| Title of Invention | DESIZING AND SCOURING PROCESS |
|---|---|
| Abstract | ABSTRACT The present invention relates to processes for combined desizing and scouring of a sized fabric containing starch or starch derivatives during manufacture of fabhc, which process comprisses indicating said :5i2:ed fabric in an aqueous treating solution having a pH m the range between 1 and 7, which aqueous treating soiuiion comprises an acid amylase and at least cne othe"" acid enzyme facilitating said other fabric treatment steps. The present compositions. |
| Full Text | This applicaticr contains a Sequence Listing in computer readable form. The computer readable forir is incorporaled herein by reference. FIELD OF THE INVENTION acid-amylase and other enzymes such as cellulase, pectinase, lipase, xylanase, protease, etc during manufacture of nev.'fabrics, BACKGROUND OF THE INVENTION The processing of f;aljric, such as cellulosic material, into material ready for garment manufacture involves seveic steps: spinning of the fiber into a yarn; construction of woven or knit fabric from the yarn; and subsequent preparation, dyeing and finishing operations. The preparation process^ which may involve desizing (for woven goods), scouring, and bleaching, produces a labric suitable for dyeing or finishing. WO 2006/(302034 (Novozymes) describes simultaneous desizing and scouring process comprising treating fabric with an alkanne alpha-amylase and an alkaline scouring enzyme. Alkaline alpha-amylases are used as auxiliaries in desizing processes to facilitate the removal of starch-containing size which has served as a protective coating on yarns during weaving. Complete removal of the size coating after weaving is important to ensure optimum results in ihe subsequent p'ocesses in which the fabric is generally scoured, bleached, dyed and/or printed. After the desizing step it is often desirable to include a demineralization step in order to remove metal ions such as Mn'^ Fe'VPe^'^'Cu^^etc., which - if present on the fabric -may result in an uneven t:)Ieaching in a later process step or might even make pin-holes in the bleached fabric. Demiieraiization is typically accomplished by acid precipitation and typically involves addition of acids such as acetic acid or sulphuric acid. There is a need for improved processes for simultaneous desizing combined with other fabric treatment steps, such as combined desizing and scouring, combined desizing and biopolishing, combined desizing and abrasion and combined desizing and carbonizing etc. BRIEF DISCLOSURWEOF THE INVENTION The present inventon is directed towards providing processes of desizing sized fabrics during iTianufao:ure o1 especially new fabrics under acid conditions. In one aspect, the present invention relates to a process for combined desizing and other fabric treatment steo;? of a sized fabric containing starch or starch derivatives during manufacture of 'abric, wnich proces;s comprises incubating said sized fabric in an aqueous treating solution havr:: a p\-\ in the range be+vv/een 1 and 7, preferably between 1 and 5, at least one other acic enzyme facilitating said other fabric treatment step(s). Preferably, said otner acid enzyme(s), facilitating said other fabric treatment step(s), is (are) acid cellulase acid pectinase, acid lipase, acid xylanase and/or acid protease. More preferably, the enzyme(s} facilitating said other fabric treatment step(s), is(are) acid pectinase(s). Preferably, thf; acic! amylase is of bacterial or fungal origin, such as filamentous fungus origin Preferably, the acid amylase is derived from a strain of Aspergillus, preferably Aspergillus niger, Aspergillus awamori, Aspergillus oryzae, or Aspergillus kawachii (SEQ ID NO: 37) or a Entrain of Rhizor.ucor, prefe-ably Rtiizomucor pusillus, or a strain of Mahpiius, preferably a strain of Meripilus giganteui More preferably the Aspergillus acid amylase is the acid Aspergillus /i/c;er alpha-amylase disclosed in SEQ ID NO: 38, or a variant thereof. Even more preferably ;he acid amylase is the fl/?/zomucor pus/7/usalpha-amylase disclosed in SEQ ID NO: 48, or a variant thereof. Preferably, the bacterial acid amylase is derived from a strain of the genus Bacillus, preferably derived fr^D.Ti a strain o; Bacillus sp., more preferably a strain of Bacillus licheniformis Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus sp., such as Bacillus sp. NCIE; 12289, NCIB 12512, NGIB 12513, DSM 9375, DSMZ 12648, DSMZ 12649. KSM API 378, KSM K36 or KSM K38. Hybrid alpha-amylase can also use in the present invention. Preferably, the hybrid alpha-amylase could be the amylase consisting of Rhizomucor pusillus alpha-amylase with Aspergillus nigerglucoamyase linker and SBD disclosed as V039 in Table 5 in co-pending International Application no PCT/US05/46725. Preferably, the acid aipha-arnylase is present in a concentration of 1-3,000 AFAU/kg fabric, preferably 10-1,000 AFAU,/ kg fabric, especially 100-500 AFAU/kg fabric or 1-3,000 AFAU/L treating solution, preferably 10-1,000 AFAU/L treating solution, especially 100-500 AFAU/L treating solution. Preferably, the abha-amvlaiie is the hybrid alpha-amylase shown in SEQ ID NO: 48 comprising a catalyti; cjorna n CD) from Rhizomucor pusillus alpha-amylase having a carbohydrate-binding :bmain (CBD) from the A. niger. Normally there are ihree types of pectic enzymes: pectesterase, depolymensing enzymes, and protopeictinase. Preferably, said acid pectinase is an acid pectate lyase, an acid pectin lyase, an a:id polygalacturonase, and/or an acid polygaiacturonate lyase. More perferabley. the acid Decinase is Pectinex BEE XXL.Pectinex Ultra; Pectinex Yield Mash. Preferably: the acid pectinase is from the genus Aspergillus. Preferably^ the acid pectinase can be added into the solution before, simultaneous, or after the addition of acid an i\ 'ase. Preferably, the orocess? 155 carried out at a temperature in the range from 5-90'C, in particular 20 "o 90°C. More preferably, the process is carried out at a temperature between 25 and BOX for a suitable period of time, preferably between 2 and 24 hours. Preferably, the pH is in the range between pH 2 to 4. Preferably: tho fabric is made from fibers of natural or man-made origin, cotton fabric, denim, linen, ramie, .nscose, lyocell, or cellulose acetate. Preferably: the fabric, ;s made of fibers from anirna! origin, in particula: silk or v\/ool. Preferably, the labri: is maci= of polyester fibers of man-made or natural origin, such as poly(ethylene teiephtfialatej )r poiy(lactic acid) or fibers of nylon, acrylic, or polyurethane. The fatiric ;.; eoirably is a polyester containin j fabric or garment consists of essentially 100% polyester. ri-:e po! /ester fabric is a polyester blend, such as a polyt n r and cetlulosic blen:i, nclijciig |)oly3-:t!ir a::d cotton blends: a polyester and wool Uend; a polyester and silk b;:;iic: a :.. -isir ^nc a:yxl\z h;;;n,-; c poiyesie^ ana nyioi: t^ena a polyester, nylon and polyu-eth&M:! bli;-:;': a polyester and polyurethane blend, rayon (viscose), cellulose acetate and :e' : el. In another asper , tlie present invention relates 10 a composition comprisinci an acid amylase and an acid scouring erzyine. The acid amylase is preferably derivec from Aspergillus niger or '^^h' Preferably, said acid pectinase is Pectinex® BE XXL, Pectinex® BE Colour, Pectinex® Ultra; Pect nex™ Ultra SP-L, Pectinex® Yield Mash, Pectinex® XXL, Pectinex® Smash XXL, Pectine);® Smash and/or Pectinex™ AR. Said acid pectinase is preferably derived from a stran of Aspergillus. The composition further comprises stabi izer. surfactant, wetting agent, ciisoersinD agents, sequestering agents and emulsifying agents, or a mixture thereof. In the third aspec;, the pres;ent invention relates to the use of the composition as described above for simuhaneous desizing and scouring. The present inventcrs have found that when carrying out a simultaneously desizing and bioscoLiring procfiss o^ ihe inventior, as defined in 'he claims, no demineraiization is needed. The demine-i^izEitio^- t3! processes involving an acid desizing step and a demineraiization step a pH adjusting step is avoided. Another ad\'antage of the invention is that process time is saved/reduced as desizing, oioscouiing end derninerElization may be carried out simultaneously. Even if the combined desizing ana bioscouring and demineraiization are not carried out as a one step process, i.e., simultaneously, costs, of, e.g., acids and manpower for adding acid(3) are saved/reduced as the pH adiustmert step between the traditional acid desizing step and the demineraiization step is avoided. As compared to simultaneous desizing and bioscouring under alkaline conditions, simultaneous desizing and bioscouring under acid conditions can remove the demineral 2BtiDn at the s.ame time without additional demineralising procedure. In the context of thi invention, the term "treatment" means the combination of enzymes that provide facili;-ied processing, such as combined desizing and scouring, combined desizing and biopolishing, combined desizing and abrasion: etc. In the context cf the invention, the term "biopolishing" is a specific treatmen: of the yarn surface v/hich improves fabric quality with respect to handle and appearance without loss of fabric vi/ettabiliy. The most important effects of biopolishing can be characterised by less fuzz and pilling, increaseo goss/luster, improve-" ;aonc hanale, inceased jjrabie softness and improved wster absorbency. In conte.xt of the nvention, the term "combined" or "combination" means that the combined process steps, c the coribination is carried out sequentially or simultaneously in one bath {i.e., same Seating solution). In a preferred embodiment the comoined process or the combination is carried cut simultaneously in one bath {i.e., same treating solution). In context of the inv-ention the term "fabric" is used interchangeable with the term "textile" and mean?; in contrast to "used" laundry fabric, newly manufactured, preferably undyed, fabrics, garments, fibres, yarns or other types of processed fabrics. Fabrics can be constructed from fibers by weaving, knitting or non-woven operations. Weaving and knitting require yarn as the input whereas the non-woven fabric is the result of random bonding of fibers (paper can be thought of as non-woven). Woven fabric s corisiructed by v^'eaving "filling" or weft yarns between warp yarns stretched in rhe longi.iidincil iiiirection on the loom. The wrap yarns must be sized before weaving in orcer to luDricale and protect them from abrasion at the high speed insenion of the filling yams dunnci weaving. Th-5 filling yarn can be woven through the warp yarns in a "over one - under the next" la shier (plain weave) or by "over one - under two" (twill) or any other myriad of perrnuta:ions. Strength, texture and pattern are related not only to the type/quality of the yarn bjt also the t\'pe of weave. Generally, dresses, shirts, pants jv ' — Knitting Is forrr: ig a fadric by joining together interlocking loops of yarn. As opposed to weaving, which is :;ons:ructed from two types of yarn and has many "ends", knitted fabric is produced from a single continuDus strand of yarn. As with weaving, there are many different ways to loop varn together and the final fabric properties are dependent both upon the yarn and the type of knit. Underwear, sweaters, socks, sport shirts, sweat shirts, etc. are derived from knit fabrics. Non-woven fal)rics are sheets of fabric made by bonding and/or interlocking fibers and filaments by rnecharical, thermal, chemical or solvent mediated processes. The resultant fabric can oe in the form of web-like structures, laminates or films. Typical examples are dispoEciblo t;;;;by d:apers, towels, wipes, surgical gowns, fibers for the "environmental friendly" fashion, filler media, bedding, roofing materials, backing for two-dimensioi'al fabrics arid frany others. According to the in/cintion, ths process may be applied to any sized fabric known in the art (woven, knitted, oi nonv/oven). The process is applied to newly manufactured sized fabric, as opposed to usee and/Dr soileci fabric to be cieanen during laundry washing, in an embodiment the fatv c s ma:.-; cf fbres c 'aturai a^a or n-an-made ir-gln. in a > itner embodimtent the fabnc is riade of fibres Irom animal origir;. In particular, the process of the invention may be appi ed to cellulose-containing or cellulosic fabrics, such as cotton, viscose, rayon, ramie, Inen, cc-llulcs3 acetate, denim, lyocell (Te: cei™, e.g., produced by Courtaulds Fibers), or mixtures thereof, or mixtures of any of these fibers together with synthetic fibres [e.g., polyester, polyamide, acrylic, or polyurethane, nvlon, po!y(ethylene terephthalate) or poly(lactic acid) or other natural fibers, such as wool and silk., such as viscose/cotton blends, lyocell/cotton blends^ \/i3cose/wool blends, lyocell/wool blends, cotton/wool blends; flax (linen), ramie and other fabrics bas.ed on cellulose fibers, including all blends of cellulosic fibers with other fibers such as wool, polyamide, acrylic and polyester fibers, e.g., viscose/cotton/polyesler blends, wool/cotton/polyester blends, flax/cotton blends etc. The process may also be used on synthetic fabric, e.g., consisting of essentially 100% polyester. polyamide, nylon, resiiectivelv Tiie lerm "wool," means any commercially useful animal hair product 'or example, woo iron sheep, camel, rabbit, goat, lama, and knowr as merino wool, Shetland v\/ool i^astimere vvocil, alpaca wool, mohair, etc. and includes wool fiber and animal hair. The process of trie invention can be used with wool or animal hair material in the form of top, fiber, varn, DI woven cr knitted fabric. The alpha-amyiase jsed in CK ;ordance with the process of the invention may be any acid alpha-amylase, bjt is pre-erably of either bacterial or fungal origin, strain of Aspergillus, Rni/.omucor or Meripillus. The term "acid alp:ia-amylase means an alpha-amylase (E.G. 3.2.1.1) which has an optimum activity at a pH m fie rani^e of 1 to 7, preferably from 1 to 5 at a temperature of 50^C. The term "des 2incr' is intended to be understood in a conventional manner, ;.e . the degradation and/or renovE.I of sizing agents from fabric, such as warp yarns in a \woven fabric. The term "fabric containing starch or starch derivatives" is intended to indicate any type of fabric, in partcular ivoven fabric prepared from a cellulose-containing material, containing starch or starch derivatives. The fabric is normally undyed and made cf cotton, viscose, flax, and the like, tie main part of the starch or starch derivatives preser on the fabric is normally size with .v-lich the yarns, normally warp yarns, have been coated prior to weaving. The term "carboh/drate-binding module (CBM)", or as often referred to a "carbohydrate-binding domain (CBD)', is a polypeptide amino acid sequence which binds oreferentially to a poly- or oligosac;naride (carbohydrate), frequently - but not necessarily exclusively - 1c a water-insoluble (including crystalline) form thereof. Even if not specifically mentioned in connection with the process of the invention, it is to be understood that the en2:yme(s) or agent(s) is(are) used in an "effective amount". The term "effective amount" means an amount of, e.g., alpha-amylase that is capable of providing the desired effeo:, i.e., desizing of the fabric, as compared to a fabric which has not been treated v/ith said enz/me(s). DETAILED DISCLOSURE: OF THE INVENTION The present in\'ention is directed towards providing a process of desizing a sized fabric during manufaciire cf especially new fabrics. The desiz-nci stepi o' the invention is in a preferred embodiment followed by a scounng step, preferable s.n enzymatic scouring step, preferably with a scouring enzyme such as 6. pectinase, o.g., si i.'ectate lyase, a lipase, a protease, or combination thereof, and a bleaching step, prelerably iivoiving bleaching with hydrogen peroxide and/or a hyorogen peroxide generating cgent. F^^levant scouring processes are described in U.S. Patent No. 5,578,489, U.S. F^atent No. 5.912,407, and U.S. Patent No. 6,630,342. Releva.nt bleach processes are descnbed in U.S. Patent No. 5.851,233. U.S. Patent No. 5.752.980, and U.S. WO 2003/002810 (Novozymes) and WO 2003/002705 (Novozymes). According to tne present invention, fabric may be desized and demineralized simultaneously in the sarre aciueous treating solution (i.e., one bath) or subsequently in the same or two separate treating solutions (i.e., one or two baths). In a preferred embodiment the desizing and den-iinoralization are carried out simultaneously in the same treating solution {i.e., one batn). Ttie process of the invention may be carried out using traditional sizing/desizing equipment, e.g., ps.d systems, J-boxes, jets, jiggers, etc. In general, no additional process equipment is neede.'d. According to tne indention simultaneous desizing and demineralization are carried Dut by incubating ::;izi3d fabri;; in an aqueous treating solution having a pH in the range between 1 and 7 whi:;h aciueous treating solution comprises an acid alpha-amylase. In a preferred embodimenv the pH during incubation is in the range between 1 and 4, especially Detween pH 2 and 4, Woven goods are the prevalent form of fabric construction. The weaN'ing process lemands a "sizing" ol the A'arp yarn to protect it from abrasion. Starches, unmodified and nodified, polyvinyl accno. (PVA), carboxy methyl cellulose (CMC), waxes and acrylic )inders, and mixtures thereof, are examples of typically used sizing agents. The sizing igent may according to the invention be a starch-based or starch derivative-based sizing igent, but may also contain one or more non-starch or starch derivative-based sizing igents. The sizing acent(s) c.re in general removed after the weaving process as the first ;tep in preparing the vwver goods. One or more other agents including stabilizers, surfactants wetting agents, iispersing agent, seqjestering agents and emulsifying agents, or mixtures thereof, may be iresent during a desi2-.ing process of tne invention. The sized fabric is allowed to incubate in ne aqueous treating solution for a .sufficiently long period of time to accomplish desizing of ne sized fabric. The Dptimal period is dependent upon the type of processing regime and le temperature and can vary from about 15 minutes to several days, e.g., 48 hours. A process of the inven-.ic.n ^s [jreferably earned out at a temperature in the range from 5 to 90°C, in particular 20 o 9i)' C deperdent on the processing regime. The processinc racjime can be eithei batch or continuous with the fabric being contacted by the aquec^us t eating stream in open width or rope form. Continuous opsraticrs may use a saturator whereby an approximate equal weight of treating solution per vveiciht of fabric is applied to the fabhc, follovved by a heated dwell chamber where the cl'emiL;&; reaction takes place. A washing section then Drepa-es the and resulting dyeability, tiie desizing enzyme(s) and other agents must be thoroughly removed. Batch process;'33 may take place in one bath (treating solution) whereby the fabric is contacted with, e.g., approximately 8-15 times its weight of aqueous treating solution. After an incubatior period, the aqueous 'Teating solution is drained, the fabric is rinsed, and the next processing £;tep is initialed. Discontinuous PB-processes {i.e., pad-batch processes) involves a saturato; \i\\-erehy an approximate equal weight of aqueous treating solution per weight of fabhc is app ied to the fabric, followed by a dwell pehod, which in the case of CPB-process (i.e., cold paj-batcl" process) miight be one or more days. For instance, a CPB-process may be carrii^d out at betw(;en 20-40°C for 8-24 hours or more at a pH in the range between 1 and 7, pr^feral'jly at a pH in the range between around 1 and 4, especially between pH 2 and 4. Fut1h9r, a F^B process may be earned out at between 40-90X for 1-6 hours at a pH in the range between around 1 and 7, preferably between around pH 1 and 5, more preferably betvi/E^en ' and 4, especially between pH 2 and 4. In one embodiment the desizing process of the inveniion may be carried out using an effective arnoun: cf alota-amyiase, preferably acid aipha-amylase, and an acid such as acetic acid or sulphuric acic or the li The atpha-amylase(s) used in the process of the invention may be any aipha-amylase, preferably of ba<:t.erial or fungal ongin. in a preferred embodiment the aipha-amylase is an acid such as hybrid disclosed wo which hereby incorporated by reference.> in a preferred errbodiment the aipha-amylase include a carbohydrate-binding module (CBM) as defined 'n WO 2005/003311, preferably a family 20 CBM as defined in WO 2005/003311. Specifically OM-itempSated are CBMs include the ones selected from the group consisting of Aspergillus kawaciii^ :iisclosed in SEQ ID NO: 2; Bacilius flavothermus disclosed in SEQ ID MO 5: Bacillus sp, disclosed in SEQ ID NO: 6; Alcaliphilic Bacillus disclosed in SEQ ID f^JQ: ?': Horrroconis resinae disclosed in SEQ ID NO: 8; Lentinula edodes disclosed in SEQ ID NO: 9; Neurospora crassa disclosed in SEQ ID NO: 10; Talaromyces byssoc'lamydiodes (fisolosed in SEQ ID NO: 11; Geosmithia cylindrospora disclosed in SEQ ID NO: 12: Scorias spodiosa disclosed in SEQ ID NO: 13; Eupenicilliun) Penicillium of. ,'r;/c2]/n;;/c/7 disclosed in SEQ ID NO: 16; Mz1 Penicillium sp. disclosed in SEQ ID NO: 17; Thysanosvora sp disclosed in SEQ ID NO: 18: Humicola grisea var. thermoidea disclosed in SEQ ID NO: 19; Aspergillus n/ger disclosed in SEQ ID NO: 20; or Althea rolfsii disclosed in SEEQ ID l\0:21. Fungal Alpha-AmylRqn;; In an embodirfient the funga! alpha-amylase is of yeast or filamentous fungus origin. In a preferred embed irent the funcial alpha-amylase is an acid alpha-amylase. Preferred a!pt'ci-ainylases iiclude, for example, alpha-amylases obtainable from Aspergillus species, in pai1ci..ilar -Tom Aspergillus niger. A. oryzae, and A. awamori, A. kawachii, such as the acid cilona-amylase disclosed as SWISSPROT P56271, or described in more detail in WO 8S/01969 (Example 3). The mature acid alpha-amylase has the amino acid sequence shov;n es 22-5' i of SE'.Q ID NO: 4, encoded by the DNA sequence shown in SEQ ID NO: 3, or tht! amino acid serjuence shown in S' 1 ID NO: 38. Also preferrer are alpha-amylase sequerces havinci nore tlian )0%, such a mor^ than 50%, more than '0%, more than 80°o or incre- t'la- -;■: ., 'r- har* 9E":i. ";:■:: ':':..^ 96'^.-, T.G:'G "r.ar 37",. .r^o?--than 98%, or even moi'c-! thai 9:'- ■ Kiartitv io the a' wno acid sesjuence shown in Si.:Q ID NOS: 4 or 38, respectively In another prefeired eiiibodimenl .he alpha-amylase sequence is denved from an A. oryzae ac\d alpha-amylase. Mo:e preferably the alpha-amylase .sequence has mce than i30%, such as more than 6[)"/o, more the'"! 70%, more than 80% or more than 90%, more than 95%, more than 96%, more than 97%, more than 98%. or more than 99% identity to the amino acid sequence shown in SEQ ID NO: 39. In one embocimeni the alpha-amylase is the Aspergillus kawachii alpha-amylase disclosed in SEEQ ID NO: 37, which in,wild-type form contains a carbohydrate-binding domain (CBD) also shown in SEQ ID NO: 2. In a preferred ^mt'Odimefit che alpha-amylase is an alpha-amylase having more than 50%, SUL : as more t!ia,n 60"-: mijre than 70%, more than 80% or more than 90%, mere than 95%, more than 95'y The alpha-arnvlase may be present in a concentration of 1-3,000 AFAU/kg fabric, preferably 10-1,000 A-AU/ kc fabric, especially 100-500 AFAU/kg fabric or 1-3,000 AFAU/L treating solution, preferably "O-IOCO AFAU/L treating solution, especially 100-500 AFAU/L In an embocimen-; the alpha-amylase is of bacterial origin. In a preferred embodiment the bacterial a pha-amylase is an acid alpha-amylase. The bacterial aiplia-arriyiase is; preferably derived from a strain of Bacillus, such as Bacillus licheniformis, bacillus amylo'iquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or other Bacillus sp., such as Bacillus sp. NCIB 12289, NCIB 12512 (WO 95/26397), fJ IB 12513 (WO 95/26397) CSM 9375 (WO 95/26397), DSMZ 12648 (WO 00/60060), DSI^/IZ 12649 (WO 00/6006:)), KSM AF'I378 (WO 97/00324). KSM K36 or KSM K38 (EP 1,022,334). Preferred ere the Bacillus sp. alpha-amylases disclosed in WO 95/26397 as SEQ ID NOS. 1 and 2, respectively tlie /\A560 alpha-amylase disclosed as SEQ ID NO.- 2 in WO 00/60060 (i.e., SEQ ![) NO: 4C herein), and the #707 alpha-amylase disclosed by Tsukamoto etal., BJi:x±ifimkLaLaci(JJ^dQplijiSJiialJjasearnh CnmmiinicFitions, 151, pp. 25-31 (1988). In an embodiment of the in\'ention the bacterial alpha-amylase is the SP722 alpha-amylase disclosed as SEQ ID NO: 2 in WO 95/26397 or the AA560 alpha-amylase (SEQ ID NO: 40 herein). In a preferred embodiment he parent alpha-amylase has one or more deletions in positions or corresponding to the following positions: D183 and G184, preferably wherein said alpha-amylase veriant further has a substitution in position or corresponding to position N195F (using the SEQ ID NO: 40 numbering). In another preferred embodiment the parent alpha-amylase has one or more of the following deletions/substilLtions or corresponding to the following deletions/substitutions: Delta (R81-G18:2); Delta (DII33-G184); Delta (D183-G184)+N195F; R181Q-t-N445Q-t-K446N; Delta (D183-G184)+R181Q, DeltEi (D1B3-G184) and one or more of the following substitutions or corresponding to: R1 I3K. N195F, R320K, R458K, especially wherein the variant has the following mutations: A(D183-IG184)-HR118K+N195F+R320K+R458K (using the SEQ ID NO: 40 numbering) In another prefiriai-J embo:in:ien1 the alpha-amylase is the AA560 alpha-amylase shown in SEQ ID NO: 40 furilier conprising one or more of the following substitutions M9L, M202L, V214T, 1^3231", M-182Y, E345R or the A560 alpha-amylase with all of the following substitutions: M9L, M202L >'214T M323T, M382Y or M9L, M202L, V214T, M323T and E345R. Commercially availaDle alpha-amylase products or products comprising alpha-amylases inciuds p'-oouct s;old under the following tradenames: NATALASE'^'^, KEMZYM'" AT 900C) (Eiozy n Ge^s. m.b.H, Austna), PURASTAR^i^ ST, PURASTAR™ HPAmL, PURAFECT^'-' 0>AITL RAPIDASE™ TEX (Genencor Int. Inc, USA), KAM (Kao, Japan). The alpha-amylase TEIV be present in a concentration of from about 0.05-150 KNU/L treating solution, prefs-atily 1100 KNU/L treating solution, especially 2-20 KNU/L treating solution or 0.O5-150 KML/Kg fabric, preferably, 1-100 KNU/kg fabnc, especially 2-20 KNU/kg fabric. Hybrid ennyme The alpha-amylase may in a preferred embodiment be an alpha-amylase comprising a carbohydrate-binding domai i (CE5D). Such alpha-amylase with a CBD may be a wild type enzyme (see e.g., Aspergillus kawachii above) or a hybrid enzyme (fusion protein) as will be described further below hlyorid erzymes or a genetically modified wild type enzyir,es as referred to herein inciude soecies comprising an amino acid sequence of an alpha-amylase enzyme (EC 3.2.1.1) liril'ed {i.e., covalently bound) to an amino acid sequence comprising a carbohydrate-bincmg jcrain iCBD). CBD-containing hybrid enzymes, as well as detailed descriptions of the preparation and purification thereof, are known in the art [see, e.g., WO 90/00609, WO 94/24158 and WO 95/16782, as well as Giieenwood et al., Biotechnology and Bioengineering, 1994, 44: 1295-1305]. They may, e.g., be prepared by transforming into a host cell a DNA construct comprising at least a tiacment of DU^ encoding the carbohydrate-binding domain ligated, with or without a linl In the latter foniMjIa, /'-CBD i5 the N-terminal or the C-terminal region of an amino acid sequence comprising it easi the ^arbonydrate-binding domain (CBD) per se. MR is the middle region (the 'linker ), and X is the sequence of ammo acid residues of a polypeptide encoded oy a DNA seouenrje en:;ocing the enzyme (or other protein) to which the CE5D is to be linked. The moiety A -lay etner be absent (such that A-CBD is a CBD per ss, i.e., comprises no amino acid residues ct-Kjr than those constituting the CBD) or may be a sequence of one linker (MR) may be a bona, or a stiort linking group comprising from about 2 to about 100 carbon atoms, in pai-:iou!3r of from 2 tc 40 carbon atoms. However, MR is preferably a sequence of fror"n abojt 2 to about lOO amino acid residues, more preferably of from 2 to 40 amino acid residues, sjch as from 2 to 15 amino acid residues. The moiety X ma/ constitule either the N-terminal or the C-terminal region of the overall hybrid enzyme. It will thus be appareint from The above that the CBD in a hybrid enzyme of the type in question may be positioned C-lerrninally, N-terminally or internally in the hybrid enzyme. Linker sequence The linker se snce may be any suitable linker sequence. In preferred embodiments the linker sequence is ck'.':\\/e6 from the Athelia rolfsii glucoamylase, the ,4, niger glucoamylase, the A. kawachi: alpha-amylase such as a linker sequence selected from the group consisting of A. niger glucoamylase linker: TGGTTTTATPTGSGSVTSTSKTTATASKTSTSTSSTSA (SEQ ID NO: 22), A. I A carbohydrate-binding domains (CBD), or as often referred to, a carbohydrate-binding modules (CB^/I), is a polypeptide amino acid sequence which binds preferentially to a poly- or oligosacchcride icarbohyjrate), frequently - but not necessarily exclusively - to a water-insoluble (inducing c-y;-;talline) form thereof. CBDi ierived 7om .starch de^grading enzymes are often referred to as starch-binding domains (SBD) or stsircf-lsirding inodules (SBM). SBDs are CBDs which may occur in certain amylolytic eni'ytres. such as certain glucoamylases, or in enzymes such as cyclodextrin glucaroransferases, or in alpha-amylases. Likewise, other sub-clas: 3S of CBDs would embraco, eg., cellulcse-binding domains (CBDs fron-; cellulolytic enzymes), (CBDs which typically occur in xylanases), mannan-binding domains (CBDs which t/oically occur in mannanases). CBDs are fouiicl as irtsgral parts of large polypeptides or proteins consisting :A two or more polypeptide amino acid sequence regions, especially in hydrolytic enzymes (hydrolases) which typical y complse a catalytic domain containing the active site for substrate hydrolysis and a carbohydrate-binding domain (CBD) for binding to the carbohydrate substrate in question SJuch enzymes can comprise more than one catalytic domain and one, tuo or three CBDs, and optionally further comprise one or more polypeptide amino acid secuence regions linking the CBD(s) with the catalytic domain(s), a region of the laner tyize usually being denoted a "linker". Examples of hydrolytic enzymes comprising a CBD - ;;om5 of whicti tiave already been mentioned above - are cellulases, xylanases, rnannanas'r'S, aia.Dinofuranosidases, acetylesterases and chitinases. CBDs have also been found in agae, e.g., in the re)d alga Porphyra purpurea in the form of a non-hydrolytic polysaccharider-binding protein. In proteins/polypeplides in which CBDs occur (e.g., enzymes, typically hydrolytic enzymes), a CBD nay be located a! the N or C terminus or at an interna! position. That part of a polypeptide or protein (e.g., hydrolytic enzyme) which constitutes a CBD per se typically :onsi:5ls of miore than about 30 and less than about 250 amino acid residues. The "Carbohyij-ate-Ending Module of Family 20" or a CBM-20 module is in the context of this invention detiited as a sequence of approximately 100 amino acids having at least 45% homology ti the Carbohydrate-Binding Module (CBM) of the polypeptide disclosed in figure 1 by Jcergenser et al (1997) in Biotechnol. Lett. 19:1027-1031. The CBM comprises tne last 1C2 amino acids of the polypeptide, i.e., the subsequence from amino acid 582 to amino acid 68-3. The numoering of Glycoside Hydrolase Families applied in this disclosure fofows ttie concept of Ccutinho, P.M. & Henrissat, B. (1999) CAZy - Carbohydrate-Active Enzymoi^ server at URL: http://afmb,r,nrs- (shiitake mushroom) such as the CBD of SPTREMBL:Q9P4C5 (SEQ ID NO: 9). from Neurospora sp, SLicfi as from Weurcspora crassa such as the CBD of SWIRSPRnr-Pi48.04 (SEQ ID NO: 10), fr::irri nui^omyces sp. such as from Talaromyces byssochlamydioides such as the CBD froTi MM005220 (SEQ ID NO: 11), from Geosmithia sp. such as from Geosmith/a cylindrosfjora. such as the CBD of NN48286 (SEQ ID NO: 12). from Sconass^. such as Uon\ Sooiias sponciosa suci as the CBD of NN007096 (SEQ !D NO: 13). from Eupenicillium sp. sucfi as from Eujzeniciliium ludwigii sucti as the CBD of NN005968 (SEQ NN001136 (SEQ ID I-ID: 15i, from Fenicillium sp. such as from Penicillium cf. miczynskii such as the CBD of Nhi48691 (SECj ID NO: 16), from Mzl Penicillium sp. such as the CBD of NN48690 (SEQ ID NO: 17), from Thysanophora sp. such as the CBD of NN48711 (SEQ ID NO: 18), and from Humicola sp. such as from Humicola grisea var. thermoidea such as the CBD of SPTREMBL:012623 (SEQ ID NO: 19). Most preferred CBDs include the CBDs of the glucoamylase from /'As,De/p/7/js sp. such as from Aspergillus niger, such as SEQ ID NO: 20, and Athelia sp. such as from Athelia rolfsii, such as SEQ ID NO: 21. Also preferred accordinci to the invention are any CBD having at least 50%, 60%, 70%, 80% or even at least 90%, 95%, 96%., 37%. 98"o, or 99%. identity to any of the afore mentioned CBD amino acid sequences. In a preferred embodiment the carbohydrate-binding domain and/or linker sequence is of fungal origin. The carbohydrate-binding domain may be derived from an alpha-amylase, but may also be derived from of proteins e.g., enzymes having glucoamylase activity. In an embodiment the alpha-amylase is derived from a strain of Aspergillus, or Athelia. In an embodiment tl-ei alphEi-amylase is derived from a strain of Aspergillus or^'zae or Aspergillus niger. In a sDuci'c embDdiment the alpha-amylase is the A. oryzae acid alpha-amylase disclosed m SEC ID NO: 39. In a specific embodiment the iinker sequence may be derived fronr. a strain d Asperjillus, such as the A. kawacliii alpha-amylase (SEQ ID NO: 23) or the A. rolfsii giucoa-nvlase [SEQ ID NO: 24). In an embodiment the CBD is derived from a strain of Aspergillus or Atlielia In ci specific embodiment the CBD is the A. kawachii alpha-amylase shown in SEIO 10 MO: 1 onhe A. ro/r's/7glucoamylase shown in SEQ ID NO: 21. Preferred is the rnibodiment wherein the hybrid enzyp'.e comprises ar alpha-amylase shown in SEQ ID NCJ: 38, and/or a Iinker sequence derived from the A. kawachii alpha-amylase shown in E;E :' 10 MO: 23 or the A. rolfsii glucoamylase shown in SEQ ID NO: 24, and/or the CBD is derived frDrri the /.. /can/ac/7/7 alpha-amylase shown in SEQ ID NO: 2, the A. rolfsii glucoamylase stiown in SEQ ID NO: 21 or the A. n/per glucoamylase shown in SEQ ID NO: 22. In a preferred embodiment the hybrid enzyme comprises the A. niger acid alpha-amylase catal^lic dorain having the sequence shown in SEQ ID NO: 38, the A. kawachii alpha-amylase linker sho\A;i ii SEQ D NO: 23, and A. /caiiacM alpha-amylase CBD shown in SEQ ID NO: 2. In a specific EITII)xiiirent the hybrid enzyme is the mature part of the amino acid sequence shown in SE:Q ID fvIO: 28 [A. niger add alpha-amylase catalytic domain-/^, kawachii alpha-amylase linl In another preferred embodment the hybrid enzyme has an amino acid sequence which differs from the amino acid sejquence amino acid sequence shown in SEQ ID NO: 28 {A. niger acid alpha-amylase catalytic domain-/^, kawachii alpha-amylase linker-/,, niger glucoamylase CBD)^ SEQ ID NO: 30 {A. niger acid alpha-amylase catalytic domain-/^. /(aivacM alpha-amylase linker-/l. roife/7 glucoamylase CBD), SEQ ID NO: 32 {A. oryzae acid alpha-amylase catalv'li:; dona,0-4, ^aivac.*?//alpha-amylase linker-4. /cai^ac/?//alpha-amylase CBD), SEQ ID NO: ::!4 \A. n/ge;acid =lplia-amylase catalytic dcmain-/\. ro/fe//glucoamylase linker-/l. /•o//s/ygluccai- /lase CBD) cr SEQ ID NO; 36 {A. oryzae adc^ alpha-amylase catalytic domain-/\. roifsii glucoarrylasc) linker-/i. rolfsii glucoamylase CBD) or the hybrid consisting of A. nigeracjcl alpha-an^vlase catalytic domain (SEQ ID NOS: 4 or 38, respectively)-^, kawachii glucoamylase iinker (oEQ ID NO: 23) -A. kawachiglucoamylase CBD (SEQ ID NO: 2) in no more than 10 postio- 5, no more 1hE;n 9 positions, no more than 8 positions, no more than 7 more than 3 positions, rio more than 2 positions, or even no more than 1 position. Preferably the |-ybrl(j E.'nzyiTie comprises a CBD sequence having at least 50%, 60%, 70%, 80% or even at least 90%, 95%, 96%, 97%, 98%, or 99% identity to any of the amino acid sequences shown in SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10. SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14. SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO: 20 or SEQ ID NO: 21. Even more preferred the hybrid enzyme comprises a CBD sequence having an amino acid secuence shown in SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO: 13, SEQ ID NO: 14, SEQ ID NO: 15, SEQ ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID HO: 20 or SEiO ID NO: 21. In yet another preferred emboo rent the CBD sequence has an amino acid sequence which differs from the amino acid sequence amino acid sequence :;hovvn in SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, SEQ ID NO: 12, SEQ ID NO; 13, SEQ ID NO: 14, SEQ ID NO: 1!5, SEC ID NO: 16, SEQ ID NO: 17, SEQ ID NO: 18, SEQ ID NO: 19, SEQ ID NO 20 or SEQ 1) NC^: 21 in TO more than 10 ammo acid positions, no more :nan 9 positions, no mort; than 3 pcis:tions, no more than 7 positions, no more than 6 positions, no more than 5 positions no noie than 4 positions, no more than 3 positions, no more than 2 positions, or even no moretiari 1 position. In a most preferred embodiment ttie hybrid enzyme comprises a CBD derived from a glucoamylase from A. roifsii, such as the glucoamylase from A. ro/fe/7 AHU 9627 disclosed in U.S. Patent No. 4,727,026. Acid scouring enzymes Any acid scouring enzyme nay be used according to the invention. The acid scouring enzyme may be an sacid enzyme selected from the group consisting of pectinase, cellulase, lipase, procease, xyloglucanase, cutinase and a mixture thereof. A scouring l enzynne is "acid" n iion.ext oi the present invention when the pH optimum under the conditions presen-; djiing BUTultaneously desizing and sec uring is below 7, such as betv^/een 1-7, prefe;-ably be'ow :5 such us betA'een 1-5, especially btiow 4, such as between 1-4^ Various scour:nig enzj/rnes a'e l gaiacturonice)giycanohyd-cis&e. Pectin lyase iE:C '1.2,2,10) catalyzes the eliminative cleavage of (1,4)-a!pha-D-galacturonan methyl ester to ewe ohgosaccharides with 4-deoxy-6-0-methyl-alpha-D-galact-4-enuronosyl ciroups =,t their nL)n-re(lui:inci ends. Examples of other names are: Pectin trans¬eliminase; polyrnethycialactu'onic transeliminase; and pectin methyitranseliminase. The systematic name is (1 4j"6-D-methyl-alpha-D-galacturonan lyase. Pectate; lyase (EiC ■-•,2.2.2) catalyzes the eliminative cleavage of (1,4)-alpha-D-galacturonan to give; jligosaccharices with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing snds. Erxarnples of other names are: pectate transeliminase; polygalacturonic trariBeiirninase: and endopectin methyitranseliminase. The systematic name is (i ,4)-alpha-0-galacturonan lyase. Pectiresterase [EC 3.'.1.11) catalyzes the reaction: pectin + n H2O = n methanol + pectate. E: The EC numberfriQ is according to the Recommendations of the Nomenclature Committee of the Internatic lal Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzyme-Catalysed Reactions published in Enzyme Nomenclature 1992 (Academic Prejss, £;an Diego, California, with Supplement 1 (1993), Supplement 2 (1994) Stpptement 3 (1995), Supplement 4 (1997) and Supplement 5 (in Eur. J. Biochem. 1994, 223: 1-5; Eur J. Biochem. 1995, 232: 1-6; Eur. J. Biochem. 1996, 237: 1-5; Eur J. BiccheiT. 1997, 250: 1-6, and Eur. J. Biochem. 1999, 264: 610-650; respectively). I'L-- In a preferred eniJDodiinent :he acid pectinase is a pectate lyase, a pectin lyase, a polygalacturonaije, or a .loi/g; lacturonate lyase. The tern- "pectinase' i; intended to include any acid pectinase enzyme. Pectinases are a group of enzymes tlic.v hydrolyse glycosidic linkages of pectic substances mainly poly-1,4-alpha-D-gala,c1urorii'Js:; and i-:s derivatives (see reference Sakai et al., Pectin, pectinase ana propectinase prodjction, properties and applications, in: Advances in Applied Microbiology. Vol. Gi9. OD. 213-294 (1993)) which enzyme is understood to include a has the activity of ti'G fijl-;e igth enzyme. Furthermore, the term pectinase enzyme is intended to include hoinoiCigues or analogues of such enzymes. Preferably the ccid pe;;tit-ia£;(5 is an enzyme which catalyzes the random cleavage of alpha-1,4-glycosidic linkages in pectic acid also called polygalacturonic acid by transelimination such as the enzyms class polygalacturonate lyase (EC 4.2.2.2) (PGL) also known as poly(1,4-al:pha-D-cialacturonide/ lyase also known as pectate lyase. Also preferred is a pectinase enzyme Vihich ca:alyzes the random hydrolysis of alpha-1,4-glycosidic linkages in pectic acid such as the einzyme class polygalacturonase (EC 3.2.1.15) (PG) also known as endo-PG. .Mso preferred is a pectinase enzyme such as polymethylgalcturonate lyase (E-IC 4.2,2.10) (l^MGL), also known as Endo-PMGL, also known as poly(methyoxygalactux)nid(i)lyase also known as pectin lyase which catalyzes the random cleavage of alpha-1,4-glycosidic linkages of pectin. Other preferred pectinases are galactanases (EC 3.2,1.89),, arabip.'jnases (EC 3.2.1.99), pectin esterases (EC 3.1,1.11), and mannanases (EC 3,2 1,' ; For the purposes.: of tl iiveiivon, tiie source of t;)." aljove enzyme.:?; inciu ^^ng pectin lyase, pectate lyaa;; ;r ■:■-■.. "-:,:^;S;::; r ".. c;ii:,:ai, .2., thv en::yr'-- I-H; -. ::,::.arTj from a plant, an anitna,, or \ rnicrtijrgisiii&rn such E .^ bacteriuni 01 a furijus, e.g., a filamentous funous or ,: yeast The enzymes mny, e.g.. on obiainoii from these Gourc ■ s by use of recombinant DIMA ^ocl :i!'.|ues as i;- knovv'ii in tlie a The pectinase may be a component occurring in an enzyme system produced by a given micro-orcanisni, such an enzyme system mostly comprising several different pectinase component;; inclucii ig those identified above. Alternatively, IIK? oe-y. nase may be a single component, i.e., a component essentially free of other pectinase t nzyrnes whichi may occur in an enzyme system produced by a given micro-organism, "he single acniponent typically being a recombinant component, i.e. produced by cloning or a ONA sequence encoding the single component and subsequeni enzymes, especially pectinase, peciin lyases and polygalacturonases are described in detail in, e.g., WO 93/120193 WO 02/092741, WO03/095638 and WO 2004/092479 (from Novozymes A/S) A'l-iich ai'e hereby incorporated by reference in their entirety including the sequence listings. The host is preferably a heterologous host, but the host may under certain conditions alsc oe ttie homologous host. In a oreferred e Titodiment the pectinase used according to the invention is derived from the genus Aspes'/'llus. In a still prefer-ed einciodime^ni, the pectinase is the protopectinase having an amino acid sequence of SEC' ID NO: 1 of u P 11682877 or the protopectinase having an amino acid sequence generated i:iy dslE^tion, substitution or insertion of one amino acid or several amino acids in the anino acid sequence and having an activity at the same level as or a higher level than the level cf trie activity of the protopectinase with the amino acid sequence of SEQ ID NO: 1 of JF' 11 382877. The pectinase, suci as especially pectate lyase, may preferably be present in a concentration in the range from 1-1,500 APSU/kg fabric, preferably 10-1,200 APSU/kg fabric, especially "00-1 OCC APSU/kg -'abric. Commercially a\'a;lcible acid pectate lyases according to present invention include Pectinex® BE XXL, Pec:inexCR) [5E Colour, Pectinex® Ultra; Pectinex™ Ultra SP-L, Pectinex®' Yield Masi. F^ectinex® XXL, Pectinex® Smash XXL, Pectinex® Smash, Pectinex^'^ /\R froiTi Novozymes A/£, Denmark. Proteases Any protease suitable for Lse in acid solutions can be used. Suitable proteases include those of an rnal, ve^getatte or microbial origin. Microbial origin is preferred. Chemically or genetic Bacillus clausii, e.g.. sjolilsir Novo, subtilisin Carlsberg, sub; :sin 309, subtilisin 147 and subtiiisin ^33 (descriD'sd in AM;) S9/C6279I. Preferred cornmerc ally avalaole protease enzymes include those sold under the trade names ALCAL.,=.SE""'v, SAVINASET^ 16 L Type Ex. PRIMASE™, DURAZYM™, and ESPERASETi-i (Ncvcizyrn>:)S A/S, Denmark), those sold under the traoename OPTICLEAN^"'^', 0Fn'MA3E'\ PFOPARASE™, PURAFECT™, PURAPECT™ MA and PURAPECT™ OX, PURAFECT™ OX-i and PURAFECT™ OX-2 by Genencor Internal ona: In an embodiment of the prDcess of the invention a protease may be present in a concentration from 0.00--10 KMPU/L, oreferably 0.1-1 KNPU/L, especially around 0.3 KNFU/L or 0.001-10 HlJPU/kg fabric, preferably 0.1-1 KNPU/kg fabric, especially around 0.3 KNPU/kg fab'ic. Lipa.ses Any lipase sui:abli5 for use in acid solutions can be used. Suitable lipases include those of bacterial or f jigal origin. Chemically or genetically modified mutants are included. Examples of useful lipaE;es include a Representative acid lipase enzymes include Lipolase.TM., Lipolase.Tiyi. Ultra, Palatase.TM. A, Palatase.TM. M and Lipozymie.TM. commercially available from ^Jo . ■ Industri A/'S. These acid lipase enzymes are 1,3-specific lipase enzymes that hydrclyze the fatty acid at the 1 and 3 position of the triglyceride. Another representative acid lipase enzyme is the Yeast Lipase-BCC commercially available from Bio-Cat, Inc. This enzyme is derived from a select strain of Candida cylindracea and is a non-specific lipase enz/me which hyd^olyzes the fatty acid at all three positions of the triglyceride. In an embodir ent ol the process of the invention a lipase enzyme may be present in a concentration from 0,01-100 LU/L treating solution, preferably 1-10 LU/L treating solution, especially around 1 LU/L treating solution or from 0.01-100 LU/kg fabhc, preferably 1-10 LU/kg fabric, especiaHy around 1 LU/kg fabric. In the present content, the term "cellulase or "cellulolytic enzyme" refers to an enzyme, v^/hich catary5;es the cegradation of cellulose to glucose, ceilobiose, triose and other cellooligosaccharides. Cellulose is a polymer of glucose linked by beta-1,4-glucosidic bonds. Cellulose chains form lumerous irrra- and intermolecular hydrogen bonds, which result in the formation of insoluble cellulose microfibhis. Microbial hydrolysis of cellulose to glucose involves the foliowinci th-ee major classes of cellulases endo-1,4-beta-glucanases (EC 3.2.1.4), which claa'v'o bet«:-'L4-glucosidic links randomly throughout cellulose molecules; cellobiohvdrolases {ciC 3.2.1.91) (sxoglucanases), which digest cellulose fron the nonreducing end; and beta-glucosida&es (EC 3.2.1.21), which hydrolyse cellobiose and low-molecular-mass celloaaxtn-iE; to release glucose. Most cellulases consist of a cellulose-binding dorT,ain (CBD; and a caialylic domain (CD) separated by a linker rich in proline and hydroxy arnrc acid rosidj(5S. In -fo specification and claims, the term "endogiucanese" is activity, which are classified in EC 3.2.1,4 according to the Enzyme Nomenclature (1992) and are capable of c£taly;:ing lendoihydrolysis of 1.4-beta-D-glucosidic linkages in cellulose, lichenin and ce'eal beta-D-glucans including 1.4-linkages in beta-D-glucans also containing 1,3-linkag(!S. Any cellulase suitable for use in acid solutions can be used. Suitable cellulases include those of bacterial or fungal origin. Chemically or genetically modified mutants are inciucled,, Eiuitable cellulases are disclosed in U.S. Patent No. 4,435,307, which discloses fungal cellulases produced from Humicola insolens. Especially suitable cellulases a-e tha cellulc.ses having colour care benefits. Examples of such cellulases are cellulases cesicribecl in Eluropean patent application No. 0 495 257, WO 91/17243 and WO 96/2939 7. The acidic cellulase enzyme specific to hydrolysis of the polymehc cellulose produced by Acetobacter biscteria can be derived from certain strains of Trichoderma reesei or Aspergillus niger, o\- their mutants or variants either naturally or artificially induced. As used herein, Trichodernia: leesei denotes microorganisms known by that name, as well as those micro(;fganisms classified under the names Trichoderma longibrachiatum and Trichoderma virida. Any celij^ase enzyme or enzyme complex that is specific to hydrolysis of cellulose produced oy Acetobacter bacteria can be used. A representati\'(; acid cellulase enzyme is the Cellulase Tr Concentrate multi-eizyme acid cellulase comple):, which is commercially available from Solvay Enzymes, Inc. Cellulase Tr Concentrate is a food grade cellulase complex obtained by controlled fermentation of a selected strain of Tncnoderma reesei. This enzyme complex consists of both exoglucanases and endoglucanases that (iirectly attack native cellulose, native cellulose derivatives, and soluble cellulose deri^'stives. This enzyme coriiplex specifically hydrolyzes the beta-D,4-glucosidic bonds of bacterial cellulose, in particular the polymeric bacterial cellulose produced by Acetobacter bacteria, as well as its oligomers and derivatives (U.S. Patent No. 5,975,095). Another repr-sentati^'a oeluase enzyme commercially available from Solvay Enzymes, in:, ; Gellulesa TRL, multi-enzyme liquid cellulase complex. Cellufase TRL cellulose enzyn-ie compieix is rieri\'ed from Trichoderma reesei in the same mar-ner as Cellulase T- Concenlrate snzyrie complex, but is prepared and sold in liquid form. Its activity against bact-Erial eel ulose has been demonstrated to be equivalent to that of Celiuiase Tr Concentrate erizyme complex. Orier suitable er-zymes --or use in the present invention include Celluzyme Acid P Cellulase 300 enzyme, commercially available from Genencor International, and Rapidase.RTM. Acid Cellu'~9 enzyme, commercially available from Gist-Brocade:5 B. V. Still other cellulase enzymes or cellulase enzyme complexes are suitable for use in the present invention, provided Jiey exhibit specific hydrolytic activity directed at the beta-glucosidic linkage characteristic of the polymeric bacterial cellulose produced by microorganisms such as /\ce :obact£r bacceria (U.S. Patent No. 5,975,095). In an emibodimenl i;)f the piocess of the invention the cellulase may be used in a concentration in the range from 0.001-10 g enzyme protein/L treating solution, preferably 0.005-5 g enzyrno pnjtein/i. treating solution, especially 0, i1-3 g enzyme protein/L solution or from u.001-10 g enz/rre prc-icjin/kci fabric, preferabiy 0.005-5 g enzyme protein/kg fabric, especially 0.01 -3 g emyrrie pictein/kg fabric, in an > rnbocliment the cellulose is used in a concentration cf from 0,1- iK)0 ECU/g fabric, r^'feraljly 0.5-200 ECU/g fabric, especially 1-500 ECU/G fcl:):ic. Cijtinase Exarnp-'es oi cutinaiies are ihose derived from Humicola insolens (U.S. Patent No. 5,827,719); from a stram of Fusarium, e.g., F. roseum culmorum, or particularly F. solanipisi (WO 90/09446; WO 194/14964, WO 94/03578). The cutinase may also be derived from a strain of Rhizoctonia., e.g., R. solani, or a strain of Alternaria, e.g., A. brassicicoia (WO 94/03578), or variants thereof such as those described in WO 00/34450, or WO 01/92502. The cutinase may as;;) be Df oacterial or gin, such as a strain of Pseudomonas, preferably Pseudomonas mendocina (li::;c;loged ir: WO 01/34899. The cutinase :--3.v bo deled in a conceniration of 0.001-25,000 micrograms enzyme protein/gram fabric, p-fife-ably 0.01-10,000 micrograms enzyme protein/g fabric, especially 0.05-1,000 micrograTis enzyire prc):ein/g fabric. solubilization of xyloglucco lo xyloglucan oligosaccharides. According to lUBMB Enzyme Nomenclature {2003 a ^./logiucanase is classified as EC 3.2.1.151. Pauly et al. (Glycobiology, 1999, i:i:93-100) disclose a xyloglucan specific endo-beta-1,4-glucanase from Aspergillus aculeatus. i\ x/logiucanase used according to the invention may be derived from micro-organisrns sue!' as furiCji or bacteria. Examples of uselul xyloglucanases are family 12 xyloglucan hydroly/.ing endoglucanases, in particular famiK' 12 xyloglucan hydrolyzing endoglucanases, obtisined from, (9.(7., Aspergillus aculeatus as described in WO 94/14953. Another useful exarnplsj is a >i/loglucanase produced by Trichoderma, especially EGIII. The xyloglucanase may a so be (;!erive(d Tom a bacterium from the genus Bacillus, including Bacillus licheniformi's, BacilA:^, aga!c\dnarens or Bacillus firmus. The xyloglucanase may also be an endoglucanase v;il.h ;!vl;)glucc.nase activity and low activity towards insoluble cellule ■? and high activity towards f-oluble cellulose, e.g., family 7 endoglucanases obtained fror e.g., Humicola insoiers. The xyloglucanase • ' y be added i;: a coiicentivioii of 0.001-25,0(iO micrograms enzyme protein/gram fabric iisferably 0.0 10,000 rpicograns enzyme proiein/g fabric, more prefe'ably CC:-1'>:; ::;--:'3rH ■:; ■:■•-•::: y^\. ■';: •■abnc^ i- 08ry:\ar 0,o-50C micrograms enzyme |:rot6,ih yiai- fibri... Composition of the in^entiQ:I In the second cispe::t ihe indention relates to a ciinpL sition suitable for use in the process of the inventicn. The composition may be a solid o; iiquid (aqueous) composition and may be a concenlrated composition or a ready-to-use composition. Ttius, in this aspect the invention relates to a composition comprising an acid alpha-amylase and an acid scouring enzyme. The enzymes comprised may preferably be the ones mentioned in the "Enzymes" section above. In a preferriEiO' emhe'Climerit the acid alpha-amylase derived from a strain of Bacillus sp., preferably from a strain jf El. lichdniformis, B. amyloliquefac'^'-ns, B. stearothermophilus, Bacillus sp. NCliB 12289^ Ni;:tB 12512, NGIB 12513 or DSM 9375, or DSMZ no. 12649, KSM API378, or KSM K36 ar KSM K38. The Bacillus alpha arnylasE may be a variant having one or more deletions in positions D18o and G i 34, respectivsly, and may further have a substitution in position N195F (using SEQ ID NO' - nimbering). The Bacillus alpha-amylase variant may also be one ot the tolicwing £ub5;itLJtioris: Rri8K, N195F, R320K, R458K (using SEQ ID NO: 6 numbering). Specifically tii;;' Bacilhjs vari,ant may have a double deletion in positions D183 and G184 and further comprise the folloA/ing ^substitutions: R118K-HN195F-fR320K-^R458K (using SEQ ID NO: 6 numbering) The acid sccuirinc en2ynne(s) is(are) selected from the group consisting of: acid pectinase^ cellulase, lioase, protease, cutinase, xyloglucanase, and mixtures thereof. In a iDreferrecl enitodirnent the acid pectinase is a pectate lyase, preferably a pectate lyase derived fi'orn a strain of Bacillus, preferably a strain of Bacillus licheniformis, Bacillus alcalophilus, Bacillus pseucloalcalophilus, and Bacillus clarkia, especiailiy the species Bacillus licheuifcrrJs. Further agents s.iiiabie for the process to be performed may be added separately or be comprised in the con"ipo3ition cf the invention. Examples of such agents include stabilizer, surfactant, ^\'etlirig agent dispersing agent, sequestering agent and emulsifying agent and mi: Liquid enzyme preparations may, for instance, be stabilized by adding a polyol such as, e.g., propylene glycol, a sugar or sugar alcohol or acetic acid, according to established methods. Other en:^yme stabilizers are weW known in the art. Protected enzymes may be prepared accordino to the nie:hod disclosed in EP 238 216. In principle the corn;;)o.>itir:i of the invention comprising an acid alpha-amyiase and a scouhng enzyme n-.a^ coitair ; ly Dther agent to be used in the combined process: of the invention. The composition of the invention comprises in a preferred embodiment at least one further component stElectecl from tne group consisting of stabilizers, surfactants, wetting agents, dispersing agBnts, sequesie' ng agents and emulsifying agents. All of such further components su^-.ab'^e r)r Textile use ar^. well know in the art. The wetting agent seves to improve the wettability of the fibre whereby a rapid anc even desizing and scouring may be obtained. The emulsifying agent serves to emulsify hydrophobic impurities present on :he fabric. The dispersing agent serves to prevent that extracted impurities recJepcsit on the fabric. The sequestering agent serve to remove ions such as Ca, Mg and -e. which may have a negative impact on the process and preferred examples include caustic soda (sodium hydroxide) and soda ash (sodium carbonate). Use Qf thiiLQmjCiasjJj^iijiXiLlhiLjjiyaDliQJi In the third asoeot the invention relates to the use of the composition of the invention in a simultaneousi di:isi.?.ing and scouring process, preferably the process of the invention. In a preferred embodinent the composition of the invention is used in a process of the invention. The invention descrbed and ciaimied herein is not to intend to limit the scope by the specific embodiments he'ein disclosed, since these embodiments are intended as Illustrations of seve'ai aspects o^ th5 nvention. Any equivalent embodiments are intended to be within the scop(3 of tnis invention. Indeed, various modifications of the invention in addition to those shown ard described herein will become apparent to those skilled in the art from the foregoing description. Sluch modifications are also intended to fall within the scope of the appended claims. In the case of conflict, the present disclosure including definitions will control. Various references an: cited herein, the disclosures of which are incorporated by reference in their entireties. Materials; & Methods Buffer SLtiaj^iiiiicQiiliiaiiikliiiiiiiLtkLiiiQaii Siubstrate: Soluble starch, approx. 0.17 g/L Buffer: Citrate, approx, 0.03 M Iodine (12): 0.03 g/L CaCb; 1.85 mM pH: 2.50 + 0.05 Reaction time: 23 seconds Vv'avelength: 590 nm Enzyme concintraliciv. 0.025 AFAU/mL Enzyme work rig range: 0.01-0.04 AFAU/mL A folder l-J.hIM:l}251W2iQ:. describing this analytical method in more detail is available upon request to Novozymes A/S, Denmark, which folder is hereby included by reference. The amylolylic ecti/itv may be determinec using (4,6-ethy!idene(G7)-p-nitrophenyl(Gl)-aT}-rnallohep:aoside (ethylidene-G7PNP) as substrate. This method is based on the break-down of e1hylicene-G7PNP by the enzyme to glucose and the yellow-colored p-nitrophenc'l. The rai-: of lormation of p-nitrophenoi can be observed by Konelab 30. This is an expression of th c;ac:tion rate and thereby tlie > n,zyme activity. The enzymf r: :^'-;y ::■ : .■^--ril-e: 'e^^-^ve :o a: ■ "'v ■■: Siandai^d. 1 FAU -s c -'i/iod as the amount of enzyn,r -NUCU d'^grao-s 5.260 rng E u^ch :irv' mat- r per hour undL-- the belo\A mentioned Stan:iaiTj r:(: ,;ci.tioriG. i^eaction condition Temperature 37-0 pH 7.15 Substrate concentrcition 1.86 mM Wavelength 405 nm Reaction time 5 min Measuring time 2 min Enzyn'ie concentration 0.46 - 2.29 mFAU(F)/ml A folder kBi'jJvt-il^L!.iiIl^iJ:i describing this analytical method in more detail is available upor requ&;5i !:o Nowzymes A/S, Denmark, which folder is hereby included by reference. lii[laLLQi.E£C::JN,L'^.AN.SELJM!NASF AHTIVITY (\ IPTF^ The acid pectinase activity rray be determined by degrading an Obipectin solution Reaction; Substr.cite concentration Tempe'atu'e pH Readier! tims Absorb a nee 0.5% Obipectin 30°C 5.4 10 minutes 238 nm One pectin transel mmase unit (UF'TE) is defined as the amount of enzyme \iA\\ch raises absorbance by 0.0' ;;i!::>sorbance units per minute under standard conditions. A folder EBz:M:i)2£).hl}2.iQ:. describing this analytical method in more detail is available upon requer^t to Movozymes A/S, Denmark, which folder is hereby included by reference. Determination of PniyCrlrKlijionase acivity (PGIJ) The acivir/ of ac c pectinases may be determined by degrading polygaiacturonic acid relative to an en.77Tie s;tandard under the conditions given as below: Buffer Polygaiacturonic a: d pH Temperature Time Polygalacturonase Sample concentration Reaction conditions Phosphate, 70 mM; Citrate 30 mM d 19g/L 3.5 30 °C 30 minutes 400 PGU/L Dn 9 PGU/mL Upon degradatior of poiygalacturonic acid, the viscosity will reduce, which is prc'Dortional to Polygacicturrjruse activity in the unkr.own samples. A folder Hi:Si;/liL!£,Ll.5. 2 ciescribing this analytical method in more detail is available upon request to Novciryrnes ,.^/S, Denmark, which folder is hereby included by reference. Dfi>sizino (]JiafiyiiaiQ£:.:Lijj:) The starch &ize resi jue is determined visually by comparing an iodine stained fabric stain. The iodine stain sDlurion is made by dissolving 10 g Ki in 10 ml water, add 0.635 g I2 and 200 mL ethanci in deioni.-zec! water to make total 1 L solution. A fabric sample is cut and immersed in the iodine solution for 60 seconds and rinsed in deionized water for about 5 seconds. The fabric sample is rated by at least two professionals after excess water in the sample is pressed out. An average number is given. Method and standard scales obtainable from Verbaro TfiiGEWA, Karlstrasse 21, Frankfurt a.M., Germany. The pectin residue on fabri:; iwas determined quantitatively. The principle is that ruthenium red binds to polyanionio compounds like unmethylated pectin. The level of pectin on the fabric is proportional to the concentration of ruthenium red on the cotton fabric which is linearly proportional to Ku belka-Munk function {i.e., K/S). The coloi reflectance (R) of ruthenium red E;tained fabric was measured at 540nm (Macbeth colorimeter. Model # CE-7000) and automatically calculated into a K/S value by: 1 The "/o pecTin 'erovaS was caiculatea using the following formula: %-pectin removal = - % Res. Pectin = 1- 100 * (K/S - K/So)/(K/Sioo- K/So) where K/S100 was froiTi fabrc with 100% pectin, typically original untreated fabric, while K/So was from the fabric vvilh 0% residual pectin, typically heavily scoured and bleached fabric. Based on information from John H. Luft and described in an article "Ruthenium red and Violet 1. Chemistry" 1971 .he stain solution was prepared by dissolving 0.2 g/l ruthenium red, 1.0 g/l ammonium chloride, 2.5 ml/I 28% ammonium hydroxide solution, 1.0 g/l Silwet L-77, and 1.0 g/l Tergitol 15-S-12 in distilled water to make total liter solution. The solution was made daily before use. During staining, 100 mL dye solution was used for 1 gram of fabric. The fabric sv>/atches were incubated in ruthenium red solution for 15 minutes at room temperature. The sv/atci was rinsed in a strainer and then hnsed in distilled water (100 ml/1 gram fabric) at 60"C for 10 minutes. The color reflectance was measured after dry. Eilatilit,: Fabric \A/ettability v/c;£; measured tsing a drop test method according to AATCC test method 79-1995. k jrop :)f «va1er was allowed to fall from a fixed height (1 cm) onto the taut surface of a lest sped Tien. The time required for the specular reflection of the water drop to disappear vvas ineasLi-ed and -ecorded as wetting time. The wicking iieign'i of "e>niies is one of the indicators for absorbency. Cut a rectangular fabric swia:ch 25 cm (warp and weft direction) X 4 cm. If the sample is not available in this size ci (ist. adjust the method to fit the sample. Using a waterproof/dye-proof pen, draw a line across ihe top of the sample 1.5 cm from the top of the swatch and 3 cm from the bottom o1 the .sample. (Draw a line across the sample 19 cm from the bottom of the swatch. Attacli a pap'or clamp with a weight to the bottom of the fabric. Place the top of the swatch in the csnter of the thermometer clamp, so that the line is at the bottom of the clamp. Fill a beal-.er about half vv-ay (at least 5 cm above bottom of glass) with 1 g/L dye solution {e.g., reactivfi blue). Adjusi the clamp with the swatch until the surface of the dye solution i:; even with tie line at the bottom of the fabric. Start the timer as soon as the swatch is in place. Mee.sure ]he height that the dye solution has wicked up from the surface of the dye solution af1(5r 30 min. Renove the swatch and allow it to air dry on a flat surface. EXAMPLEES Example 1 Scouring cnttnn fp.b'c. iv^ii .^-id nqdinase A A 100% 460U cotlon fabric was purchased from Test Fabrics. Fabric swatches were cut to about 2 g each. Two buffets w.j-e rrade for his sludy. Buffer pH 3 was made by dissolving 1.954 g Citric acid Tionohydra;e anci (3,206 g sodium citrate dehydrate in 1 liter de-ionized. Buffer pH 4 was made by dissolvincj 1.376 g citric acid monohydrate and 1.015 g sodium citrate dehydrate in 1 liter de-ionized. The scouring was conducted with a Lab-0-Mat. The beaker was filled with 40 ml bjffe- and two iDieces of pre-cut fabric. 1. Pre-rinse: The vi/etting agent, L.eophan, was added to the buffer to a concentration of 0.25 g/L. Then the tenperature wae increased to 40°C for pre-rinse. After 10 min, the liquid was drained. 2. Bio-scciuring: ""ne tec.kf wth pre-rinsed fabrics was filled with 40 ml buffer. Acid pectinase was added re 9iacl-' weaker as specified. In the meanwhile, the second wetting agent, Keirlon Jet E;, was dcst; 1 to a concentration of 1 g/L. Temperature was raised to 55°C and kept for 30 min. 3. Inactivation; /Vier the required time reached, add the Deko! NS in the machine/beaker thf-'i 'aised the; tenperature to 95°C and run for 15 min, decreased the temperature tc 70-C;' •:-a\neti. 5. Cold rinse: F-i^^u in LXMU v^ater and rinsed for 10 min 6. Spinned off the water on the fabrics and air dry. 7. Measured resdua! peotin and wetting time in the treated fabrics. The reisult ot the test is shov\n in Table 1. Example 2 Scouring nQttaQ-[aitLii:i:tM.tL!^.ai.dJ?ja:tij:Ba£LB The same fabric; swatch and buffers were prepared as in Example 1. Acid Pectinase B had different enzyie ccrrioositicn compared to Acid Pectinase A. The performance of pectin removal was s\'o\! E nzyme Dose Pectin removal (%) (average) 0 24.7 9 UPTE/g fabric 46.8 90 UPTE/g fabric 61.8 13 PGU/g fabric 60.4 130 PGU/g fabric 95.6 0 24.0 5B 130 PGU/g fabric 91.2 Table 1 Enzyme type PH Ho en;!yrne Acid Pectinase A Ai;id Pecrinase A Acid Pectinase B Acid Pectifiase B No en;!:yrne Acid Alpha-Amylase B (ml/Kc) 7PH"4"' Pedinex "leici l\/la::ilr, pl-i 4 Pectinex U:tra, ol:-l 4 24.7% 24.7% 24.7% 0.5 46.8% 47.2% 60.4% 5.00 61.8% 79.8' 95.6% Pectinex )!:XL pH 4 24.7% 30.4% Pectinex Smasi'i KXL, p^ 4 24.7% 32.9% 88.9% Fec:inex E?: -w 24.0% 91.2% Example 3 iitia:li:i].^ii[riLiJllaaa!;LL:i>....d(i£'Jziiaa_c A The Vilisco fatric (100% coton) was from Vlisco and cut to 5 cm * 15 cm. Buffer pH 3 and pH 4 vjere prepared follov/ec the procedures described in Example 1. 100 ml buffer was added 1:o a beaks^r, Keirlon >.let B was added to a concentration of 2 g/L. Enzymes (the doses were listed in TEible 2) were Edded to the impregnation solution and mixed well. Fixed 2 swatches of the sarie fsbric in z. pair of forceps. Dip the swatches in the impregnation bath for 3D seconds and pao: it with the padder (Mathis Inc, U.S.A.). Repeated dipping and squeezing for one more ;ime to ersure a 100%> wet pick-up. Placed the swatches in two layers of plastic bag, pressed out the air and place the bac at room temperature. After 24 hours, removed tho sarnphs from the plastic bag. Fixed the samples in the forceps and dipped them in a water bathi at 90"C for 30 seconds and squeeze with padder. Repeated the dipping and squeezing twice. Rinsed the fabric in cold tap water for at least 60 seconds and squeeze off the wate' by fia' d. Then airs dry the fabric and measure TEGEWA, residual pectin, wetting time ario ^Micking test. The result of the test was shown in Table 2. Example 4 '-SlrDii]:ta£Lej:iLiSL.£[£.s.i::Jng-aiKihin,scniirino with Acid AmylasR A and Acid P£clJma£ A The same fabric and same buffer system were used as Example 3. Added 100 ml impregnation solution to (^ach beaker and placed them in the Lab-o-Mat, heated the solutions to 60°C. Took oLit {he btaker and added enzymes according to Table 2 to the impregnation solution and mixed v/ell. Fixed 2 swatches of the same fabric in a pair of forceps. Dipped the swatchies in the impregnation bath for 30 seconds and padded it with the padder. Repeated dipping and squeezing for one more time to ensure a 100% wet pick¬up. Placed the swatches n two layers of plastic bag, pressed out the air and placed the bag at the water bath Dre-='3* lo eCi'C. After 2 hours, removed the samples from the plastic bag. Fixed the samples m tt fcrciips and dipped them in a water bath at 90^^C for 30 seconds and squeezed witn paccBr. Repeated the dipping and squeezing twice. Rinsed the fabric in cold tap water for at lEiasi (;iO secords arid squeezed off the water by hand. Then air dried the fabric and measu'Eid TE;G[;;V\fA, residual pectin, wetting time and wicking test. The result of the test was sho'wr in Table 2. Table 2 -- \l- - — =..--;--w^::^ 2-^s.~-: -=-—■- /:^—2 '" A (TEGEWA) removal time (s) g(cm) Raw fabric C C) 1 0 >60s NA Cold Pad-Batch 50 SoOOO 7 72.6% 5 9 (pH 3); 25'C /5>FAL)/L UPTE/L Cold Pad-Batch 7 68.2% 6 9 (pH 4 ); 25°C Pad-Batch (pH 3), 9 73.3% 6 9 60°C Pad-Batch (pH 4), 6.5 69.9% 4 9 60°C Example 5 a-tr.h f;imiill.qnRr)ii::; dH^;i7ing and hinscnurinq with Acid Amylase A and Acid The proceduios ^Ne^e the same as described In Example 3 except that Acid Pectinase 3 was usea. "^he result c1 the test is shown in Table 3. Example 6 Pad-hatch sirnultaneoiic; rlpsiyinq pnrt hlnRrnuring with Acid Amylase A and Acid Pectinase a The procedures were the same as described in Example 4 except Acid Pectinase B was used. The result ot the test is sho^ft/n in Table 3. Table 3 /'.nT/hise A 50 Af-AJ/L Pectinase B Desizing (TEGEWA) Pectin removal Wetting time (s) Wicking (cm) Cold Pad-Batch (pH 3), 25°C r)2000 PQU/L 7 76.5% 5 10 Cold Pad-Batch (pH 4>. 25^0 8 75.4% 2 10 60°C " _ — ~ - Pad-Batch (pH 4), 60°C 6.5 72.6% 4 9.5 Example 7 Cold Pad-h.qtf:h .qirriuHrineoii--. dpisijing and hio.snnuring with Acid Amylase B ard Acid The procedures vjere the sane as described in Example 3 except that Acid Amylase A was replactsd by Acid Amylase B. The result of the test is shown in Table 4. Example 8 Pad-hatch sirnultan-::kiS-il££ji:ina and hinRGQiirinp with Acid Amylase B and Acid Pectimsa A The procedures v>/ere the sane as described in Example 4 except that Acid Amylase A was replaced by Acid Amylase B. The result of the test was shown in Table 4. Table 4 Amylase B Pectinase A Desizing Pectin Wetting ■\A'icking (TEGEWA) removal time (s) (cm) Cold Pad-Batch ipH SO F/!,U/L •;6000 9 69.9% 6 9.5 3), 25°C UPTE/L Cold Pad-Batch ipH 9 58.1% 5 8.5 4), 25^0 ■'■=-"r=:~ Z~ - - - -- - - _ - - 60°C Pad-Batch (pH 4), 9 62.1% 5 10 60°C Example 9 l-h,qtch ?;irni]l1anfiOii:; df^.c;i7ing ^nn hinsnnuring with Acid Amylase B and Acid The procedures were the sane as described in Example 3 except that Acid Amylase A was replace(j isy y\cid Amylase B and Acid Pectinase A was replaced by Acid Pectinase B. The result of tfie test jj shovvr in Taole 5. Example 10 Pad-hatch .simultaneoiis desiring and bios E The procedures were the sane as described in Example 4 except that Acid Amylase A was replaced by Acic AiTiyiase B and Acid Pectinase A was replaced by Acid Pectinase B. The result of the test is shown in Taole 5. / { Table 5 ^rri\icist; :.D FfiXj/l Cold Pad-EJatcfi ipH 3), 25^0 Cold Pad-tiatch (pH 4). 25=0 ' b F'ectinase B Desizing (TEGEWA) Pectin removal Wetting time [s) Wicking icm) ^^2000 F'GU/L 8 74.5% 13 9,5 8.5 65.7% 2 10 7.25 69.4% Example 11 A 100% cc'tton fabric (270 g/m") was from Boras Wafveri Kungsfors AB, Sweden. It was made in 2003 wiih CuDper 3/1 construction. The fabric contained 28 thread/cm warp yarn and 14 thread/cm weft yarn. The warp yarn has Ne 11 and the weft has Ne 8. Both yarns were open end. The: diy size^ pick up on the warp yarn was 8%. The size contained mainly Kollotex 5, Sovitose XO, and beef tallow wax with emulsifier. Kollotex 5 is a low viscous potalo starch esster. Soiviose XO is a high viscous starch ether with DS about 0.07. Fabric swatches were cut to about 25 g each. Buffer pH 3 was nacle by dissolving 11.53 g 85% phosphoric acid in 4.5 liter pure water, titrating v\/ith 5 M NaOH to p-i 2.95, then adding water to 5 liter. After adding 2 g/l nonionic surfactant t,a 'V9":tin3 ager;;) in the buffer, the buffer pH was measured as 3.05 at 25°C. The close of enzymes was added as listed in table 6. The desizing treatment was conducted in a Lab-o-mat (Werner Mathis). A 250 mL buffer solution was accied in each beaker. A given amount of alpha-amylase enzyme was added. One fabric swatch (25 g) was placed in each beaker. The beaker was closed and placed in the Lab-o-n',-t. Beakers were heated at 5°0/min to 50°C by an infrared heating system equipped v\/i1hin the Lab-o-miat. Beakers were rotated at 30 rpm, 50'C for 45 minutes. After the enizyme treatment, the fabric swatch was sequentially washed with water in the same beake'^ ttiree times at 95, 75, and 40-C, respectively. After dry overnight in air, the fabric swatch was stained with an iodine solution. The stained fabric sample was visually compared to TEGEWA standard photos with 1-9 scale where 1 is dark and 9 has no colcr stain. Thus higher number indicates a better starch removal. The visusi! evaiua >r] WES done by at least three professionals and an average TEGEW/i value was civen Ci each faoric sample. The results are shown in Table 6. The residue of rnelal ons on fabric was also evaluated. The fabric was first cut through 1 mm sievfr with a Thomas-Wiley mill. Fabric mash 4.00 (+/-0.01) g was mixed with 80 mL 1 g/L EDTA solution. The rrix';ure was incubated at 70-C and 200 rpm in a shaker (new Bru iswick Sciei'tfi: Co, Inc, Series 25) for 15 hours. After cooled down for about 30 minutes, the mi^^ture was csnlrifuged at 2500 rpm at 20'C for 10 minutes. The supernatant spectrophone-;er. Table 6 Enzyme Type ; [E'^zyme] (AFAU/kg fabric) TEGEWA Value (average) Metal content (mg/L) Mn Fe No enzyme C) Acid Alpha- 27.5 Amylase A 2.75 ■100 1.3 2.3 3.8 5.2 0.23 n/a 0.20 n/a 3.91 n/a 2.72 n/a n/a =: not measLired. CLAIMS 1. A process for oornb ric;d denizing and scouring of a sized fabric containing starch or starch derivatives ciwrg inaiufacture of a fabric, which process comprises incubating said sized fabric in an aciuei .,!!■; Irsatirig 5;olution having a pH in the range between 1 and 7 which aqueous treating soljtion ccmpnses an acid amylase and at least one acid scouring enzyme. ^. I lie orocess CT Siaini 1, vvneiein said aqueous treating solution has a pH in the range between 1 and 5, prefarablv bi;:'tween 1 and 4. 3. The process cf claiTi 1 or 2, wherein said scouhng enzyme is acid cellulase, acid pectinase. acid lipase, acid xylanasei and/or acid protease or a mixture thereof. 4. The process of any of claims 1-3, wherein the acid amylase is of bacterial or fungal origin, such as filan'ento i 5 lungua origin. 5. The process of a'/ of ciaimj 1-4, wherein the acid amylase is derived from a strain of Aspergllus, prelei abiy Aspergillus niger, Aspergillus awamori, Aspergillus oryzae or Aspergillus kawachii, Dr a siticin of Rhizomucor, preferably Rhizomucor pusillus, or a strain of Meripilus, preferably a strai i of Meripilus giganteus. 6. The process of any ol claims 1-5, wherein the Aspergillus acid amylase is the acid Aspergillus n/geralpha amyla.re disclcsed in SEQ ID NO: 38. or a variant thereof. 7. The process oi any of claims 1-6, wherein the Rhizomucor acid amylase is the Rhizomucor pusillus a pha-arrylase disclosed in SEQ ID NO: 48, or a variant thereof. 8. The process of any of claims 1-7, wherein the acid amylase, preferably an acid fungal alpna-amylase is present in a concentration of 1-3,000 AFAU/kg fabric, preferably 10-1,000 AFAU/ kg fabiic, especially 100-500 AFAU/kg fabric or 1-3,000 AFAU/L treating solution, preferably 1(1-1,000 AFAU'L treating solution, especially 100-500 AFAU/L treating solution. 9. The process o" any o1 :;laimj; 1-8, wherein the bacterial acid amylase is derived from a strain of the genis Baalkjs. p'elerably derived from a strain of Bacillus sp., more preferably a slrciin o" Bacillus licheniformis, Bacillus amylollquefaciens, Bacillus stearotfiermophiius, Bacillus subtilis, or Bacillus sp., such as Bacillus sp. NCIB 12289, NCIB 12512, NCIB 12513 IDSM 9375. DSMZ 12648, DSMZ 12649, KSM API378, KSM K36 or KSM K38. amylase shown in SEiO ID \ 11. The process cr claim 3, whei'ein said acid pectinase i£ an acid pectate lyase, an acid pectin lyase, an acid pcilygalacturonase, and/or an acid polygatacturonate lyase. 12. The process of any of claims 1-11, wherein said acid pectinase is Pectinex® BE XXL, Pectinex® BE Cclour Pectinex© Ultra; Pectinex™ Ultra SP-L, Pectinex® Yield Mash, Pectinex® XXL, Pectiiex® Smash KXL, Pectinex® Smash, Pectinex™ AR or any mixtures thereof. 13. The process o an/ of claims 1-12, wherein said acid pectinase is derived 'rom the genus Aspergillus or Bacillus. 14. The process of any of claims 1-13, wherein said acid pectinase is added to the solution before, siTxitaneous. or aftar addition of acid amylase. 15. The process of any of claims 1-14, wherein the process is carried out at a temperature in the ranee from 5-90-, in particular 20 to 90°C. 16. The process of claim i5, wherein the process is carried out at a temperature between 25 and 60C for a suitable period of time, preferably between 2 and 24 hours. 17. The process ot any off claims 1-16. wherein the pH is in the range between pH 2 to 4. 18. The process o' any o: clainrus "-17, wherein the fabric is made of fibres of natural or man-made origin. 19. The procesi^ of any of claims 1-18, wherein the -'abric is cotton fabric, denin", linen, ramie, viscose, lyocell or cciliuiose acetate. 20. The process; cf any oi claims 1-19, wherein the fabric is made of fibres of animal origin, in particulars slop . man-made oi natural oiigin ':;.icfi as poly(ethyle^e terephthalate) or poly(lactic acid). 22. The process of any of clairrs 1-21, wherein the fabric is made of nylon, acrylic, or polyurethane fibres. 23. The process o' any o1 claims; 1-22, wherein the fabric is a polyester containing fabric or garment consists ol essent ally 100% polyester. 24. The method oi anv of claims; 1-23, wherein the polyester fabric is a polyester blend, such as a polyester aid (;:eIlulosic tilend, including polyester and cotton blends; a polyester and wool blend; a poly9ster and stIk blend; a polyester and acrylic blend; a polyester and nylon blend; a polyester, nylDn and polyurethane blend; a polyester and polyurethane blend, rayon (viscose), cellulose acetate and tencel. 25. A coiTiposition coiTiprising ar acid amylase and an acid scouring enzyme. 26. The composition of claim 25, wherein the bacterial acid amylase is derived from a strain of the genus Bctullus, preferably derived from a strain of Bacillus sp., more preferably a strain of Bacillus Inheriiformis Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus sp., sucfi as Bacillus sp. NCIB 12289, NCIB 12512, NCIB 12513, DSM 9375, DSMZ 12648, DS.MZ 12649, KSM API 378, KSM K36 or KSM K38. 27. The composition oi claim 25 or 26, wherein said acid amylase is derived from Aspergillus nigercn Rnizomucorpusillus or mixtures thereof. 28. The composit (DH C'f clain- 25 or 26, vviierein said acid scouring enzyme is selected from the ciroupi consisiing of c:;ic cellulase, acid pectinase. acid lipase, acid xylanase and/or acid protease, and mixlu'fjs thereof. 29. The comoositiori of any of claims 25-28, wherein said acid pectinase is derived from a strain of Aspergillus- c r Ba cii us. BE XXL, Pectinex® Hz: Co'cur, Feclinex® Ultra; Pectinex Ultra SP-L, Pectinex® Yield l\4ash, Pectine.x® KXL, Pec'inex® Snash XXL, Pectinex® Smash and/or Pectinex™ AR. 31. The composition of any of claiins 25-30, wherein said composition further comprises stabilizer, surfactant, wetting ^gent, dispersing agents, sequestering agents and emulsifying agents, or a mixture thereol. 32. The use of a comfx::sition of any of claims 25-31 for simultaneous desizing and scouring. |
|---|
| Patent Number | 279001 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Indian Patent Application Number | 6810/CHENP/2008 | ||||||||||||
| PG Journal Number | 02/2017 | ||||||||||||
| Publication Date | 13-Jan-2017 | ||||||||||||
| Grant Date | 06-Jan-2017 | ||||||||||||
| Date of Filing | 11-Dec-2008 | ||||||||||||
| Name of Patentee | NOVOZYMES NORTH AMERICA, INC. | ||||||||||||
| Applicant Address | 77 PERRY CHAPEL CHURCH ROAD, FRANKLINTON, NORTH CAROLINA 27525 | ||||||||||||
Inventors:
|
|||||||||||||
| PCT International Classification Number | C12N9/28 | ||||||||||||
| PCT International Application Number | PCT/US07/70485 | ||||||||||||
| PCT International Filing date | 2007-06-06 | ||||||||||||
PCT Conventions:
|
|||||||||||||