4. The two primers used for PC?, amplifi¬cation have the following sequence: #LWN"8 64 5' -AACAGCTGATCACGACTGATCTTTTAGCTTGGCAC-3' SLWN7 9Q1 5' -AACTGCAGCCGCGGCACATCATAATGGGACAAATGGG -3' The primer #LWN7 901 inserts a SacII site in the plasmid. Cultivation of donox strains and isolation of genomic DNA The relevant strain of Bacillus, eg Bacillus sp. 1633, was grown ir. TY with pH adjusted to approximately pH 3.7 by the addition of 50 ml of 1M Sodium-Sesqu.icarbor.at per 500 ml TY. After 24 hours incubation at 30°C and 30G rpm, the cells were harvested, and genomic DNA was isolated by the method described by Pitcher et al. [Pitcher, D. G. , Saunders, N. A. , Owen, R. J; Rapid extraction of bacterial genomic DNA with guanidium thiocy-anate; Lett Appl Microbiol 1989 8 151-156], Media TY (as described in Ausubel, F. M. et al. (eds.) "Current protocols in Molecular Biology". John Wiley ar.d Sons, 1995). LB agar ias described ir. Ausubei, F. K. et al. fees.; "Current protocols ir. Molecular Biology". John Wiley er.d Sons, 1995). LBPG is LB agar supplemented with 0.5% Glucose and 0.05 M potassiurn phosphate, pH 7 . C AZCL-galactomannan is added to LBPG-agar to C.5 % A2"CL-gaiaencmannar: is frorr. Megazyme, Australia. BPX media is described in ZP 0 506 730 (WO 91/09129:. NZY agar (per liter) 5 c of MaCi, 2 g of MgS04, 5 g of yeast extract, 10 g of NS amine (casein hydrolysate), 15 g cf agar; ace deionized water to 1 liter, adjust pK with MaOH to pH 7.5 and autoclave NZY broth (per liter) 5 g cf KaCl, 2 g of MgS04, 5 g of yeast extract, ID g of KZ amine (casein hydrolysate} ; add deion-j ized water to 1 liter, adjust pH with NaOH to pH 7.5 and auto¬clave NZY Top Agar (per liter) 5 g of KaCl, 2 g of M'gS04, 5 g of yeast extract, 13 g cf !\Z amine (casein hydrolysate), 0.7 % (w/v) agarose; add deionized water to 1 liter, adjust pn with NaOH to pH 7,5 and autoclave. The following non-limiting examples illustrate the inven¬tion. EXAMPLE 1 Mannanase derived from. Bacillus sp (1633) Construction of a genomic library from Bacillus sp. 1633 in the lambdaZAPExpress vector Genomic DNA of Bacillus sp. 1633 was partially digested with restriction enzyme Sau3A, and size-fractionated by elec¬trophoresis on a 0.7 % agarose gel (SeaKem agarose, FMC, USA). Fragments between 1.5 ar.c 1C kb in size were isolated and ccn-centrated tc a DNA band by running the DMA fragments tackwards on a 1.5 % agarose eel relieved by extraction c: the fragments from the agarose gel slice using the Qiaquiet: gel extraction kit 5 according tc the manufacturer's instructions {Qiagen Inc., USA;. To construct a genomic library, ca. lOOng cf purified, fraction¬ated DNA frcrc above was ligated with 1 ug cf BanHI-cleaved, dephosphoryiated lambdaZAPexpress vector arms (Stratagene, La Jcila CA, USA; for 2\ hours at + 4 °C according to the manufac- ) turer's instructions. A 3-uI aliquot of tne ligation mixture was packaged directly using the GigaPscklll Gold packaging extract (Stratagene, USA) according tc the manufacturers instructions (Stratagene). The genomic lanbdaZAPExpress phage library was titered using the E. cell XLI-31ue MRF- strain from Stratagene . (La Jclla, USA). The unamplified genomic library comprised of 3 x 10' plaque-terming units (pfu) with a vector background of less than 1 %. Screening for beta-mannanase clones fay functional expression in lambdaZAPExpress Approximately 5000 plaque-forming units (pfu; frorr. the genomic library were plated on NZY-agar plates containing C.i % AZCL-galactomannan (MegaZyme, A.ustralia, cat. no. I-AZGMA;, using E. eeli XLl-Blue MRF' ; Stratagene, USA) as a hest, fol¬lowed by incubation cf the plates at 31 °C for 24 hours. Man-nanase-positive lambda clones were identified by the formation of blue hydrolysis hales around the positive phage clones. These were recovered from the screening plates by coring the TOF-agar slices containing the plaques cf interest into 500 ul of SM buffer and 20 ul of chlcrcform. The mannanase-positive lamb¬daZAPExpress clones were plaque-purified by plating an aliquot of the cored phage stock en NZY plates containing 0.1 % AZCL- cjaiactcnannan as above. Single, manr.anase-positi ve ia~rda ccr.es were cored. in~o 500 ul cf SM buffer and 20 ul cf chicrofcrx., and purified by one more plating round as described above. Single-clone in vivo excision of the phagemids from the man-nanase-positive lambda2APExpress clones E. ccli Xll-Biue'cells (Stratagene, La Jolia Ca. ■ were prepared and resuspended in lOmM MgS04 as recommended by Scratagene (La Joila, CSA) . 250-ul aliquocs of tne pare phage srocks from the mannase-positive clones were combined in Falcon 2059 rubes with 200uis of XLl-Elue MRF' cells (CO6C0 = 1.0) and > 10c pfus/ml cf the ExAssist M13 helper phage !£:ratacen=;, and the mixtures were incubated a: 37 °C for 15 minutes. Three mis cf NZY broth was added to each tube and the tubes were incubated at . 37 C fcr 2.5 hours. The tubes were heated at 65°C fcr 20 minutes to kill the E. coli cells and bacteriophage lambda; tne phagemids being resistant to hearing. The tubes were spun en 3000 rprr. fcr 15 minuoes to remove cellular debris and che super-natants were decanred into clean Falcon 2059 tubes. Aliqucos of the supernatants containing the excised single-stranded phagemids were used to infect 200uls of E. coli XLQL? cells (Stratagene, OD600=1.0 in lOmM MgS04) by incubation at 37°c for 15 minutes. 350uls of NZY broth was added to the ceils and the tubes were incubated fcr 45 min a.t 37DC. Aliquots of the cells were plated onto LB kanamycin agar plates and incubated fcr 24 hours at 37°C. Five excised single colonies were re-streaked onto LB kanamycin agar plates containing 0.1 % A2CL-galactcmannan (MegaZyme, Australia). The mannanase-positive phagemid clones were characterized by the formation of blue hydrolysis haios around the positive colonies. These were fur¬ther analysed by restriction enzyme digests cf the isolated plagemid DMA [QiaSpin kit, Qiagen, USA) with Sco?.I, ?stl, EcoRI- Pst_, and HindiI, followed cy agarose gel electrophoresis. Nucleotide sequence analysis The nucleotide sequence cf the genomic beca-1, 4-^.ar.nanase f clone pBXK3 was determined from both strands by "he dideoxy chain-termination method (Sanger, F., Nickien, S., and Coulson, A. R. (1977; Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467] using 500 ng of Ciagen-purifled template (Qiager., USA!, the Tag deoxy-terminal cycle sequencing kit (Perkin-Elmer, USA,, fluo¬rescent labeled terminators and 5 pmoi of either pBK-CXV polylinker primers (Strataoene, USA) or synthetic oligonucleo¬tide primers. Analysis cf the sequence data was performed ac¬cording to Devereux et al., 1984 (Devereux, J., Haeberli, P., and Smithies, G. (1964) Nucleic Acids Res. 12, 357-295;. Sequence alignment A multiple sequence alignment of the giycohydrclasa family 5 beta-1, 4-itar.nanase from Bacillus sp. 1633 of the present invention (ie SEQ ID N0:2), Bacillus circulans (GenEank/EMBL accession no. 066185), Vibrio sp. (ace. no. 069347), Streptomyces lividans (ace. nc. P51529), and Caldicellulosizuptoz saccharolyticus (ace. no. P22533;. The multiple sequence alignment was created using the Pile:Jp program of the GCG Wisconsin software package,version 8.1.; with gap creation penalty 3.00 and gap extension penalty 0.1C. Sequence Similarities The deduced amino acid sequence cf the family 5 beta-1,4-mannanase of the present invention cloned from Bacillus sp. 1633 shows 75 % similarity and 60.1 % sequence identity to the beta-1,4-mannanase of Bacillus circulans (GenBank/EM3L accession no. 066185), 64.4 % similarity and 44.6 % identity to the beta-1,4- mannanase from Vibrio sp. (ace. nc. 06934";, 63 % similarity anc 43.2 % ioenticy to the be" a-1, 4-mannanase from 5rrepcomy'ce5 iividans (ace. no. P5152 9), 52.5 -i similarity and 34.4 % sequence identity to the beta-1,4-mannanase from Caldicellulosirvptor saccharolyticus (ace. no. P22 5 3 j . The sequences were aligned using the GAP program of the GCG Wisconsin software package,version 8.1.; with gap creation penalty 3.00 and cap extension penalty 0,10. "loning of Bacillus sp (1633) mannanase gene A. Subclcninc and expression cf a catalytic core manna.-.ase enzyme in B.suttilis: The mannanase encoding DNA sequence cf the invention was PCR amplified using the PCR primer set consisting of the follow¬ing two cligo nucleotides: BXM2.upper.SacII 5'-GTT GAG AAA GCG GCZ GCG TTT TTT CTA TTC TAG AAT CAC ATT ATC-3' BXM2.core,lower.Not I 5'-GAG GAC GTA CAA GCG GGG GCT CAC TAC GGA GAA GTT CCT CCA TCA G-3' Restriction sites SacII and NotI are underlined. Chromosomal 3NA isolated from Bacillus sp. 1633 as described above was used as template in a PCR reaction using Amplitaq DNA Polymerase (Perkin Elmer) according to manufacturers instructions. The PCR reaction was set up in PCR buffer (10 mM Tris-HC_, pH S.3, 50 mM KC1, 1.5 mM MgCl2, C.01 % (w/v) gelatin) containing 20C uM of each dKTF, 2.5 units of AmpliTaq polymerase {Parkin-Elmer, Cetus, USA) and 10C pmol of each primer. The PCR reactions was performed using a DNA thermal cycler 'Landgrai, Germany;. One incubation at S4°C tor 1 nit followed by thirty cycles of PCR performed using a cycle profile cf denaturatior: at S4~C for 30 sec, annealing a: 60GC for 1 min, and extension at 12 "Z for 2 r.in. Five-ul aliqucts of the ampli¬fication product was analysed by electropnoresis in 0.7 ? agarose gels (MuSieve, FMCj . The appearance of a DKA fragment size 1.0 kb indicated proper amplification of the gene segment. Subcloning cf PCR fragment: Fcrtyfive-ul aliquots cf the PCR products generated as described above were purified using QIAquick PCR purification Kit (Qiagen, USA) according zo the manufacturer's instructions. The purified DN'A was eiuted in 5C ul of iOrnK Tris-HCl, pK 8.5. 5 pg cf pMOL944 and twencyfive-ul of the purified PCR fragment was digested with Sac": and NotI, electrophoresed in 0.8 % low gelling temperature agarose (SeaFlaque GTG, FMC) gels, the relevant fragments were -excised from the gels, and purified using QIAquick Gel extraction Kit (Qiagen, USA) according to the manufacturer's instructions. The isolated PCR DNA fragment was then iigated to the SacII-NotI digested and purified pMOL94 4. The ligation, was performed overnight at 16°C using 0.5 pg of each DHA fragment, 1 V of T4 DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany). The ligation mixture was used to transform competent B.subtilis PL2306. The transformed cells were plated onto LBPG-10 ug/ml of Kanarnycin-agar plates. After 18 hours incubation at 37 °C colonies were seer, on plates. Several clones were analyzed by isolating plasmid DMA from overnight culture broth. One such positive clone was restreaked several times or. agar plates as used above, this clone was called M3748. The clone MB748 was grown overnight in TY-lOug/ml Kanarnycin at 37°C, and next day 1 ml cf cells were used to isolate plasmid from the cells using tne Qiaorec Spin rlasmid Miniprep Kit #27106 accorc-ir.c to "he ir,ar.-f=cturors recommendations for B.subcilis plasnid oreparaiior.s. This DMA was DNA sequenced and revealed Che DNA sequence corresponding tc the mature part cf the mannanase (corresponding to positions 91-990 in the appended DNA sequence SEQ ID NO: 1 and positions 31-330 in the appended protein, se¬quence SEQ ID NC:2) with introduced stop codon replacing the amino acid residue no 331 corresponding to the base pair posi¬tions 12C1-1203 in SEQ ID NO:1 - B-. Suboloning and expression of mature full length mannanase ir. B.subtil is, The mannanase encoding DMA sequence of the invention was PCR amplified using the FCE primer set consisting of these two cligo nucleotides: BXM2.upper.SacII 5'-CAT TCT GCA C-CC GCG GCA AAT TCC GGA TTT TAT GTA AGC GG-31 BXM2.lower.Not I 5'-GTT GAG AAA GCG GCG C-CC TTT TTT CTA TTC TAC AAT CAC ATT ATC -3 ' Restriction sites SacII and NotI are underlined Chromosomal DNA isolated from Bacillus sp . (1633) as described above was used as template in a PCR reaction using Artiplitaq DNA Polymerase (Perkin Elmer) according to manufacturers instructions. The PCR reaction was set up in PCR buffer (10 mM Tris-HCl, pK 8.3, 50 mM KC1, 1.5 mM MgCl2, 0.01 % (w/v) gelatin! containing 200 \M of each dNTP, 2.5 units of AmpliTaq polymerase (Perkin-Elmer, Cetus, USA) and 100 pmol of each primer The PCR reactions was performed using a DNA thermal cycler (Landgraf, Germany). One incubation at 94°C for 1 min followed by thirty cycles of PCR performed using a cycle prcfile of denaturation at 94ZC for 30 sec, annealing at 60°C for 1 tr.ir., and extension at 72 °C for 2 min. Five-ul aliquots of the ampli¬fication product was analysed by electrophoresis in 0.7 % agarose gels (NuSieve, FMC) . The appearance of a DNA fragment size 1.5 kb indicated proper amplification of the gene segment. Subcloning of FCR fragment: Fortyfive-/xl aliquots of the PCR products generated as described above were purified using QIAquick PCR purification kit (Qiagen, USA) according to the manufacturer's instructions. The purified DNA was eluted in 50 JJI of lOmM Tris-HCl, pK 8.5. 5 /ig of pMOL94 4 and twenty five -/J.1 of the purified PCR fragment was digested with SacII and Not;, electrophoresed-in 0.8 % low gelling temperature agarose (SeaPlaque GTG, FMC) gels, the relevant fragments were excised from the gels, and purified using QIAquick Gel extraction Kit (Qiagen, USA) according to the manufacturer's instructions. The isolated PCR DNA fragment was then ligated to the SacII-NotI digested and purified pMOL944. The ligation was performed overnight at 16°C using 0.5 ^g of each DNA fragment, 1 U of T4 DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany). The ligation mixture was used to transform competent B.subtilis PL2306. The transformed cells were plated onto LBPG-10 /xg/ml of Kanamycin-agar plates. After 18 hours incubation at 37°C colonies were seen on plates. Several clones were analyzed by isolating piasmid DNA from overnight culture broth. One such positive clone was restreaked several times on agar plates as used above, this clone was called MB643. The clone MB643 was grown overnight in TY-10/ig/mi Kanamycin at 37°C, and next day 1 ml of cells were used to isolate piasmid from the cells using the Qiaprep Spin Piasmid Miniprep Kit #27106 accord¬ing to the manufacturers recommendations for B.subtilis piasmid preparations. This DNA was BNA sequenced and revealed the DNA sequence corresponding tc the mature part of the mannanase position 317-16S3 in SEQ ID NO. 1 and 33-453 in the SEQ ID NO. 2 . The clone M3643 was grown in 25 x 200 ml BPX media with 10 /jg/ml of Kanamycir. in 500 ml two baffled shakeflasks for 5 days at 37°C at 300 rpm. The DNA sequence encoding the C-tsrminal domain of unknown function from amine acid residue no. 341 to amino acid residue , no. 49C shows high homology tc a domain denoted X18 from a known mannanase. This X16 is found in EKEL entry AB007123 from: Yoshida S., Sake Y. , Uchida A.: "Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for an enzyme from Bacillus circuians K-l that degrades guar gum" in Biosci. ■ Biotechnol. Biochem. 62:514-520 (1998;. This gene codes for the signal peptide (aa 1-34), the catalytic core of a family 5 mannanase (aa 35-335), a linker (aa 336-352) and finally the X18 domain cf unknown function (aa 363-516}. This X1S domain is also found in Bacillus subtilis beta-mannanase Swiss protein database entry P55278 which discloses a gene coding for a signal peptide (aa 1-2 6;, a catalytic core family 26 mannanase (aa 27-360) and this X18 protein domain cf unknown function (aa 361-513); (Cloning and sequencing of beta-mannanase gene from Bacillus subtilis NM-3 9, Mendoza NS ; Arai M ; Sugimoto K ; Ueda N ; Kawaguchi T ; Joson LH , Fhillippmes. In Biochiir.ica Et Eiophysica Acta Vol. 1243, No. 3 pp. 552-554 (1995)). EXAMPLE 2 Expression, purification and characterisation of mannanase from Bacillus sp. 1633 The clone MB748 obtained as described in Example 1 and un¬der Materials and Methods was grown in 25 x 200rr,i BPX media wit?. 10 pg/ml of Kar.amycin in 500ir.l two baffled shakefiasks for 5 days at 37°C at 300 rpm. 4500 ml of the shake flask culture fluid cf the clone M5743 was collected and pK was adjuste'd to 5.6. 100 ml of catior.ic agent (102o C5211 and rSO ml of anionic agent (A130) was added during agitation, for fIccculation, The flocculated material was separated by centrifugation using a Sorval RC 3B centrifuge at 9000 rpm for 20 IT.in at 6°C. The supernatant was clarified using Whatman glass filters GF/D and C and finally concentrated on a filtron with a cut off of 10 kDa. 7CQ mi cfi this concentrate was adjusted to pK 7.5 using so¬dium, hydroxide. The clear solution was applied to anion-exchange chromatography using a 1000 ml Q-Sepharose column equilibrated with 50 mmol Tris pK ".5. The mannanase activity bound was eluted in 1100ml using a sodium chloride gradient. This was concentrated to 440 ml using a Filtron membrane. For obtaining highly pure mannanase the concentrate was passed over a Superdex 200column equilibrated with 0.1M sodium acetate, pK 6.C. The pure enzyme gave a single band in SDS-PAGE with a mo¬lecular weight of 34 kDa. Steady state kinetic using locus' bean gum: The assay was carried out using different amounts of the substrate locust bean gum, incubating for 20 min at 40CC at pH 10 in 0.1 M Glycine buffer, followed by the determination cf formation of reducing sugars. Glucose was used as standard for calculation of micromole formation of reducing sugar during steady state. The following data was obtained for the highly purified mannanase of the invention: KCat cf 467 per sac with a scancarc deviation oi 12; kM of 0."? with a standard deviation of 0.C7, The computer program grafit by Leatherbarrow frcrr. Erithacus Software U.K. was used for calculations. Reducing sugar was determined using the ?H3AH method (Lever, M. (1972', A new reaction for colormetric determination cf carbohydrates. Anal. Biochem. 47, 273-279.i The following N-cerminal sequence cf the purified protein was determined: ANSGFYV3GTTL"jfDAHG. Stability; The mannanase was fully stable between pH €.C and 11 after incubation for 2 cays at room temperature. The enzyme precipitated at low pH. The pH activity profile shows that the enzyme is more than 60% active between pH 7.5 and pH 10. Temperature optimum was found to be 50°C at pH 1C. DSC differential scanning calometry gave 6£°C as melting point at pH 6.0 in sodium acetate buffer indicating that this mannanase enzyme is thermostable. Immunological properties; Rabbit polyclonal monospecific serum was raised against the highly purified cloned mannanase using conventional techniques at the Danish company DAKO. The serum formed a nice single precipitate in agarose gels with the crude nor, purified mannanase of the invention. EXAMPLE 3 Use of the enzyme of example 2 in detergents Using commercial detergents instead of buffer and incuba¬tion for 20 minutes at 4 0°C with 0.2% AZCL-Galactomanr.sn (Megazyme, Australia) from carcb degree as described above followed by determination o£ the formation of blue color, the enzyme obtained as described in example 2 was active in European powder detergent Ariel Futur with 60% relative activity, Euro- pean liquid detergent Ariel Futur with 80% relative activitv, in US Tide powder with 45% relative activity and in US Tide licuid detergent with 57% relative activity to the activity measured in Glycine buffer. In these tests, the detergent concentration was as recommended on the commercial detergent packages ar.d. the wasr. water was tap water having 18 degrees German hardness under European (Ariel Futur; conditions and 9 degree under US condi¬tions (US Tide;. EXAMPLE 4 Construction and expression of fusion protein between the man-nanase of Bacillus sp. 1633 (example 1 and 2) and a cellulose binding domain (CBO) The CED encoding DNA sequence of the CipE gene from Clostridium thermocellum strain YS (Poole D M; Morsg E; Lamed R; Bayer £A; Haziewood GP; Gilbert HJ (1992S Identification of the cellulose-binding domain of the cellulosome subunit 51 from Clostridium thermocellum YS, Ferns Microbiology Letters Vol. 78 , No. 2-3 pp. 181-186 had previously been introduced to a vector pMOL1578. Chromosomal DNA encoding the CBD can be'obtained as described in Poole DM; Mcrag E; Lamed R; Bayer EA; Hazlewood GP Gilbert HJ (1992) Identification of the cellulose-binding domain of the cellulosome subunit SI from Clostridium thermocellum Y3, Ferns Microbiology Letters Vol. 78 , No. 2-3 pp. 181-186. A DNA sample encoding the CBD was used as template in a PCR and the C3D was cloned in an apprpopriate piasmid pMB993 based on the pMOL944 vector. The pMB993 vector contains the CipB CBD with a peptide linker preceeding the CBD. The linker consists of the following peptide sequence ASPEPTPEPT and is directly followed by the CipB CBD. The AS amincacids are derived from the DNA sequence that constitute the Restriction Er.dcnuclease site Nhel, which ir. tne following is used to clone the mannanse of one invention. Mannanase.Upper.SacII 5'-CAT TCT GCA GCC GCG GCA AAT TCC GGA TTT TAT GTA AGO GG -3' Mannanase.Lower.Nhel 5'-CAT CAT GCT AGC TCT AAA AAC GGT GCT TAA TCT CG -3' Restriction sites Nhel and SacII are underlined. Chromosomal DMA isolated from Bacillus sp. 1633 as described above was used as template in a PCR reaction using Amclitac DKA Polymerase (perkin Elmer) according to manufacturers instructions. The PCR reaction was set up in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 rnW MgCl2, 0.01 % {w/v} gelatin; containing 200 u!^ of each dNTP, 2.5 units of AmpliTaq polymerase (Perkin-Eimer, Cetus, USA) and 10C pmol of each primer. The PCR reactions was performed using a DNA thermal cycler (Landgraf, Germany). One incubation at 943C for 1 rein followed by thirty cycles of PCR performed using a cycle profile of denaturaticr. at 94°C for 30 sec, annealing at 60~C for 1 rr.in, and extension at 72 °C for 2 min. Five-ul aliquots of ohe ampli¬fication product was analysed by electrophoresis in C.7 % agarose gels (NuSieve, FMC). The appearance of a DNA fragment size 0.9 kb indicated proper amplification of the gene segment. Subcloning of PCR fragment: Fortyfive-pl aiiqucts of the PCR products generated as described above were purified using QIAquick PCR purification kit IQiagen, USA) according to the manufacturer's instructions. The purified DNA was eluted in 50 pi of 10mM Tris-HCl, pH 8.5. pg of pMB993 and twentyfive-ui of the purifies PCR fragment: i was digested with SacII anc Nhel, electrophoresed in 0.7 % low gelling temperature agarose (SesPlaque GTG, FMC) gels, the relevant fragments were excised from tne gels, and purified using QIAquick Gel extraction Kit (Qiage.n, USA) according to the manufacturer's instructions. The isolated PCP, DNA fragment was then ligated to the SacII-Nhel digested and purified pM3993. The ligation was performed overnight at 1 6°C using 0.5 ]ig of each DNA fragment, 1 U of T4 DNA ligase and 14 ligsse buffer (Boehringer Mannheim, Germany). The ligation mixture was used to transform competent B.subtilis PL2306. The transformed cells were plated onto LB?G-10 ng/ml of Kanamycin-agar plates. After 18 hours incubation at 37DC colonies were seen on plates. Several clones were analyzed by isolating piasmid DMA from overnight culture broth. One such positive clone was restreaked several times or. agar plates as used above, this clone was called MB1Q14; The clone MB1014 was grown overnight in Ty-10ug/mi Kanamycin at -37°C, and next day 1 ml of cells were used to isolate piasmid from the cells using the Qiaprep Spin Piasmid Miniprep Kit #27106 according to the manufacturers recommendations for B.subtilis piasmid preparations. This DNA was DNA sequenced and revealed the DNA sequen.ce corresponding to the mature part of the Mannanase-linker-cbd as represented in SEQ ID NO:3 and in the appended protein sequence SEQ ID NO: 4. Thus the final construction contains the following expression relevant elements: (amyL-promoter)-(amyL-signalpeptide)-mannanase-linker-CBD. Expression and detection of mannanase-CBD fusion protein MB1014 was incubated for 20 hours in TY-medium at 37°C and 250 rpm. 1 rr.l of cell-free supernatant was mixed with 200 \il of 10% Avicel- (Merck, Darmstadt, Germany) in Kiilipore H2G. The mixture was left for h. hour incubation at 0°C. After -his bind¬ing of BXM2-Linker-CBD fusion protein tc Avicel the Avicel with bound protein was spun 5 min at 5000g. The pellet was resus-pended in ICO ui of SD3-page buffer, boiled at 95°C for 5 min, spun at 5000g for 5 min and 25 ul was loaded or. a 4-20% Laemmli Tris-Glycine, SDS-PAGE HOVEX gel (Novex, USA). The samples were electrophoresed in a KGell™ Mini-Cell (NQVEX, USA) as recom¬mended by the manufacturer, ail subsequent handling of gels including staining with comassie, destaining and drying were performed as described by the manufacturer. The appearance c: a protein band of appro:. 53 kDa, verified the expression in B.subtilis of the full length Man-nanase-Linker-CBD fusion encoded on the plasmid pME1014. EXAMPLE 5 Mannanase derived from Bacillus agaradhaeretis Cloning of the mannanase gene from Bacillus agaradheren-s Genomic DNA preparation Strain Bacillus agaradherens NCIMB 40482 was propagated in liquid medium as described in WO94/01532. After 16 hours incuba¬tion at 30°C and 300 rpm, the cells were harvested, and genomic DNA isolated by the method described by Pitcher et al. (Pitcher, D. G., Saunders, N. A., Owen, R. J. (19B9). Rapid extraction of 'bacterial genomic DNA with guanidium thiocyanate. Lett. Appl. Microbiol., 8, 151-156;. Genomic library construction Genomic DNA was par-ially digested with restriction enzyme Sau3A, and size-fractionated by electrophoresis on a 0. "7 % agarose gel. Fragments between 2 and 7 kb in size was isolated by electrophoresis onto DEAE,-cellulose paper (Dretzen, G., Beliard, M. , Sassone- :orsi, P., Chamber., ?. (1961) A reliable method for the recovery cf DNA fragments from agarose ar.d acrv-lamide gels. Anal. Eiochem., 112, 295-298). Isolated DNA fragments were ligated to BamKi"digested pSJ1678 plasrr.id DNA, and the ligation mixture was used to trans¬form E. coli SJ2. Identification of positive clones A DNA library in £. coli, constructed as described above, was screened on LB agar plates containing 0.2% AZ.CL-galactomannan (Megazyme) and 9 ug/ml Chloramphenicol and incu¬bated overnight at 37°C. Clones expressing mannanase activity appeared with blue diffusion halos. Plasmid DNA from one cf these clone was isolated by Qiagen plasmid spin preps on 1 ml of overnight culture broth (cells incubated at 37°C in TY with 9 ug/ml Chloramphenicol and shaking at 25D rpm!. This clone (MB525) was further characterized by DMA se¬quencing of the cloned 5au3A DNA fragment. DMA sequencing was carried out by primerwalking, using the Taq deoxy-termir.al cycle sequencing kit (Perkin-Elmer, USA], fluorescent labelled termi¬nators and appropriate oligonucleotides as primers. Analysis of the sequence data was performed according to Devereux et al. (1984) Nucleic Acids Res. 12, 387-395. The sequence encoding the mannanase is shown in SEQ ID Ho 5. The derived protein seauence is shown in SEQ ID No.6. Subcloning and expression of B. agraradhaerens mannanase in B.subtills The mannanase encoding DNA sequence of the invention was PCR amplified using the PCR primer set consisting of these two oligo nucleotides: Mannanas-e.upper.SacII 5'-CAT TCT GCA GCG GCG GCA GCA AGT ACA GGC TTT TAT GTT GAT GG-3' Mannanase.lower.Hot I f 5'-GAC GAG GTA CAA GCG GCC GCG CTA TTT CCC TAA CAT GAT GAT ATT TTC G -3' Restriction sites SacII and NotII are underlined. Chromosomal DNA isolated from B.agaradherens NCIMB 40432 as described above was used as template in a PCR reaction using Amplitaq DNA Polymerase (Perkin Elmer) according to manufacturers instructions. The PCR reaction was set up in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KCI, 1.5 mM MgCl:, 0.01 s= (w/v) gelatin) containing 200 uM of each dNTP, 2.5 units of AmpliTaq polymerase (Perkin-Elmer, Cetus, USA) and 100 pniol of each primer. The PCR reaction was performed using a DMA thermal cycler (Landgraf, Germany). One incubation at 94°C for 1 min followed by thirty cycles of PCR performed using a cycle profile of denaturation at 94CC for 30 sec, annealing st 60"C for 1 min, and extension at 72°C for 2 min. Five-ui aliquots of the ampli¬fication product was analysed by electrophoresis in 0.7 % agarose gels (NuSieve, FMC). The appearance of a DNA fragment size 1.4 kb indicated proper amplification of the gene segment. Subcloning of PCR fragment Fortyfive-pl aliquots of the PCR products generated as described above were purified using QIAquick PCR purification kit (Qiagen, USA) according to the manufacturer's instructions. The purified DftA was eluted in 50 pi of lOmM Tris-HCl, pH 8.5. 5 pg of pMOL94 4 and twentyfive-pl of the purified PCR fragment was digested with SacII and NotI, electrophoresed in 0.8% low gelling temperature agarose (SeaPlaque GTG, FMC) gels, the relevant fragments were excised from the gels, and purified using QIAquick Gel extraction Kit (Qiagen, USA; according to tr.e manufacturer's instructions. The isolated ?CR DNA fragment was then ligated to the SacII-Notl digested and purified pMOL944. The ligation was performed overnight at I6°C using 0.5ug of each DNA fragment, 1 U of ?4 DNA Iigase and T4 ligase buffer (Boehringer Mannheim, Germany) . The ligation mixture was used to transform competent B.subtilis PL2306. The transformed cells were plated onto LBPG-10 ug/ml of Kanamycin plates. After 18 hours incubation at 37°C colonies were seen on plates. Several clones were'analysed by isolating plasrald DNA from overnight culture broth. One such positive clone was restreaked several times on agar plates as used above, this clone was called MB594. The . clone MB594 was grown overnight in TY-10 ug/ml kanamycin at 37°C, and next day 1 ml of ceils were used to isolate piasmid from the cells using the Qiaprep Spin Piasmid Miniprep Kit #27106 according to the manufacturers recommendations for B.subtilis piasmid preparations. This DNA was DNA sequenced and revealed the DNA sequence corresponding to the mature part of the marmanase, i.e. positions 94-1404 of the appended SEQ ID NO:1. The derived mature protein is shown in SEQ ID NO:8. It will appear that the 3' end of the mannanse encoded by the sequence of SEQ ID NO:5 was changed to the one shown in SEQ ID NO:7 due to the design of the lower primer used in the PCR. The resulting amino acid sequence is shown in SEQ ID NO:8 and it is apparent that the C terminus of the SEQ ID NO:6 (SHHVREIGVQFSAADNSSGQTALYVDNVTLR) is changed to the C terminus Of SEQ ID N0:8 (IIMLGK). EXAMPLE 6 Expression, purification, and characterisation of niannanase from BaciJLlus agaradhaerens The clone ME 594 obtained as cescribec in example 5 was grown in 25 x 200ml EPX media with 10 ug/ml of Kanamycin in 500ml two baffled shakeflasks for 5 days at 37°C at 300 rpm. 6500 ml of the shake flask culture fluid cf the clone MB 594 {batch #9813) was collected and pH adjusted tc 5.5. 146 ml cf cationic agent (C521) and 292 ml of anionic agent fA13C' was added during agitation fcr flocculation. The flocculated mate¬rial was separated by centrifligation using a Sorvai RC 3E cen¬trifuge at 9000 rpm for 20 min at 6°C. The supernatant was clarified using Whatman glass filters GF/D and C and finally concentrated on a filtron with a cut off of 10 kDa, 750 ml of this concentrate was adjusted to pK 7.5 using so-j dium hydroxide. The clear solution was applied to anicr.-exchange chromatography using a 9C0 ml Q-Sepharose column equilibrated with 50 mmol Tris pH 7.5. The mannanase activity bound was eluted using a sodium chloride gradient. The pure enzyme gave a single band in SDS-P.AGE with a molecular weight of 38 kDa. The amino acid sequence of the mannanase enzyme, i.e. the translated DNA sequence, is shown in SEQ ID No.6. Determination of kinetic constants: Substrate: Locust bean gum (carob) and reducing sugar analysis (PHBAH). Locust bean gum from Sigma (G-0753). Kinetic determination using different concentrations cf lo¬cust bean gum and incubation for 20 min at 4C°C at pH 10 gave Kcat: 467 per sec. PL,: 0.08 gram per 1 MW: 38kDa pi (isoelectric point): 4.2 The temperature optimum cf the irannanase was found to be. 60QC. The pK activity profile showed maximum activity beoween pH 8 and 10. DSC differential scanning caiometry gives 77aC as melting point at pH 7.5 ir. Tris buffer indicating that this enzyrce is very termostable. Detergent compatibility using 0.2% AZCL-Galaccomannar. from carcb as substrare and incubation as described above ac 40°C 1 shows excellent compaoility with conventional liquid detergents and good compatility with conventional powder detergents. EXAMPLE 1 Use of the enzyme of the invention in detergents The purified enzyme obtained as described in example 6 (batch #9313) showed improved cleaning performance when tested at a level of I ppm in a mini wash test using, a conventional commercial liquid deoerqent. The test was carried out under conventional North American wash conditions. EXAMPLE 8 Mannanase derived from Bacillus sp. AAI12 Construction of a genomic library from Bacillus sp. AAI12 Genomic DK'A of Bacillus sp. was partially digested with restriction enzyme Sau3A, and size-fractionated by elec¬trophoresis on a 0.7 % agarose gel (SeaKem agarose, FMC, USA). Fragments between 1.5 and 10 kb in size were isolated and con¬centrated to a DMA bar.d by running the DMA fragments backwards :>n a 1.5 % agarose gel followed by extraction of the fragments from the agarose gel slice using the Qiaquick gel extraction kit according to the manufacturer's instructions (Qiagen Inc., USA). To construct a genomic iiorary, ca. lOOr.q o: purified, fraction¬ated DNA from, above was iiqated with 1 ug of SamHl -cleaved, dephosphorylatec lambdaZAPe.xpress vector arms (Stratagene, La Jolla CA, USA) fcr 24 hours a: t ^ °c according to the manufac-i turer's instructions. A 3-ul aliquot of the ligation mixture was packaged directly using the GigaPacklll Gold packaging extract (Stratagene, USA; according to the manufacturers instructions (Stratagene). The genomic lambdaZAPExpress phage library was titered using the E. coii XLl-Blue MRF- strain from Stratagene (La Jolla, USA) . The unamplified genomic library coitprisec o: 7.8 x 10^ plague-forming units (pfu) with a vector background of less than i %. Screening for beta-mannanase clones by functional expression in lambdaZAPExpress Approximately 500C plaque-forming units (pfu) from the genomic library were plated on NZY-agar plates containing C.l % AZCL-galactomannan (MegaZyme, Australia, cat. no. I-AZGMA;, using E. coli XLl-Blue MRF' (Stratagene, USA) as a host, fol¬lowed by incubation of the plates at 37 °C for 24 hours. Man-nanase-positive lambda clones were identified by the formation of blue hydrolysis halos around the positive phage clones. These were recovered from the screening plates by coring the TOF-agar slices containing the plaques of interest into 500 ul of £M buffer and 20 ul of chloroform. The mannanase-positive lamb¬daZAPExpress clones were plaque-purified by plating an aliquot of the cored phage stock on NZY plates containing 0.1 % A2C1-galactomannan as above. Single, mannanase-positive lambda ciones were cored into 500 ul of SM buffer and 2C ul of chloroform, and purified by one more plating -round as described above. Single-clone in vivo excision of the phagemids from the man-nanase-positive lambdaZAPExpress clones £. coli XLl-BIue cells ;Stratagene, La Jolla Ca. .■ were prepared ar.d resuspended in lOrruM MgS04 as recommended by Stratagene (La Jolla, USA). 250-ul aliquots of the cure phage stocks frora the rr.annase-positive clones were combined in Falcon 2059 tubes with 200uls of XLl-Blue MRF' cells (OD60C=1.0; and > 106 pfus/ml of the ExAssist M13 helper phage (Stratagene) , and the mixtures were incubated at 37 C for 15 ninutes. Three mis of KZY broth was added to each tube and the tubes were ir.cubs-ed at 37 C for 2.5 hours. The tubes were heated at 65 C for 20 minutes to kill the E. ccli cells and bacteriophage lambda; the phagemids being resistant to heating. The tubes were spun at 3000 rpm for 15 minutes to remove cellular debris and the super-natants were decanted into clean Falcon 2059 tubes. Aliquots of the supernatants containing the excised single-stranded phagemids were used to infect 200uls of E. coli XLOLR ceils (Stratagene, OD600=1.0 in lOmM MgS04) by incubation at 37°C for 15 minutes. 35Quls cf NZY broth was added to the cells and the ) tubes were incubated for 45 min at 37°C, Aliquots of the cells were plated onto LB kanamycin agar plates and incubated fcr 24 hours at 37DC. Five excised single colonies were re-streaked onto LB kanamycin agar plates containing 0.1 % A2CL-galactomannan (MegaZyme, Australia). The mannanase-positive phagemid clones were characterized by the formation of blue hydrolysis hales around the positive colonies. These were fur¬ther analysed by restriction enzyme digests cf the isolated plagemid DNA (QiaSpi.n kit, Qiagen, USA) with EcoRI, PstI, EcoRI-Pstl, and HindiII followed by agarose gel electrophoresis. Nucleotide sequence analysis Trie r,ucie;:;oe sequence c; the genomic beta-1, 4-mannanase clone pBXMl was deterrti.nee from bctr. strands by the dideoxy chain-termination method (Sanger, F. , Nickle.n, S., and Couiscn, A. R. (1977) Pre-. Nati. Acac. 3ci. 0. 3. A. 74, 5463-5467} ! using 500 ng cf Qiagsr.-purified template (Qiagen, USA), the Taq deoxy-terminai cycle sequencing kit {Perkin-Elmer, US?.;, fluo¬rescent labeled terminators and 5 pmol of either pEK-CMV poiyiinker primers (Stratagene, USA) or synthecic'oligonucleo¬tide primers. Analysis cf the sequence data was performed ac¬cording to Bevereux et al., 1984 (Devereux, J., Haeberli, P., and Smithies, C. (1984; Nucleic Acids Res. 12, 367-395). Sequence alignment A multiple sequence alignment of the glycohydrclass family 26 beta-1, 4-mar.r.sr,3ses frcm Bacillus sp. AAI 12 cf the present invention (ie SEQ ID NC: 10), Caldicallulcsirvptor saccharolyticus (GenBenk/EMEL accession no. P77S47), Diczyoglomus therxicphilum (ace. no. 030654) , Rhodothermus mazinus (ace. r.c. P4S425), Bircmycas sp. encoded by ManA (ace. no. P55296), Bacillus sp. (ace. no. P91007), Bacillus subvilis (ace. nc. O055I2) and Fsaudcmonas fluoresceins (ace. no F49424. was created using the FiieUp program of the GCG Wisconsin software package,version 8.1. (see above); with gap creation penalty 3.00 and gap extension penalty 0.10. Sequence Similarities The deduced amine acid sequence cf the family 26 beta-1,4-mannanase of the invention cloned from Bacillus sp. AAI 12 shows 45 % sequence similarity and 19.8 % sequence identity to the beta-1,4-mannanase frcm Caldicallulosiruptor saccharolyticus (GenBank/EM3L accession no. P77847), 49 % similarity and 25.1. % identity to the beta-1, 4-mar.r.anase from DiczyoglcTUs thermophilic^ (sec. nc, 030654), 48.2 % similarity and 26.3 % identity to the beta-1, 4 -mar.r.anase from RinodJtherrnus xarinus (ace. no. P49425), 4o % similarity and 19.5 % sequence identity to the ManA-encoded bsta-1, 4-ma.nnanase from Piromyces sp. [azc. nc. P55296), 47.2 % similarity and 22 % identity to the beta-1,4-mannanase from Bacillus sp. (ace. no. £91007}, 52.4 % similarity and 27.5 % sequence identity to the beta-1,4-mannanase frorr. Bacillus subtilis (ace. no. 005512) and 60.6 % similarity and 37.4 I identity to the beta-1,4-mannanase from Ps&udomonas fluorescer.s (ace. no P49424. The sequences were aligned using the GAP program cf the GCG Wisconsin software package,version 8.1.; with gap creation penalty 3.00 and gap extension penalty 0.10. Cloning of the Bacillus sp (AA.I 12) mannanase gene Subcloninq and expression of mannanase in E.subtilis The mannanase encoding DNA sequence of the invention was PCR amplified using the PCR primer set consisting of these two oligo nucleotides: BXM1.upper.SacII 5'- CAT TCT GCA GCC GCG GCA TTT TCT GGA AGC GTT TCA GC-3' BXM1.lower.NotI 5'-CAG CAG TAG CGG CCG CCA CTT CCT GCT GGT ACA TAT GC -3' Restriction sites SacII and NotI are underlined. Chromosomal DNA isolated from Bacillus sp. AAI 12 as described above was used as template in a PCR reaction using Amplitaq DNA Polymerase (Perkin Elmer) according to manufacturers instructions. The PCR reaction was set up in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 mM -MgCl2, 0.01 % (w/v) gelatin) containing 200 uM of each dNTP, 2.5 units of AmpliTac polymerase (Perkin-Elmer, Cetus, USA) and 100 pmci cf each primer. The PC? reactions was performed using a DMA thermal cycler (Landgraf, Germany!. One incubation at 94CC for I min followed by thirty cycles of PCR performed using a cycle profile of denaturation at 94'C for 30 sec, annealing at 6C=C for 1 rr.in, and extension at 72 QC for 2 min. Five-pl aliquots cf the ampli¬fication product: was analysed by electrophoresis in 0.7 % agarose gels (NuSieve, FMC). The appearance of a DKA fragment size 1.0 kb indicated proper amplification of the gene segment. Subcloning of PCR fragment Fortyfive-pl aliquots of the PCR products generated as described above were purified using QIAquick PCR purification kit (Qiagen, USA) according to the manufacturer's instructions. The purified DNA was eluted in 50 ul of lOmM Tris-HCl, pH 3.5. 5 pg of-pMOL944 and twentyfive-pl of the purified PCR fragment was digested with SacII and NotI, electrophoresed in 0.8 % low gelling temperature agarose (SeaPlaque GTG, FMC) gels, the relevant fragments were excised from the gels, and purified using QIAquick Gel extraction Kit (Qiagen, USA) according to the manufacturer's instructions. The isolated PCR DNA fragment was then ligated to the SacII-NotI digested and purified pMOL944. The ligation was performed overnight at 16aC using C.5 pg of each DNA fragment, 1 U of T4 DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany). The ligation mixture was used to transform competent B.subtilis PL2306. The transformed cells were plated onto LBPG-10 pg/ml of Kanamycin-agar plates. After 18 hours incubation at 37°C colonies were seen on plates. Several clones were analyzed by isolating plasmid DNA from overnight culture broth. One such positive clone was restreaked several times or. agar plates as used above, this clone was called MB747. The clone MB747 was grown overnight in TY-lOug/ml Kanamycin at 37°C, and nex: day 1 ml of cells were used to isolate plasmid from the cells using the Qiaprep Spin Plasmid Miniprep Kit #27106 accord¬ing to the manufacturers recommendations for 3.subtilis plasmid preparations. This DNA'was DNA sequenced and revealed the DNA sequence corresponding to the mature part of the mannanase in the SEQ ID NO. 9. Expression, purification and characterisation of mannanase from Bacillus sp. AAI 12 The clone MB747 obtained as described above was grown in 25 x 200mi 3PX media with 10 ug/ml of Kanamycin in 500ml two baf¬fled shakeflasks for 5 days at 37°C at 300 rpm. 41 CO ml of the shake flask culture fluid of the clone MB747 was collected, pH was adjusted to 7.0, and EDTA was added to a final concentration of 2mM. 185 ml of caticnic agent (10% C521) and 370 ml of anionic agent (A130) was added during agitation for flocculation. The flocculated material was separated by centrifugation using a Sorval RC 3B centrifuge at 900C rpm for 20 min at 6°C. The supernatant was clarified using Whatman glass filters GF/D and C and finally concentrated on a filtron with a cut off of 10 kDa. 1500 mi of this concentrate was adjusted to pH 7.5 using sodium hydroxide. The clear solution was applied to anion-exchange chromatography using a 1000 ml Q-Sepharose column equilibrated with 25 mmol Tris pH 7.5. The mannanase activity bound was eluted in 1100ml using a sodium chloride gradient. This was concentrated to 440 ml using a Filtron membrane. For obtaining highly pure mannanase the concentrate was passed over a Superdex column equilibrated with 0.1M sodium acetate, pH 6.0. The pure er. syne gave a single band in SDS-?AGE with a mo¬lecular weight cr 62 k.Da. The amino acid sequence of the mannanase enzyme, i.e. the translated DNA sequence, is shown in SEQ 13 Mc.10. The following H-terminal sequence was deternined: F3GSVSASGQELK.VT0QM. pi (isoelectric point): 4.5 DSC differential scanning calcmetry gave 64 °C as melting point at pH 6.0 in sodium acetate buffer indicating that this rr.annanase enzyme is thermostable. It was found that the catalytic activity increases with ionic strength indicating that the specific activity of the enzyme may be increased by using salt of phosphate buffer witn high ionic strength. The mannanase activity of the polypeptide of the invention is inhibited by calcium ions. Immunological properties: Rabbit polyclonal monospecific serum-was raised against the highly purified mannanase of the inven¬tion using conventional techniques at the Danish company DAKO. The serum formed a nice single precipitate in agarose gels with the crude mannanase of the invention. EXAMPLE 9 Use of the enzyme of example 8 in detergents Using commercial detergents instead of buffer and incuba¬tion for 20 minutes at 40°C with 0.2% AZCL-Galactomannar. (Megazyme, Australia) from carob degree as described above followed by determination of the formation of blue color, the enzyme obtained as described in example 8 was active in European powder detergent Ariel Futur with 132% relative activity, in US Tide powder with 108% relative activity and in US Tide liquid detergent with 86% relative activity to the activity measured in Glycine buffer. In these tests, the detergent concentration was as recommended on the commercial detergent packages ar.d tne wash water was tap water having 13 degrees German hardness under European (Ariel Futur) conditions and 5 degree under US condi¬tions (US Tide). EXAMPLE 10 Mannanase derived from Bacillus halodurans Construction of a genomic library from Bacillus halodurans in the pSJ167 8 vector Genomic DNA of Bacillus halodurans was partially digested with restriction enzyme 5au3A, and size-fractionated by elec¬trophoresis on a 0.7 % agarose gel (SeaKem agarose, FMC, USA}. DNA fragments between 2 and 10 kb in size was isolated by elec¬trophoresis onto DEAE-cellulose paper {Dretzen, G., Bellard, M., Sassone-Corsi, P., Chambon, P. (1981) A reliable method for the recovery of DNA fragments from agarose and acrylamide gels. Anal. Biochem., 112, 295-298}. Isolated DNA fragments were ligated to BamHI-digested pSJ1678 plasmid DNA, and the ligation mixture was used to transform E. coli SJ2. Screening for beta-maimana.se clones by functional expression in Escherichia coli Approximately 10.000 colony-forming units (cfu) from the genomic library were plated on LB-agar plates containing con¬taining 9 /xg/ml chloramphenicol and 0.1 % ASCL-galactomannan .(MegaZyme, Australia, cat. no. I-AZGMA), using E. coli SJ2 as a host, followed by incubation of the plates at 37°C for 24 hours. Mannanase-positive E. coli colonies were identified by the formation of blue hydrolysis halos around the positive plasmid clones. The mannanase-positive clones in pSJISTS were cclonv-purified by re-streaking the isolated colonies on LB plates containing 9 ^g/ml Chloramphenicol and 0.1 % AZCL-galactotnannar. as above. Single, mannanase-positive plasmid clones were inocu-l lated into 5 ml of LE medium containing containing 9 ^g/ml Chloramphenicol, for purification cf the plasmid DNA. Nucleotide sequence analysis The nucleotide sequence of the genomic beta-l,4-mannanase clone pBXM5 was determined from both strands by the dideoxy chain-termination method (Sanger, F-, Nicklen, S., and Coulson, A. R. (1977) Proc. Natl. Acad. Sci. U. S. A. 74, 5463-5467) using 500 ng of Qiagen-purified template (Qiagen, USA}, the Taq deoxy-terminal cycle sequencing kit (Perkin-Elmer, USA), fluo¬rescent labeled terminators and 5 prnol of either pBK-CMV polylinker primers (Stratagene, USA) or synthetic oligonucleo¬tide primers. Analysis of the sequence data was performed ac¬cording to Devereux et al., 19B4 (Devereux, J., Haeberli, P., and Smithies, 0. (1984) Nucleic Acids Res. 12, 387-395). Sequence alignment A multiple sequence alignment of the glycohydrolase family 5 beta-l,4-mannanase from Bacillus halodurans of the present invention (ie SEQ ID N0-.12), Bacillus circulans (GenBank/EMEL accession no. 066185), Vibrio sp. (ace. no. OS9347), Streptomyces lividans (ace. no. P51529), and Caldicellulosiruptor saccharolyticus (ace. no. P22533). The multiple sequence alignment was created using the PileUp program of the GCG Wisconsin software package,version 8.1.; with gap creation penalty 3.00 and gap extension penalty 0.10. Sequence Similarities The deduced amino acid sequence of the family 5 beta-l,4-mannanase of the present invention cloned from Bacillus halodurans shows 77% similarity and 60% sequence identity to the I beta-l,4-mannanase of Bacillus circulans (GenBank/EMBL accession no. 066185), 64.2% similarity and 46% identity to the beta-l,4-mannanase from Vibrio sp. (ace. no. 069347), 63% similarity and 41.8% identity to the beta-l,4-mannanase from Streptomyces lividans (ace. no. P51529), 60.3% similarity and 42% sequence identity to the beta-l,4-mannanase from CaJdicelluIosiruptcr saccharolyticus {ace. no. P2253). The sequences were aligned using the GAP program of the GCG Wisconsin software package,version 8.1.; with gap creation penalty 3.00 and gap extension penalty 0.10. Cloning of Bacillus h&lodurans mannanase gene Subclor.ina and expression of mature full length mannanase in The mannanase encoding DNA sequence of the invention was PCR amplified using the PCR primer set consisting of these two oligo nucleotides: BXM5.upper-Sacli 5'-CAT TCT GCA GCC GCG GCA CAT CAC AGT GGG TTC CAT G-3' BXM5.lower.NotI 5l-GCG TTG AGA CGC GCG GCC GCT TAT TGA AAC ACA CTG CTT CTT TTA G-3* Restriction sites SacII and NotI are underlined Chromosomal DMA isolated from Bacillus halodurans as described above was used as template in a PCR reaction using Amplitaq DNA Polymerase (Perkin Elmer) according to manufacturers instructions. The PCR reaction was set ur: in PCR buffer (10 mM Tris-HCi, pK B.3, SO mM KCI, 1.5 mM MgCl2, C.01 % (w/v) gelatin} containing 200 /JM of each dNTP, 2.5 units cf \ AmpliTaq polymerase (Perkm-Elmer, Cetus, USA) ar.c IOC pmcl of each primer. The PCR reactions was performed using a DNA thermal cycler (Landgraf, Germany). One incubation at 94QC for 1 rain followed by thirty cycles of PCR performed using a cycle profile of denaturaticn at 94aC for 30 sec, an-nea-ling a: 60°C for 1 min, and extension at 72°C for 2 min. Five-/il aiiquocs cf the ampli-fication product was analysed by electrophoresis in C.7 % agarose gels (NuSieve, FMC). The appearance of a DNA fragment size 0.9 kb indicated proper amplification of the gene segment. Subcloninq of PCR fragment: Fortyfive-jil aiiquots of the PCR products generated as de¬scribed above were purified using QIA-quick PCR purification kit (Qiagen, USA) according tc the manufacturer's instructions. The purified D-NA was eluted in 50 fj.1 of lOmM Tris-HCl, pH 8.5. 5 fig of pMOL944 and twentyfive-fil of the purified PCS. frag¬ment was digested with SacII and NotI, electrophoreses in Q.8 % low gelling temperature agarose {SeaPla-que GTG, FMC) gels, the relevant fragments were excised from the gels, and purified using QIA-quick Gel extraction Kit (Qiagen, USA) according to the manufacturer's instructions. The isolated PCR DNA fragment was then ligated to the Sacll-Notl digested and purified pMOL944. The ligation was performed overnight at 16°C using 0.5 tig of each DNA fragment, 1 U of T4 DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany). The ligation mixture was used to transform competent B.subtilis PL2306. The transformed cells were plated onto LEPG- xv fig/ml of Ksnamycin-agar plates. After 18 hours incubacicn at 37°C colonies were seen on plates. Several clones were analyzed by isolating piasmid DNA from overnight culture broth. One such positive clone was restreaked several times on agar plates as used above, this clone was called MBS78. The clone MH678 was grown overnight in TY-lOfig/ml Kanamycin at 37°C, and next day 1 ml of cells were used to isolate plasmid from the cells using Che Qiaprep Spin Plasmid Miniprep Kit #27106 accord¬ing to the manufacturers recommendations for B.subtilis piasmid „ preparations. This DNA was DMA sequenced and revealed the DNA sequence corresponding to the mature part of the mar.nanase position 97-9S3 in SEQ ID NO. II and 33-331 in the SE2 ID NC. 12. i Expression, purification and characterisation of mannanase from Bacillus halodurans The clone MBS78 obtained as described above was grown in 25 x 200ml BPX media with 10 fig/ml of Kanamycin in 500ml two baf¬fled shakeflasks for 5 days at 37°C at 300 rpm. 5000 ml of the shake flask culture fluid of the clone MB878 was collected and pH was adjusted to 6.0. 125 ml of cationic agent (10% C521) and 250 ml cf anionic agent (A130) was added during agitation for flocculation. The flocculated material was separated by centrifugation using a Sorval RC 3B centrifuge at 9000 rpm for 20 min at 6°C. The supernatant was adjusted to pH 8.0 using NaOH and clarified using Whatman glass filters GF/D and C. Then 50 g of DEAE A-50 Sephadex was equilibrated with 0.1M Sodium acetate, pH S.0, and added to the filtrate, the enzyme was bound and left overnight at room temperature. The bound enzyme was eluted with 0.5 M KaCl in the acetate buffer. Then the pH was adjusted to pH 8.0 using sodium hydroxide and then concentrated on a Filtron with a 10 kDa cut off to 450 ml and then stabilized with 2C% glycerol, 20% MPG and 2% Beroi. The product was used for application trials. 2 ml of this concentrate was adjusted to pH 8.5 using so¬dium hydroxide. For obtaining highly pure mannanase the concen¬trate was passed over a Superdex column equilibrated with 0.1 M sodium phosphate, pH 3.5. The pure enzyme gave a single band in SDS-PAGE with a mo¬lecular weight of 34 kDa. The amino acid sequence of the mannanase enzyme, i.e. the translated DHA sequence, is shown in SEQ ID NO:12. The following H-terminal sequence cf the purified protein was determined: AHHSGFHVNGTTLYDA. The pH activity profile using the ManU assay (incubation for 20 minutes at 40DC} shows that the enzyme has a relative activity higher than 50% between pH 7.5 and pH 10. Temperature optimum was found (using the ManU assay; gly¬cine buffer) to be between 6Q°C and 7Q°C at pK 10. Immunological ,pro_perCies,: Rabbit polyclonal monospecific serum was raised against the highly purified cloned mannanase using conventional techniques at the Danish company DAKO. The serum formed a nice single precipitate in agarose gels with the crude non purified mannanase of the invention. EXAMPLE 11 Use of the mannanase enzyme of example 10 in detergents Using commercial detergents instead of buffer and incuba¬tion for 20 minutes at 40°C with 0.2% AZCL-Galactomannan (Megazyme, Australia) from carob degree as described above followed by determination of the formation of blue color, the mannanase enzyme obtained as described in example 10 was active with an activity higher than 40% relative to the activity in buffer in European liquid detergent Ariel Futur, in US Tide powder and in US Tide liquid detergent. In these tests, Che detergent concentration was as recommended on the commercial detergent packages and the wash water was tap water having 13 degrees German hardness under European (Ariel Futur) conditions S and 9 degree under US conditions (US Tide). EXAMPLE 12 Mannanase derived from Bacillus sp. AA349 Cloning of Bacillus sp (AA349) mannanase gene Subcloning and expression of a catalytic core manr.ar.age enzyme in B.subtilis: The mannanase encoding DNA sequence of the invention was PCR amplified using the PCR primer set consisting of the follow¬ing two oligo nucleotides: BXH7 .upper. Sad I 5'-CAT TCT GCA GCC GCG GCA AGT GGA CAT GGG CAA ATG C-3' BXM7.lower.NotI 5'-GCG TTG AGA CC-C GCG GCC GCT TAT TTT TTG TAT ACA CTA ACG ATT TC-3' Restriction sites SacII and NotI are underlined. Chromosomal DNA isolated from Bacillus sp. AA349 as described above was used as template in a PCR reaction using Mnpiitaq DNA Polymerase (perkin Elmer) according to Ttanufacxurers instructions. The PCR reaction was set up ir. PCR suffer (10 mM Tris-HCl, pH 8.3, 50 mM KC1, 1.5 mM MgCl;, 0.01 % (w/v) gelatin] containing 200 uM of each dNTP, 2.5 units cf MnpliTaq polymerase (Perkir.-Elmer, CetuS, USA) and 100 pmcl of ;ach primer. The PCR reactions was performed using a DNA thermal :ycler (Landgraf, Germany)- One incubation at 94°C for 1 min followed by ;r.i:-,y cycles cf PCR performed using a cycle profile of denaturaticr. at 94~C tor 30 sec, annealing at 60 Subcloning cf PCR fragment: Fortyfive-ul aliquots cf the PCR products generated as described above were purified using QIAquicic PCR purification kit (Qiagen, USA) according to the manufacturer's instructions. The purified DNA was eluted ir. 50 ul of lQmM Tris-HCl, pH 3.5. 5 ug of pM01944 and twentyfive-pl of the purified PCR fragment was digested with Sacll and NotI, electrophoresed in 0.3 % low gelling temperature agarose (SeaPlaque GTG, FMC) gels, the relevant fragments were excised from the gels, and purified using QlAquick Gel extraction Kit (Qiagen, USA) according to the manufacturer's instructions. Che isolated PCR DNA'fragment was then ligated to the Sacll-Nctl digested and purified pMOL944. The ligation was performed overnight at 16°C using 0.5 ug of each DNA fragment, 1 U of T4 DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany). The ligation mixture was used to transform competent E.subtilis PL2306. The transformed cells were plated cnto LBPG-10 ug/ml of Kanamycin-agar plates. After 13 hours incubation at 37°C colonies were seen on plates. Several clones were analyzed by isolating piasmid Dt-iA from overnight culture broth. One such positive clone was restreaked several times on .,_ agar plates as used above, this clone was called M3879. The clone MB879 was grown overnight in TY-lCpg/ml Kanamycin at 37°C, and next day 1 ml cf cells were used to isolate piasmid from, the cells using -,e QiaPrec Spin Plasma Kimprep Ki, *27106 accord¬ing to the manufacturers recommendations for R.sub;UiS plasnid preparations. This DMA was DMA. sequenced and reveaiea the DNA sequence corresponding to the mature part of the msnnanase (corresponding to positions 204-1107 in the appended DNA se¬quence SEQ ID N0:15 and positions 26-369 in the appenaed protein sequence SEQ ID NO:16. Expression, purification and characterisation of mannanase from Bacillus sp. AA349 The clone HE879 obtained as described above was grown in 25 x 200ml EPX media with 10 ug/ml of Kanamycin in 530ml two baf¬fled shakeflasks for 5 days at 37°C at 300 rpm. 400 ml of the shake flask culture fluid of the clone MB87S was collected and pH was 6.5. 19 ml of cationic agent (ic% C521) and 38 ml of anionic agent {A130) was added during agitation for flocculation. The flocculated material was separated by cer.-trifugation using a Sorval RC 3B centrifuge at 5000 rpm for 25 min at 6°C. The then concentrated and washed with water to ; reduce the conductivity on a Filtron with a 10 kDa cut off to ISO ml. then the pH was adjusted to 4.0 and the liquid applied to S-Sepharose column cromatography in a 50 mM Sodium acetete buffer pH 4.0. The column was first eluted with a NaCl gradient to 0.5 M then the mannase eluted using 0.1 M glycin buffer pK 10. The mannanase active fraction was pooled and they gave a single band in SDS-PAGE with a molecular weight of 38 kDa. The amino acid sequence of the mannanase enzyme, i.e. the translated DNA sequence, is shown in SEQ ID NO;16. The pH activity pyo^i^e using the ManU assay (incubation for 20 minutes at 40°C) shows that the enzyme has a relative activity higher than 30% between pH 5 and pH 10. Temperature .optimum was found (using the ManU assay; gly- cine buffer) to be between 60°C and 70°C at pH 10. Immmalagj,cal prnpp.rr^ Rabbit polyclonal monospecific serum was raised against the highly purified cloned mannanase using conventional techniques at the Danish company DAKO. The serum formed a nice single precipitate in agarose gels with the crude non purified mannanase of the invention. EXAMPLE 13 Use of the mannanase enzyme of example 12 in detergents Using commercial detergents instead of buffer and incuba¬tion for 20 minutes at 4C°C with 0.2% AZCL-Galactomannan (Megazyme, Australia■ from carob degree as described above followed by determination of the formation of blue color, the mannanase enzyme obtained as described in example 12 was active rfith an activity higher than 65% relative to the activity in suffer in European liquid detergent Ariel Futur and in US Tide liquid detergent. The mannanase was more than 35% "active in powder detergents from Europe, Ariel Futur and in U3 tide pow¬der. In these tests, the detergent concentration was as recom-l mended on the commercial detergent packages and the wash water was tap water having 18 degrees German hardness under European (Ariel Futur) conditions and 9 degree under US conditions (US Tide). EXAMPLE 14 Mannanase derived from the fungal strain Humlcola. insolens DSM 1800 Expression cloning of a family 26 beta-1,4-mannanase from Humi- cola xngolens Fungal strain and cultivation conditions Humzcola S.nsole-s strain DSM 1800 was fermented as de¬scribed ir: V!0 57/32014, the mycelium was harvested after 5 days growth at 26 SC, immediately frozen in liquid N,, and stored at - 80 °C.. f Preparation of RNase-free glassware, tips and solutions Ail glassware used in RNA isolations were baked at + 220 °C for at least 12 h. Epper.dorf tubes, pipet tips and plastic columns were treated in 0.1 % diethylpyrocarbonate !DE?c; in EtOK for 12 b, and autoclaved. All buffers and water (except Tris-ccntaining buffers) were treated with 0.I % DEPC for 12 h at 37 Dc, and autoclaved. Extraction of total SNA The total RNA was prepared by extraction with guanidiniurn, thiocyanate followed by uitracentrifugation through a 5.7 M CsCl cushion (Chirgwin et si., 1979) using the following modifica¬tions. The frozen mycelia was ground in liquid N; to fine powder with a mortar and a pestle, followed by grinding in a precocled coffee mill, and immediately suspended in 5 vols cf RNA extrac¬tion buffer (4 M GuSCN, 0.5 % Na-laurylsarcosine, 25 mM Na~ citrate, pH 7.0, 0.1 M fi-mercaptoethanol). The mixture was stirred for 30 ram. at RT° and centrifuged {30 min., 5000 rpm, RTP, Heraeus Megafuge 1.0 R) to pellet the cell debris. The supernatant was collected, carefully layered onto a 5.7 M CsCl cushion (5.7 M CsCl, 0.1 M EDTA, pK 7.5, 0.1 i DE?C; autoclaved prior tG usei using 26.5 ml supernatant per 12.0 ir.l CsCl cush¬ion, and centrifuged to obtain the total RNA (sectarian, SV! 28 rotor, 25 CQ0 rpm, RT°, 24h) . After centrifugation the super¬natant was carefully removed and the bottom of the tube contain¬ing the RNA pellet was cut off and rinsed with 70 i EtOK. The total RNA pellet was transferred into an Epper.dorf tube, sus- Isolation of poly(A)*RNA The poly(A)'RNAs were isolated by cligo (dT) -cellulose affinity chromatography (Aviv & Leder, 1972}. Typically, 0.2 q of cligo(dT) cellulose (Boehringer Mannheim, check for binding capacity} was preswolien in 10 ml of 1 x column loading buffer (2D mM Tris-Cl, pH 7.6, 0.5 M NaCl, 1 mM EDTA, C.l % SDS} , loaded onto a CEPC-treated, plugged plastic column (Poly Frep Chromatography Column, Bio Rad), and equilibrated with 23 ml 1 x loading buffer. The total RNA was heated at £5 °C for 8 min., quenched on ice for 5 min, and after addition of I vol 2 x column loading buffer to the RNA sample loaded onto the column. The eluare was collected and reloaded 2-3 times by heating the sample as above and quenching on ice prior to each loading. The oligo(dT) column was washed with 10 vols of 1 x loading buffer, then with 3 vols of medium salt buffer (20 mM Tris-Ci, pH 7.6, 0.1 M NaCl, 1 mM EDTA, 0.1 % SDS), followed by elution of the ooly(A)' RNA with 3 vols of elution buffer (10 mM Tris-Cl, pH 7.6, 1 mM EDTA, 0.05 % SDS) preheated to + 65 °C, by collecting ;00 ml fractions. The ODj6D was read for each collected fraction, ind the mRNA containing fractions were pooled and ethancl pre¬cipitated at - 20 °C for 12 h. The poly(A!+ RNA was collected by :entrifugation, resuspended in DEPC-DIW and stored in 5-10 mg liquots at - 80 °C. cDNA synthesis First strand synthesis Double-stranded cDNA was synthesized from 5 mg on Kuxicola insolens poiy(A)' RNA cy tne RNase H methoo (Gubler 5 Hoffman i 1983, Sambrock et al., 1989) ^sing the hair-pin modification developed by F, S, Hagen (pers. coram.). The poly(A}*RNA (5 mg in 5 ml cf DEPC-treated water} was heated at 70°C for 8 ram., quenched on ice, and combined in a final volume of SO ml with reverse transcriptase buffer (50 mM Tris-Cl, pH 8.3, 75 mM KC1, 3 mM MgC12, 10 mM DTT, Bethesda Research Laboratories) contain¬ing 1 mM each dNTP (Pharmacia), 40'units of numar. placental ribonuclease inhibitor (RNasin, Promega), 10 mg cf oligo (dT) u_:a primer (Pharmacia) anc 1000 units of Superscript 11 RNase H-reverse transcriptase (Sethesda Research Laboratories). First-strand cDNA was synthesized by incubating the reaction mixture at 45 °C for 1 h. Second strand synthesis After synthesis 30 ml of 10 mM Tris-Cl, pH 7.5, 1 mM EDTA was added, and the m.RNA:cDNA hybrids were ethanol precipitated for 12 h at - 20 QC by addition cf 40 mg glycogen carrier (Boehringer Mannheim) 0.2 vols 10 M NH,Ac and 2.5 vols 96 % EtOK. The hybrids were recovered by centrifugation, washed in 70 I EtOH, air dried and resuspended in 250 ml of second strand buffer (20 mM Tris-Cl, pH 7.4, 90 mM KC1, 4.6 mM MgC12, 10 mM (NKJ.SO., 16 mM HNADTJ containing 100 mM each cLNTP., 44 unics of E. coli DMA polymerase 1 (Airiersham) , 6.25 units of RNase H (Bethesda Research Laboratories) and 10.5 units of E. coli DMA Ligase (New England Biolabs). Second strand cDMA synthesis was performed by incubating the reaction tube at 16 DC for 3 h, and the reaction was stopped by addition of EDTA to 20 mM, final concentration followed by phenol extraction. Mung bean nuclease treatment The double-stranded (ds) cDNA was ethanol precipitated at -20°C for 12 h by addition of 2 vols of S6 % EtOH, 0.1 vol 3 M MaAc, pH 5.2, recovered by centrifugation, washed in 70 % EtOH, dried (SpeedVac), and resuspended in 30 ml of Mung bean nuclease buffer (30 mM NaAc, pH 4.6, 300 mM NaCI, 1 iaM ZnS04, C.35 mM DTT, 2 % glycerol) containing 36 units cf Mur.g bean nuclease (Bethesda Research Laboratories). The single-stranded hair-pin DNA was clipped by incubating the reaction at 33 °C for 30 rr.in, followed by addition cf 70 ml 1C rrJM Tris-Ci, pH 7.5, 1 ml-: EDTA, phenol extraction, and ethane1 precipitation with 2 vols cf 96 % EtOH and 0.1 vol 3K NaAc, pH 5.2 at - 20 "C for 12 h. Blunt-ending with T4 DNA polymerase The ds cDNA was blunt-ended with T4 DNA polymerase in 50 ml of T4 DNA polymerase buffer (20 mM Tris-acetate, pH ~>. 9, 10 mM MgAc, 50 mM KAc, I mM DTT) containing 0.5 mM each dNT? and 7.5 units of T4 DKA polymerase (Invitrogen) by incubating the : reaction mixture at + 37 °C for 15 min. The reaction was stopped by addition of EDTA to 20 roM final concentration, followed by phenol extraction and ethanol precipitation. Adaptor ligation and size selection After the fill-in reaction the cDNA was ligated to non-palindromic SstX I adaptors (1 mg/rrd, Invitrogen) in 30 ml of ligation buffer (50 mM Tris-Cl, pH 7.8, 10 mM MgC12, 10 mM DTT, 1 mM ATP, 25 mg/ml bovine serum albumin) containing 600 pmol BstX I adaptors and 5 units of T4 ligase (Invitrogen) by incu¬bating the reaction mix at + 16 °C for 12 h. The reaction was stopped by heating at + 70 °C for 5 min, and the adapted cDNA was size-fractionated by agarose gel electrophoresis (0.S % H3B- agarose, FMC; co separate ur.ligated adapters and small cDNAs. The cDNA was size-selected with a cut-off at 0.7 kb, and the cDNA was electroeluted from the agarose gel in 10'mM Tris-Cl, DH 7.5, 1 nM EDTA for 1 h at IOC volts, phenol extracted and etha-nol precipitated at - 20 °C for 12 h as above. Construction of the Hnmicola insolens cDNA library The adapted, ds cDNAs were recovered by centrifugation, washed in 70 % EtOH and resuspended in 25 rr.l DIW. Prior to large-scale library ligation, four test ligations were carried out in 10 ml of ligation buffer (same as above; each containing 1 rr.l ds cDNA (reaction tubes #1 - #3), 2 units c: T4 ligase (Invitrogen) and 50 ng (tube #1), 100 ng (tube #2; and 200 ng (tubes #3 and #4} Est XI cleaved pYES 2.0 vector (Invitrogen). The ligation reactions were performed by incubation at + 16 °C for 12 h, heated at 70 "C for 5 min, and 1 ml of each ligation electroporated (200 W, 2.5 kV, 25 mF) to 40 ml competent E. coli 1061 cells (OD600 = 0.9 in 1 liter L3-broth, washed twice in cold DIM, once in 20 ir.I of 10 % glycerol, resuspended in 2 ml 10 % glycerol). After addition of 1 ml SOC to each transformation mix, the cells were grown at + 37 °C for 1 h , 50 mi plated on LB + ampicillin plates (100 mg/ml) and grown at + 37 °C for 12h. Using the optimal conditions a large-scale ligation was set up in 4 0 ml of ligation buffer containing 9 units of T4 ligase, and the reaction was incubated at + 16°C for 12 h. The ligation reaction was stopped by heating at 70°C for 5 min, ethanoi precipitated at - 20DC for 12 h, recovered by centrifugation and resuspended in 10 ml DIW. One ml aliquots were transformed into electrocompetent E. coli 1061 cells using the same electropora-tion conditions as above, and the transformed cells were titered and the library plated on LB + ampicillin plates with 5000-7000 c.f.u./plate. The cDNA library , comprising of 1 x 10e recombi- riant clones, was stored as 1; individual pools [500J-700G c.f.u./pool) in 20 % glycerol a: - 80°C, 2) cell pellets of the same pools at - 20 = C, and 3) Ginger, purified piasr.id DM1- from individual pools at - 20°C (Qiagen Tip 100, Diager.j. Expression cloning in Saccharomyces cerevislae of beta-1,4 mannanase cDNAs from tfumicola insolens One ml aliquots cf purified plasmid DNA {100 ng/rr.l) from individual pools were electrcporated (200 W, 1.5 kV, 25 mF) into 40 ml of electrccomp_etent S. cerevisiae W3124 (MATa; ura 3-52; leu 2-3, 112; his 3-D200; pep 4-1137; prcl::H1S3, prbl::LEU2; cir-; cells (OD60G = 1.5 in 500 ml YPD, washed twice in cold DIW, once in cold 1 M sorbitol, resuspended in 0.5 nl 1 M sorbitol, Becker & Guarante, 1991). After addition of 1 ml 1M cold sorbitol, 80 ml aliquots were plated on SC + glucose -uracil to give 250-40C colony forming units per plate and incu-oated at 30 °C for 3-5 days. The plates were replicated or. S"C -galactose - uracil plates, containing AZCl-ga.lactcmar.nan {MegaZyme, Australia) incorporated in the agar plates. In total, oa. 50 000 yeast colonies from the H. ir.solens library were screened for mannanase-positive clones. The positive clones were identified by the formation of Dlue hydrolysis halos around the corresponding yeast colonies. The clones were obtained as single colonies, the cDNA inserts jere amplified directly from yeast cell lysates using biocir.y-Lated pYES 2.0 pclylinker primers, purified by magnetic beads [Dynabead M-2SG, Dynai) system and characterised individually by =eauencing the 5'-end of each cDNA clone using the chain-:erminaticn method (Sanger et al., 1977) and the Sequenase system (United States Biochemical). The mannanase-positive yeast colonies were inoculated into 20 ml YPD broth in a 50 ml tubes. The tubes were shaken for 2 days at 30°C, and the cells were harvester by centri :uca;icr. for 10 mir.. at 3C00 rprr:. Total yeas- DNA was isolated according to WO 94/14953, dissolved in 50 ir.I of autoclaved water, and trans¬formed into E. coli by eiectroporation as above. The insert-containing pYES 2.0 cDNA clones were rescued by plating on LE + ampicillin agar plates, the plasmid DMA was isolated from E. coli using standard procedures, and analyzed by digesting with restriction enzymes. r Nucleotide sequence analysis The nucleotide sequence of the full-length- H. insole.ns beta-1,4-mannanase cDNA clone pClM59 was determined from both strands by the dideoxy chain-termination method (Sanger e: al. 1977), using 500 ng of Qiagen-purified template (Qiagen, USAj template, the Tac deoxy-terminal cycle sequencing kit (Perkin-Elmer, USA}, fluorescent labeled terminators and 5 pmol of the pYES 2.0 polylinker primers (Invitrogen, USA). Analysis of the sequence data were performed according to Devereux et al. (1984) . Heterologous expression in Aspergillus oryzae Transformation of Aspergillus oryzae Transformation of .Aspergillus oryzae was carried out as de¬scribed by Christensen et al., (1988), Biotechnology 6, 1419-1422. Construction of the beta-1,4-mannanase expression cassette for Aspergillus expression Plasmid DNA was isolated from the mannanase clone pC!M59 using standard procedures and analyzed by restriction enzyme analysis. The cDNA insert was excised using appropriate restric¬tion enzymes and ligated into the Aspergillus expression vector p'r.DAiA, wr.ich is a derivative cf the piasmid p775 (descrioed m EP 238023). The construction cf pHD414 is further described in WO 93/11249. Transformation of Aspergillus oryzae or Aspergillus niger General procedure: 100 ml of YPD (Sherman et al., Methods in Yeast Genetics, Cold Spring Harbor Laboratory, 1981) is inoculated with spores cf A. oryzae or A. niger and incubated with shaking at 37 °C for about 2 days. The mycelium is harvested by filtration through miracloth and washed with 200 ml cf 0.6 M MgSG.. The mycelium is suspended in 15 mi of 1.2 M MgSO,. 10 mM NaH:P0,, pH = 5.5. The suspension is cooled or. ice and 1 ml of buffer containing 120 mg of Novozym® 234 is added. After 5 minutes 1 ml cf 12 mg/ml 5SA is added and incubation with gentle agitation continued for 1.5-2.5 hours at 37°C until a large number of protoplasts is visible in a sample inspected under the microscope. The suspension is filtered through miracloth, the filtrate transferred to a sterile tube and overlayered with 5 ml of 0.6 M sorbitol, 100 mM Tris-HCl, pH = 7.0. Centrifugatior. is performed for 15 minutes at 100 g and the protoplasts are col¬lected from the top cf the MgSO, cushion. 2 volumes cf STC are added to the protoplast suspension and the mixture is centrifu-gated for 5 minutes at 1000 g. The protoplast pellet is resus-pended in 3 ml of STC and repelleted. This is repeated. Finally the protoplasts are resuspended in 0.2-1 ml of STC. 100 ui of protoplast suspension is mixed with 5-25 ug of the appropriate DNA in 10 pi of STC. Protoplasts are mixed with p3SR2 (an A. nidulans amdS gene carrying piasmid]. The mixture is left at room temperature for 25 minutes. 0.2 ml of 60% PEG 4000. 10 mM CaCl, and 10 mM Tris-HCl, pH 7.5 is added and carefully mixed (twice) and finally 0.85 ml of the same solution is added ana carefully mixed. The m.ixture is left at room temperature for 25 rainut.es, spun, a- 2500 g for 15 mir.utss and the pellet is resus-pended in 2 ml of 1.2 M sorbite!. After cne mere sedimentation the protoplasts are spread on the appropriate plates. Proto¬plasts are spread on minimal plates to inhibit background growth. After incubation for 4-1 days at 37°C spores are picked and spread for single colonies. This procedure is repeated and spores of a single colony after the second re-isolation is stored as a defined trar.sformant. Purification of the Aspergillus oryzae transfonnants Aspergillus oryzae colonies are purified through ccr.idial spores or. AmdS~-plates (+ 3,01% Triton X-100) and growth in YFM for 3 days at 30°C. Identification of mannanase-positive Aspergillus oiyzae trans¬fonnants The superr.atants from the Aspergillus cryzae' transfcrmants were assayed for beta-1, 4-mannanase activity or. agar plates containing 0.2 % AZCl-galactomannan (MegaZyme, Australia) as substrate. Positive transformants were identified by analyzing the plates for blue hydrolysis halos after 24 hours of incuba¬tion at 30°C. SDS-PAGE analysis SDS-PAGE analysis of supernatants from beta-1,4-mannanase producing Aspergillus oryzae transformants . The transformar.ts were grown in 5 ml Y?M for three days. 10 ul of supernatant was applied to 12% SDS-poiyacrylanide gel which was subsequently stained with Coonassie Brilliant Blue. Purification and characterisation of the Humlcola. insolens mannanse The gene was transformed into A. cryzse ads described arove and the transformed strain was grown ir. a ferruentcr us in a stan¬dard medium c: Maltose syrup, sucrose, MgSC, Ka^PO. and K,SO, ana citric acid yeast extract and trace metals. Incubation for 6 . days at 34°C with air. The fermentation broth (5000 ml) was harvested and the my¬celium separated from the liquid by filtration. The clear liquid was concentrated on a filtron to 275 ml. The mannanase was purified using Cationic chromatography. A S-Spharose cci'iir.n was equilibrated with 25 mM citric acid pH 4.C and the nar.nanase bound to the column and was eluted using a sodium chloride gradient (0-0.5 Mi. The mannanase active frac¬tions was pooled and the pH adjusted to 7.3. The 100 ml pooled mannanase was then concentrated to 5 ml with around 13 mg pro¬tein, per ml and used for applications trials. For futher purifi¬cation 2 ml was applied to size chromatography on Superdex 200 in sodium acetate buffer pK 6.1. The manr.ase active fraction showed to equal stained bands in SDS-PAGE with a MW of 45 kDa and 38 kDa, indicating proteolytic degradation of the N-terminal non-catalytic domain. The amino acid sequence of the mannanase enzyme, i.e. the translated DNA sequence, is shown in SEQ ID NO:14. The DNA sequence of SEQ ID NO:13 codes for a signal peptide in positions 1 to 21. A domain of unknown function also found in other mannanases is represented in the amine acid sequence SEQ ID NO: 14 in positions 22 to 159 and the catalytic active domain is found in positions 160 to 488 of SEQ ID NO:14. Highest sequence homology was found to DICTYOGLOMUS TKERMOPHILUM (49% identity); Mannanase sequence EMBL; AF013939 submitted by REEVES R.A., GIBBS M.D., BERGQUIST P.L. submitted in July 1997. Molecular Wg_igh.tj_ 28 k^a . DSC in sodium acetate buffer pH 6.0 was 65°. The pK activity profile using the ManU assay (incubation for 20 minutes at 40°C) shows that the enzyme has optimum activ-, ity at pH S. Temperature optimum was found (using the ManU assay; Mega-zyme AZCL locust beer, gum as substrate) to be ?0°C at pK 10. Immunological properties?; Rabbit polyclonal monospecific serum was raised against the highly purified cloned mannanase using conventional techniques at the Danish company DAKO. The serum formed a nice single precipitate in agarose gels with the crude non purified mannanase of the invention. EXAMPLE 15 Wash evaluation of Htimicola Insolens family 26 mannanase Was.-, performance was evaluated by washing locust bean gum coated swatches in a detergent solution with the mannanase of the invention. After wash the effect were visualised by soiling the swatches with iron oxide. Preparation of lccust bean gum swatches: Clean cotton swatches were soaked in a solution of 2 g/1 locust bean gum and dried overnight, at room temperature. The swatches were prewashed in water and dried again. Wash: Small circular locust bean gum swatches were placed in a beaker with 6,7 g/1 Ariel Futur liquid in 15°dH water and incubated for 30 min at 40°C with magnetic stirring. The swatches were rinsed in tap water and dried. Soiling: The swatches were placed in a beaker with 0.25 g/i Fe,03 and stirred for 3 min. The swatches were rinsed in tap water and dried. Evaluation: Remission of the swatches was measured at 440 nm using a MacBeth ColorEye 7000 remission spectrophotometer. KXAMPLES 16-40 The following examples are meant Co exemplify compositions of the present invention, but are not necessarily meant to limit or otherwise define the scope of the invention. In the detergent compositions, the enzymes levels are ex¬pressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are ex¬pressed by weight of the total compositions. The abbreviated component identifications therein have the following meanings: LAS : Sodium linear Cn-13 alkyl benzene sul- phonate. TAS : Sodium tallow alkyl sulphate. The following nil bleach-con.cain.ing detergent compositions of particular use in the washing of colored clothing were precared according to the present invention : r Example 2 5 The following liquid detergent formulations were preDared ac¬cording to the present invention (Levels are given in parts per weight, enzyme are expressed in pure enzyme) : Example ?.£, The following liquid detergent formulations were prepared ac¬cording to the present invention (Levels are given in parts per weight, enzyme are expressed in pure enzyme) : Example 27 The following liquid detergent compositions were prepared ac¬cording to the present invention (Levels are giver, ir. parts per weight, enzyme are expressed in pure enzyme) : Example 2 8 The following liquid decergent compositions were prepared ac¬cording to the present invention {Levels are given in -Darts by weight, enzyme are expressed in pure enzyme} : Example 2 9 The following granular fabric detergent compositions which provide "softening through the wash" capability were prepared according to the present invention : Example 31 The following fabric softener and dryer added fabric conditioner compositions were prepared according to the present invention : Example "?A The following compact high density (0.96Kg/l) dishwashing deter¬gent compositions were prepared according to the present inven¬tion : The following granular dishwashing detergent compositions of bulk density 1.02Kg/L were prepared according to the present: invention : The following tablet detergent compositions were prepared ac¬cording to the present invention by compression of a granular dishwashing detergent composition at a pressure of !3KN/cm2 using a standard 12 head rotary press: Example 3fi The following liquid dishwashing compositions were prepared according to the present invention : Example .19 The following liquid hard surface cleaning compositions were prepared according to the present invention : Example 4 0 The following spray composition for cleaning of hard surfaces and removing household mildew was prepared according to the present invention : LITERATURE Aviv, H. & Leder, P. 1972. Proc. Naci. Acad. Sci. U. S. A. 69: 1408-1412. Becker, D. M, & Guarante, L. 1991. Methods Enzymol. 194: 192-18*?. Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J. 5 Ruttsr, W. J. 1979. Biochem¬istry IS: 5294-5299. Gubler, U. & Hcfiir.an, E. J. 1983. Gene 25: 263-269. i Sambrook, J., Fritsch, E. F. & Maniatis, T. 1989. Molecular Cloninc: A Laboratory Manual. Cold Spring Harbor Lab., Cold Spring Harbor, NY. Sanger, F., Nicklen, S. & Coulson, A. R. 1977. Prcc. Natl. Acad. Sci. U. S. A. 74: 5463-5467. Lever, M. (1972) A new reaction for colormetric determination of carbohydrates. Anal. Biochem. 47, 273-279. N. C. Carpita and D. M. Gibeaut (1993) The Plant Journal 3:1-30. Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, B. R., Sj0holm, C. (1990) Cloning of aldE, which encodes alpha-acetolactate decarboxylase, an exoer.zyme from Eacillus hrevis. J. Bacteriol. 172:4315-4321. WE CLAIM: [lyAn isolated mannanase which is (a) a polypeptide encodable by the mannanase enzyme encoding part of the DNA sequence cloned into the plasmid present in Escherichia coli DSM 12197. or (b) a polypeptide comprising an amino acid sequence as shown in positions 31-330 of SEQ ID NO:2. or (c) a polypeptide encodable by the DNA sequence as shown in positions 91-990 or positions 91-1470 of SEQ ID NO:l, or (d) an analogue of the polypeptide defined in (a) or (b) which is at least 65% homologous with said polypeptide, or a fragment of (a), (b) or (c). 2. The mannanase according to claim 1 which is derivable from a strain of Bacillus sp. 3. The mannanase according to claim 2 which has i) a relative mannanase activity of at least 60% in the pH range 7.5-10. measured at 40°C; ii) a molecular weight of 34 ± 10 kDa, as determined by SDS-PAGE; and/or iii) the N-terminal sequence ANSGFYVSGTTLYDANG. ■ $\ An isolated polynucleotide molecule comprising a DNA sequence encoding an enzyme exhibiting mannanase activity, which DNA sequence comprises: (a) the mannanase encoding part of the DNA sequence cloned into the plasmid present in Escherichia coli DSM 12197; (b) the DNA sequence shown in positions 91-1470 in SEQ ID NO 1, preferably position 91-990, or its complementary strand; (c) an analogue of the DNA sequence defined in (a) or (b) which is at least 65% homologous with said DNA sequence; (d) a DNA sequence which hybridizes with a double-stranded DNA probe comprising the sequence shown in positions 91-990 in SEQ ID NO 1 at low stringency; (e) a DNA sequence which, because of the degeneracy of the genelic code, does not hybridize with the sequences of (b) or (d), but which codes for a polypeptide having exactly the same amino acid sequence as the polypeptide encoded by any of these DNA sequences; or a DNA sequence which is a fragment of the DNA sequences specified in (a), (b), (c), (d), or (e). 5. The cloned DNA sequence according to claim 4. in which the DNA sequence encoding an enzyme exhibiting mannanase activity is obtained from a microorganism, preferably a filamentous fungus, a yeast, or a bacteria; preferably from Bacillus, Caldicellulosiruptor or Humicola- 6. )An isolated polynucleotide molecule encoding a polypeptide having mannanase activity which polynucleotide molecule hybridizes to a denatured double-stranded DNA probe under medium stringency conditions, wherein the probe is selected from the group consisting of DNA probes comprising the sequence shown in positions 91- 990 of SEQ IDNO:l, the sequence shown in positions 91-1470 of SEQ IDNO:l and DNA probes comprising a subsequence of positions 91-990 of SEQ ID NO:l having a length of at least about 100 base pairs. 7. An expression vector comprising the following operably linked elements: a transcription promoter; a DNA segment selected from the group consisting of (a) polynucleotide molecules encoding a polypeptide having mannanase activity comprising a nucleotide sequence as shown in SEQ ID NO:l from nucleotide 91 to nucleotide 990, (b) polynucleotide molecules encoding a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SEQ ID NO:2 from amino acid residue 31 to amino acid residue 330, and (c) degenerate nucleotide sequences of (a) or (b); and a transcription terminator. 8. A cultured cell, selected from a bacterial or fungal cell, into which has been introduced an expression vector according to claim 7, wherein said cell expresses the polypeptide encoded by the DNA segment. 9. An isolated polypeptide having mannanase activity selected from the group consisting of: (a) polypeptide molecules comprising an amino acid sequence as shown in SEQ ID NO; 2 from residue 31 to residue 330; and (b) polypeptide molecules that are at least 65% identical to the amino acids of SEQ ID NO: 2 from amino acid residue 31 to amino acid residue 330. 10. The polypeptide according to claim 9 which is produced by Bacillus sp. 1633. 11. An enzyme preparation comprising a purified polypeptide according to claim 9. 12. A method of producing a polypeptide having mannanase activity comprising culturing a cell into which has been introduced an expression vector according to claim 7, whereby said cell expresses a polypeptide encoded by the DNA segment; and recovering the polypeptide. 13. The preparation according to claim 11 wherein it comprises one or more enzymes selected from the group consisting of proteases, cellulases (endoglucanases), (3-glucanases, hemicellulases, lipases, peroxidases, laccases, a-amylases, glucoamylases, cutinases, pectinases, reductases, oxidases, phenol oxidases, ligninases, pullulanases, pectate lyases, xyloglucanases, xylanases, pectin acetyl esterases, polygalacturonases, rhamnogalacturonases, pectin lyases, other mannanases, pectin methylesterases, ceflobiohydrolases, transglutaminases; or mixtures thereof. 14. An isolated enzyme having mannanase activity, in which the enzyme is (i) free from homologous impurities, and (ii) produced by the method according to claim 12. 15. A method for improving the properties of cellulosic or synthetic fibres, yarn, woven or non-woven fabric in which method the fibres, yarn or fabric is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 16. The method according to claim 15, wherein the enzyme preparation or the enzyme is used in a desizing process step. 17. A method for degradation or modification of plant material in which method the plant material is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 18. The method according to claim 17 wherein the plant material is recycled waste paper; mechanical, chemical, semichemical, kraft or other paper-making pulps; fibres subjected to a retting process; or guar gum or locust bean gum containing material. 19. A method for processing liquid coffee extract, in which method the coffee extract is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 20. A cleaning composition comprising the enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2. 21. The cleaning composition according to claim 20 wherein it comprises an enzyme selected from cellulases, proteases, lipases, amylases, pectin degrading enzymes and xyloglucanases; and conventional detergent ingredient. 22. The cleaning composition according to claim 20 wherein said enzyme or enzyme preparation is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferably from 0.001% to 0.1% pure enzyme by weight of total composition. 23. The cleaning composition according to claim 21 wherein the enzyme is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferably from 0.001% to 0.1% pure enzyme by weight of total composition. 24. The cleaning composition according to claim 21 wherein the enzyme is an amylase. 25. The cleaning composition according to claim 24 wherein it comprises yet another enzyme selected from cellulase, protease, lipase, pectin degrading enzyme and xyloglucanase. 26. The cleaning composition according to claim 21 which comprises a surfactant selected from anionic, Don-ionic, cationic surfactant, and/or mixtures thereof. 27. The cleaning composition according to claim 21 which comprises a bleaching agent. 28. The cleaning composition according to claim 21 which comprises a builder. 29. A fabric softening composition according to claim 21 which comprises a cationic surfactant comprising two long chain lengths. 30. A process for machine treatment of fabrics which process comprises treating fabric during a washing cycle of a machine washing process with a washing solution containing the enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2. 31. A method for removing stains on a fabric in which method the fabric is treated with an effective amount of an enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2 together with a enzyme selected from cellulase, protease, lipase, amylase, pectin degrading enzyme and xyloglucanase. 8. A cultured cell, selected from a bacterial or fungal cell, into which has been introduced an expression vector according to claim 7. wherein said cell expresses the polypeptide encoded by the DNA segment. 19. ;An isolated polypeptide having mannanase activity selected from the group consisting of: (a) polypeptide molecules comprising an amino acid sequence as shown in SEQ ID NO: 2 from residue 31 to residue 330; and (b) polypeptide molecules that are at least 65% identical to the amino acids of SFQ ID NO: 2 from amino acid residue 31 to amino acid residue 330. 10. The polypeptide according to claim 9 which is produced by Bacillus sp. 1633. 11. An enzyme preparation comprising a purified polypeptide according to claim 9. 12. A method of producing a polypeptide having mannanase activity comprising culturing a cell into which has been introduced an expression vector according to claim 7, whereby said cell expresses a polypeptide encoded by the DNA segment; and recovering the polypeptide. 13. The preparation according to claim 11 which further comprises one or more enzymes selected from the group consisting of proteases, cellulases (endoglucanases). [5-glucanases, hemicellulases, lipases, peroxidases, laccases, a-amylases, glucoamylases, cutinases, pectinases, reductases, oxidases, phenoloxidases. ligninases, pullulanases. pectate lyases, xyloglucanases, xylanases. pectin acetyl esterases, polygalacturonases, rhamnogalacturonases, pectin lyases, other mannanases, pectin methylesterascs, cellobiohydrolases. transglutaminases; or mixtures thereof. 14. An isolated enzyme having mannanase activity, in which the enzyme is (i) free from homologous impurities, and (ii) produced by the method according to claim 12. 15. A method for improving the properties of cellulosic or synthetic fibres, yam, woven or non-woven fabric in which method the fibres, yarn or fabric is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 16. The method according to claim 15. wherein the enzyme preparation or the enzyme is used in a desizing process step. 17. A method for degradation or modification of plant material in which method the plant materia] is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 18. The method according to claim 17 wherein the plant material is recycled waste paper; mechanical, chemical, semichemical, kraft or other paper-making pulps; fibres subjected to a retting process; or guar gum or locust bean gum containing material. 19. A method for processing liquid coffee extract, in which method the coffee extract is treated with an effective amount of the preparation according to claim 11 or an effective amount of the enzyme according to claim 1 or 2. 20. A cleaning composition comprising the enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2. 21.'The cleaning composition according to claim 20 which further comprises an enzyme selected from cellulascs, proteases, lipases, amylases, pectin degrading enzymes and xyloglucanases; and conventional detergent ingredient. 22. The cleaning composition according to claim 20 wherein said enzyme or enzyme preparation is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferably from 0.001% to 0.1% pure enzyme by weight of total composition. 23. The cleaning composition according to claim 21 wherein the enzyme is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%. more preferably from 0.001% to 0.1% pure enzyme by weight of total composition. 24. The cleaning composition according to claim 21 wherein the enzyme is an amylase. 25. The cleaning composition according to claim 24 which further comprises yet another enzyme selected from cellulase. protease, lipase, pectin degrading enzyme and xyloglucanase. 26. The cleaning composition according to claim 21 which comprises a surfactant selected from anionic, Clon-ionic, cationic surfactant, and/or mixtures thereof. 27. The cleaning composition according to claim 21 which comprises a bleaching agent. 28. The cleaning composition according to claim 21 which comprises a builder. 29. A fabric softening composition according to claim 21 which comprises a cationic surfactant comprising two long chain lengths. 30. A process for machine treatment of fabrics which process comprises treating fabric during a washing cycle of a machine washing process with a washing solution containing the enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2. 31. A method for removing stains on a fabric in which method the fabric is treated with an effective amount of an enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2 together with a enzyme selected from cellulase. protease, lipase, amylase, pectin degrading enzyme and xyloglucanase. 32. A method for cleaning hard surfaces such as floors, walls, balhroom tile, dishes in which method the fabric is treated with an effective amount of an enzyme preparation according to claim 11 or the enzyme according to claim 1 or 2 together with a enzyme selected from cellulase, amylase, protease, lipase, pectin degrading enzyme and xyloglucanase.

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