Title of Invention	A PROCESS FOR DESIZING A FABRIC
Abstract	A process for desizing of a sized fabric containing starch or starch derivatives during manufacture of a fabric, which process comprises incubating said sized fabric in an aqueous treating solution having a pH in the range between 1 and 5 which aqueous treating solution comprises an alpha-amylase.

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DESIZING PROCESS REFERENCE TO A SEQUENCE LISTING This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference. FIELD OF THE INVENTION The present invention relates to a process of desizing sized fabrics during manufacture of especially new fabrics. BACKGROUND OF THE INVENTION The processing of a fabric, such as of a cellulosic material, into 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. The preparation process, which may involve desizing (for woven goods), scouring, and bleaching, produces a fabric suitable for dyeing or finishing. 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 the subsequent processes 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 Mn2+, Fe2+/Fe3+1 Cu2+etc, which - if present on the fabric - may result in an uneven bleaching in a later process step or might even make pin-holes in the bleached fabric. Demineralization is typically accomplished by acid precipitation and typically involves addition of acids such as acetic acid or sulphuric acid. It is desirable to provide improved processes for desizing of sized fabrics during manufacture of especially new fabrics. BRIEF DISCLOSURE OF THE INVENTION The present invention is directed towards providing a process of desizing a sized fabric during manufacture of especially new fabrics. In the first aspect the invention relates to a process for desizing a sized fabric containing starch or starch derivatives during manufacture of a fabric, which process comprises incubating said sized fabric in an aqueous treating solution having a pH in the range between 1 and 5 which aqueous treating solution comprises an alpha-amylase. The present inventors have found that when carrying out a desizing process of the invention, as defined in the claims, no demineralization is needed. The demineralization takes place simultaneously and/or after the desizing of the sized fabric in the same treating solution. Compared to traditional processes involving an alkaline desizing step and a demineralization step a pH adjusting step is avoided. Another advantage of the invention is that process time is saved/reduced as desizing and demineralization may be carried out simultaneously. Even if the desizing and demineralization are not carried out as a one step process, i.e., simultaneously, costs of, e.g., acids and manpower for adding acid(s) are saved/reduced as the pH adjustment step between the traditional alkaline desizing step and the demineralization step is avoided. In context of the invention the term "fabric" is used interchangeable with the term "textile" and means, 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 is constructed by weaving "filling" or weft yarns between warp yarns stretched in the longitudinal direction on the loom. The wrap yarns must be sized before weaving in order to lubricate and protect them from abrasion at the high speed insertion of the filling yarns during weaving. The filling yarn can be woven through the warp yarns in a "over one - under the next" fashion (plain weave) or by "over one - under two" (twill) or any other myriad of permutations. Strength, texture and pattern are related not only to the type/quality of the yarn but also the type of weave. Generally, dresses, shirts, pants, sheeting's, towels, draperies, etc. are produced from woven fabric. Knitting is forming a fabric by joining together interlocking loops of yarn. As opposed to weaving, which is constructed from two types of yarn and has many "ends", knitted fabric is produced from a single continuous strand of yarn. As with weaving, there are many different ways to loop yarn 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 fabrics are sheets of fabric made by bonding and/or interlocking fibers and filaments by mechanical, thermal, chemical or solvent mediated processes. The resultant fabric can be in the form of web-like structures, laminates or films. Typical examples are disposable baby diapers, towels, wipes, surgical gowns, fibers for the "environmental friendly" fashion, filter media, bedding, roofing materials, backing for two-dimensional fabrics and many others. According to the invention, the process may be applied to any sized fabric known in the art (woven, knitted, or non-woven). The process is applied to newly manufactured sized fabric, as opposed to used and/or soiled fabric to be cleaned during laundry washing. In an embodiment the fabric is made of fibres of natural and/or man-made origin. In another embodiment the fabric is made of fibres from animal origin. In particular, the process of the invention may be applied to cellulose-containing or cellulosic fabrics, such as cotton, viscose, rayon, ramie, linen, cellulose acetate, denim, lyocell (Tencel™, e.g., produced by Courtaulds Fibers), or mixtures thereof, or mixtures of any of these fibers together with synthetic fibres (e.g., polyester, polyamid, acrylic, or polyurethane, nylon, poly(ethylene terephthalate) or poly(lactic acid) or other natural fibers, such as wool and silk., such as viscose/cotton blends, lyocell/cotton blends, viscose/wool blends, lyocell/wool blends, cotton/wool blends; flax (linen), ramie and other fabrics based on cellulose fibers, including all blends of cellulosic fibers with other fibers such as wool, polyamide, acrylic and polyester fibers, e.g., viscose/cotton/polyester 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, polyamid, nylon, respectively. The term "wool," means any commercially useful animal hair product, for example, wool from sheep, camel, rabbit, goat, lama, and known as merino wool, Shetland wool, cashmere wool, alpaca wool, mohair, etc. and includes wool fiber and animal hair. The process of the invention can be used with wool or animal hair material in the form of top, fiber, yarn, or woven or knitted fabric. The alpha-amylase used in accordance with the process of the invention may be any alpha-amylase, but is preferably of either bacterial or fungal origin. Preferably the alpha-amylase is an acid alpha-amylase, such as an acid alpha-amylase derived from a filamentous fungus, especially a strain of the genera Aspergillus, Rh/zomucor or Meripillus. The term "acid alpha-amylase" means an alpha-amylase (E.C. 3.2.1.1) which has an optimum activity at a pH in the range of 1 to 7, preferably from 1 to 5 at a temperature of 50°C. The term "desizing" is intended to be understood in a conventional manner, i.e., the degradation and/or removal 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 particular woven fabric prepared from a cellulose-containing material, containing starch or starch derivatives. The fabric is normally undyed and made of cotton, viscose, flax, and the like. The main part of the starch or starch derivatives present on the fabric is normally size with which the yarns, normally warp yarns, have been coated prior to weaving. The term "carbohydrate-binding module (CBM)", or as often referred to a "carbohydrate-binding domain (CBD)", is a polypeptide amino acid sequence which binds preferentially to a poly- or oligosaccharide (carbohydrate), frequently - but not necessarily exclusively - to 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 enzyme(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 effect, i.e., desizing of the fabric, as compared to a fabric which has not been treated with said enzyme(s). BRIEF DESCRIPTION OF THE DRAWING Fig. 1 shows the desizing performance of Alpha-Amylase D on Viisco fabric at pH 4.0. Fig. 2 shows the desizing performance of Alpha-Amylase C on Viisco fabric at pH 4.0. DETAILED DISCLOSURE OF THE INVENTION The present invention is directed towards providing a process of desizing a sized fabric during manufacture of especially new fabrics. The desizing step of the invention is in a preferred embodiment followed by a scouring step, preferable an enzymatic scouring step, preferably with a scouring enzyme such as a pectinase, e.g., a pectate lyase, a lipase, a protease, or combination thereof, and a bleaching step, preferably involving bleaching with hydrogen peroxide and/or a hydrogen peroxide generating agent. Relevant scouring processes are described in US patent no. 5,578,489, US patent no. 5,912,407, and US patent no. 6,630,342. Relevant bleach processes are described in US patent no. 5,851,233, US patent no. 5,752,980, and US patent no. 5,928,380. Relevant combined scouring and bleach processes are described in WO 2003/002810 (Novozymes) and WO 2003/002705 (Novozymes), respectively. According to the present invention, fabric may be desized and demineralised simultaneously in the same aqueous treating solution or subsequently in the same or two separate treating solutions. In a preferred embodiment the desizing and demineralization are carried out simultaneously in the same treating solution. The process of the invention may be carried out using traditional sizing/desizing equipment, e.g., pad systems, J-boxes, jets, jiggers, etc. In general, no additional process equipment is needed. According to the invention simultaneous desizing and demineralisation are carried out by incubating sized fabric in an aqueous treating solution having a pH in the range between 1 and 5 which aqueous treating solution comprises an alpha-amylase. In a preferred embodiment the pH during incubation is in the range between 1 and 4, especially between pH 2 and 4. Woven goods are the prevalent form of fabric construction. The weaving process demands a "sizing" of the warp yarn to protect it from abrasion. Starches, unmodified and modified, polyvinyl alcohol (PVA), carboxy methyl cellulose (CMC), waxes and acrylic binders, and mixtures thereof, are examples of typically used sizing agents. The sizing agent may according to the invention be a starch-based or starch derivative-based sizing agent, but may also contain one or more non-starch or starch derivative-based sizing agents. The sizing agent(s) are in general removed after the weaving process as the first step in preparing the woven goods. One or more other agents including stabilizers, surfactants, wetting agents, dispersing agent, sequestering agents and emulsifying agents, or mixtures thereof, may be present during a desizing process of the invention. The sized fabric is allowed to incubate in the aqueous treating solution for a sufficiently long period of time to accomplish desizing of the sized fabric. The optimal period is dependent upon the type of processing regime and the temperature and can vary from about 15 minutes to several days, e.g., 48 hours. A process of the invention is preferably carried out at a temperature in the range from 5 to 90°C, in particular 20 to 90°C dependent on the processing regime. The processing regime can be either batch or continuous with the fabric being contacted by the aqueous treating stream in open width or rope form. Continuous operations may use a saturator whereby an approximate equal weight of treating solution per weight of fabric is applied to the fabric, followed by a heated dwell chamber where the chemical reaction takes place. A washing section then prepares the fabric for the next processing step. In order to ensure a high whiteness or a good wettability and resulting dyeability, the desizing enzyme(s) and other agents must be thoroughly removed. Batch processes 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 incubation period, the aqueous treating solution is drained, the fabric is rinsed, and the next processing step is initiated. Discontinuous PB-processes (i.e., pad-batch processes) involves a saturator whereby an approximate equal weight of aqueous treating solution per weight of fabric is applied to the fabric, followed by a dwell period, which in the case of CPB-process (i.e., cold pad-batch process) might be one or more days. For instance, a CPB-process may be carried out at between 20-40°C for 8-24 hours or more at a pH in the range between 1 and 5, preferably at a pH in the range between around 1 and 4, especially between pH 2 and 4. Further, a PB-process may be carried out at between 40-90°C for 1-6 hours at a pH in the range between around 1 and 5, preferably between around pH 1 and 4, especially between pH 2 and 4. In one embodiment the desizing process of the invention may be carried out using an effective amount of alpha-amylase, preferably acid alpha-amylase, and an acid such as acetic acid or sulphuric acid or the like. Detergents In the context of this invention, a detergent is synonymous with a surfactant, and it may in particular be a non-ionic surfactant, an anionic surfactant, a cationic surfactant, an ampholytic surfactant, a zwitterionic surfactant, and a semi-polar surfactant, or a mixture hereof. The surfactant is typically present in a composition of the invention at a level from 0.1% to 60% by weight. The surfactant is preferably formulated to be compatible with enzyme components present. In liquid or gel compositions the surfactant is most preferably formulated in such a way that it promotes, or at least does not degrade, the stability of any enzyme in these compositions. Preferred systems to be used according to the present invention comprise as a surfactant one or more of the non-ionic and/or anionic surfactants described herein. Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are suitable for use as the non-ionic surfactant of the surfactant systems of 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 8 to about 14 carbon atoms, in either a straight chain or branched-chain configuration 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 non-ionic surfactants of this type include Igepal™ CO-630, marketed by the GAF Corporation; and TRITON™ X-45, X-114, X-100 and X-102, all marketed by the Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (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 non-ionic surfactant system. 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 products. Examples of commercially available non-ionic surfactants of this type include TERGITOL™ 15-S-9 (The condensation product of CirC15 linear alcohol with 9 moles ethylene oxide), TERGITOL™ 24-L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles ethylene oxide with a narrow molecular weight distribution), both marketed by Union Carbide Corporation; NEODOL™ 45-9 (the condensation product of C14-C15 linear alcohol with 9 moles of ethylene oxide), NEODOL™ 23-3 (the condensation product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide), NEODOL™ 45-7 (the condensation product of C14-C15 linear alcohol with 7 moles of ethylene oxide), NEODOL™ 45-5 (the condensation product of C14-C15 linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company, KYRO™ EOB (the condensation product of C13-C15 alcohol with 9 moles ethylene oxide), marketed by The Procter & Gamble Company, and Genapol LA 050 (the condensation product of C12-C14 alcohol with 5 moles of ethylene oxide) marketed by Hoechst. Preferred range of HLB in these products is from 8-11 and most preferred from 8-10. Also useful as the nonionic surfactant of the surfactant system 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- positions on the preceding saccharide units. The preferred alkylpolyglycosides have the formula R20(CnH2nO)t(glycosyl)x wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, 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, preferably 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 non-ionic surfactant system. 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% of 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 non-ionic surfactant of the non-ionic surfactant system are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and 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 2,500 to about 3,000. This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000. Examples of this type of non-ionic surfactant include certain of the commercially available TETRONIC™ compounds, marketed by BASF. Preferred for use as the non-ionic surfactant of the surfactant system are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethyfeneoxide, alkylpolysaccharides, and mixtures hereof. Most preferred are C8-C14 alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and C8-C18 alcohol ethoxylates (preferably C10 avg.) having from 2 to 10 ethoxy groups, and mixtures thereof. Highly preferred non-ionic surfactants are poly hydroxy fatty acid amide surfactants of the formula R2 - C - N - Z, II II, O R1 wherein R1 is H, or R1 is C-M hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl or a mixture thereof, R2 is CM1 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl, R2 is straight C^-is alkyl or C16_18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from 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 RO(A)mS03M wherein R is an unsubstituted C10-C-24 alkyl or hydroxyalkyl group having a C10-C24 alkyl component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-C18 alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6, 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 sub-stituted-ammonium cation. Alkyl ethoxylated 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 C12-C18 alkyl polyethoxylate (1.0) sulfate (C12-C18E(1.0)M), C12-C18 alkyl polyethoxylate (2.25) sulfate (C12-C18(2.25)M, and CirC18 alkyl polyethoxylate (3.0) sulfate (C12-C18E(3.0)M), and C12-C18 alkyl polyethoxylate (4.0) sulfate (C12-C18E(4.0)M), wherein M is conveniently selected from sodium and potassium. Suitable anionic surfactants to be used are alkyl ester sulfonate surfactants including linear esters of C8-C20 carboxylic acids (i.e., fatty acids) which are sulfonated with gaseous S03 according to "The Journal of the American Oil Chemists Society", 52 (1975), pp. 323-329. Suitable starting materials would include natural fatty substances as derived from tallow, palm oil, etc. The preferred alkyl ester sulfonate surfactant comprise alkyl ester sulfonate surfactants of the structural formula: O II R3 - CH - C - OR4 S03M wherein R3 is a C8-C20 hydrocarbyl, preferably an alkyl, or combination thereof, R4 is a CrC6 hydrocarbyl, preferably an alkyl, or combination thereof, and M is a cation which forms a water soluble salt with the alkyl 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 C10-C16 alkyl, and R4 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonates wherein R3 is C10-C16 alkyl. Other suitable anionic surfactants include the alkyl sulfate surfactants which are water soluble salts or acids of the formula ROS03M wherein R preferably is a C10-C24 hydrocarbyl, preferably an alkyl or hydroxyalkyl having a C10-C2o alkyl component, more preferably a C12-C18 alkyl or hydroxyalkyl, and 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 cations derived from alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like). Typically, alkyl chains of C12-C16 are preferred for lower wash temperatures (e.g. below about 50°C) and C16-C18 alkyl chains are preferred for higher wash temperatures (e.g. above about 50°C). Other anionic surfactants useful for detersive purposes include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono- di- and triethanolamine salts) of soap, C8-C22 primary or secondary alkanesulfonates, C8-C24 olefinsulfonates, 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, Cs_C24 alkylpo- lyglycolethersulfates (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 C12-C18 monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated C6-C12 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(CH2CH2O)k-CH2C00-M+ wherein R is a Cs-C^ 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. Alkylbenzene sulfonates are highly preferred. Especially preferred are linear (straight-chain) alkyl benzene sulfonates (LAS) wherein the alkyl group preferably contains from 10 to 18 carbon atoms. Further examples are described in "Surface Active Agents and Detergents" (Vol. I and II by Schwartz, Perrry and Berch). A variety of such surfactants are also generally disclosed in US 3,929,678, (Column 23, line 58 through Column 29, line 23, herein incorporated by reference). When included therein the compositions of the present invention typically comprise from about 1% to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants. The compositions of the present invention may also contain cationic, ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein. Cationic detersive surfactants suitable for use in the 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: [R2(OR3)y][R4(OR3)y]2R5N+X-wherein R2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R3 is selected form the group consisting of -CH2CH2-, -CH2CH(CH3)-, -CH2CH(CH2OH)-, -CH2CH2CH2-, and mixtures thereof; each R4 is selected from the group consisting of C-rC4 alkyl, C1-C4 hydroxyalkyl, benzyl ring structures formed by joining the two R4 groups, -CH2CHOHCHOHCOR6CHOHCH. 2OH, wherein R6 is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when y is not 0; R5 is the same as R4 or is an alkyl chain,wherein the total number of carbon atoms or R2 plus R5 is not more than about 18; each y is from 0 to about 10,and the sum of the y values is from 0 to about 15; and X is any compatible anion. Highly preferred cationic surfactants are the water soluble quaternary ammonium compounds useful in the present composition having the formula: R1R2R3R4N+X- (i) wherein Rn is C8~Ci6 alkyl, each of R2, R3 and R4 is independently C-pC4 alkyl, C-pC4 hydroxy alkyl, benzyl, and -(C2H40)XH where x has a value from 2 to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl. The preferred alkyl chain length for R, is C12-C15, 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 OXO alcohols synthesis. Preferred groups for R2R3 and R4 are methyl and hydroxyethyl 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 trimethyl ammonium chloride or bromide; coconut methyl dihydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; C12-15 dimethyl hydroxyethyl ammonium chloride or bromide; coconut dimethyl hydroxyethyl ammonium chloride or bromide; myristyl trimethyl ammonium methyl sulphate; lauryl dimethyl benzyl ammonium chloride or bromide; lauryl dimethyl (ethenoxy)4 ammonium chloride or bromide; choline esters (compounds of formula (i) wherein R^ is CH2-CH2-0-C-C12-14 alkyl and R2R3R4 are methyl). O di-alkyl imidazolines [compounds of formula (i)]. Other cationic surfactants useful herein are also described in US 4,228,044 and in EP 000 224. When included therein, the 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. Ampholytic surfactants are also suitable for use in the compositions of the present invention. These surfactants can 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., carboxy, sulfonate, sulfate. See US 3,929,678 (column 19, lines 18-35) for examples of ampholytic surfactants. When included therein, the 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 the composition of the invention. 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 phosphonium 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 compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such zwitterionic surfactants. Semi-polar nonionic 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 hydroxy a Iky I 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 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 nonionic detergent surfactants include the amine oxide surfactants having the formula: wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereof containing from about 8 to about 22 carbon atoms; R4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is from 0 to about 3: and each R5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure. These amine oxide surfactants in particular include C10-C18 alkyl dimethyl amine oxides and C8-C12 alkoxy ethyl dihydroxy ethyl amine oxides. When included therein, the composition of the present invention typically comprises from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such semi-polar nonionic surfactants. Enzymes Alpha-Amylases The alpha-amylase(s) used in the process of the invention may be any alpha-amylase, preferably of bacterial or fungal origin. In a preferred embodiment the alpha-amylase is an acid alpha-amylase, such as an alpha-amylase or hybrid alpha-amylase disclosed in WO 2005/003311 which is hereby incorporated by reference. In a preferred embodiment the alpha-amylase include a carbohydrate-binding module (CBM) as defined in WO 2005/003311, preferably a family 20 CBM as defined in WO 2005/003311. Specifically contemplated are CBMs include the ones selected from the group consisting of Aspergillus kawachii disclosed in SEQ ID NO: 2; Bacillus flavothermus disclosed in SEQ ID NO: 5; Bacillus sp. disclosed in SEQ ID NO: 6; Alcaliphilic Bacillus disclosed in SEQ ID NO: 7; Hormoconis resinae disclosed in SEQ ID NO: 8; Lentinula edodes disclosed in SEQ ID NO: 9; Neurospora crassa disclosed in SEQ ID NO: 10; Talaromyces byssochlamydiodes disclosed in SEQ ID NO: 11; Geosmithia cylindrospora disclosed in SEQ ID NO: 12; Scorias spodiosa disclosed in SEQ ID NO: 13; Eupenicillium ludwigii disclosed in SEQ ID NO: 14; Aspergillus japonicus disclosed in SEQ ID NO: 15; Penicillium cf. miczynskii disclosed in SEQ ID NO: 16; Mz1 Penicillium sp. disclosed in SEQ ID NO: 17; Thysanospora sp. disclosed in SEQ ID NO: 18; Humicola grisea var. thermoidea disclosed in SEQ ID NO: 19; Aspergillus niger disclosed in SEQ ID NO: 20; or Althea rolfsii disclosed in SEQ ID NO: 21. Fungal Alpha-Amylases In an embodiment the fungal alpha-amylase is of yeast or filamentous fungus origin. In a preferred embodiment the fungal alpha-amylase is an acid alpha-amylase. Preferred alpha-amylases include, for example, alpha-amylases obtainable from Aspergillus species, in particular from Aspergillus niger, A. oryzae, and A. awamori, A. kawachii, such as the acid alpha-amylase disclosed as SWISSPROT P56271, or described in more detail in WO 89/01969 (Example 3). The mature acid alpha-amylase has the amino acid sequence shown as 22-511 of SEQ ID NO: 4, encoded by the DNA sequence shown in SEQ ID NO: 3, or the amino acid sequence shown in SEQ ID NO: 38. Also preferred are alpha-amylase sequences having more than 50%, such as more than 60%, more than 70%, more than 80% or more than 90%, more than 95%, more than 96%, more than 97%, more than 98%, or even more than 99% identity to the amino acid sequence shown in SEQ ID NOS: 4 or 38, respectively. In another preferred embodiment the alpha-amylase sequence is derived from an A. oryzae acid alpha-amylase. More preferably the alpha-amylase sequence has more than 50%, such as more than 60%, more than 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 embodiment the alpha-amylase is the Aspergillus kawachii alpha-amylase disclosed in SEQ ID NO: 37, which in wild-type form contains a carbohydrate-binding domain (CBD) also shown in SEQ ID NO: 2. In a preferred embodiment the alpha-amylase is an alpha-amylase having more than 50%, such as more than 60%, more than 70%, more than 80% or more than 90%, more than 95%, more than 96%, more than 97%, more than 98%, or even more than 99% identity to the amino acid sequence shown in SEQ ID NOS: 43, 44, 46 or 47, respectively. The alpha-amylase may be 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. Bacterial Alpha-Amylases In an embodiment the alpha-amylase is of bacterial origin. In a preferred embodiment the bacterial alpha-amylase is an acid alpha-amylase. The bacterial alpha-amylase is preferably derived from a strain of Bacillus, such as Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or other Bacillus sp., such as Bacillus sp. NCIB 12289, NCIB 12512 (WO 95/26397), NCIB 12513 (WO 95/26397), DSM 9375 (WO 95/26397) , DSMZ 12648 (WO 00/60060), DSMZ 12649 (WO 00/60060), KSM AP1378 (WO 97/00324), KSM K36 or KSM K38 (EP 1,022,334). Preferred are the Bacillus sp. alpha-amylases disclosed in WO 95/26397 as SEQ ID NOS. 1 and 2, respectively, the AA560 alpha-amylase disclosed as SEQ ID NO: 2 in WO 00/60060 (i.e., SEQ ID NO: 40 herein), and the #707 alpha-amylase disclosed by Tsukamoto et al., Biochemical and Biophysical Research Communications, 151 (1988), pp. 25-31. In an embodiment of the invention 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 the parent alpha-amylase has one or more deletions in positions or corresponding to the following positions: D183 and G184, preferably wherein said alpha-amylase variant 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/substitutions or corresponding to the following deletions/substitutions: Delta (R81 -G182); Delta (D183-G184); Delta (D183-G184)+N195F; R181Q+N445Q+K446N; Delta (D183-G184)+R181Q, Delta (D183-G184) and one or more of the following substitutions or corresponding to: R118K, N195F, R320K, R458K, especially wherein the variant has the following mutations: A(D183+G184)+R118K+N195F+R320K+R458K (using the SEQ ID NO: 40 numbering). In another preferred embodiment the alpha-amylase is the AA560 alpha-amylase shown in SEQ ID NO: 40 further comprising one or more of the following substitutions M9L, M202L, V214T, M323T, M382Y, E345R or the A560 alpha-amylase with all of the following substitutions: M9L, M202L, V214T, M323T, M382Y or M9L, M202L, V214T, M323T and E345R. Commercially available alpha-amylase products or products comprising alpha-amylases include product sold under the following tradenames: NATALASE™, STAINZYME™ (Novozymes A/S), Bioamylase - D(G), BIOAMYLASE™ L (Biocon India Ltd.), KEMZYM™ AT 9000(Biozym Ges. m.b.H, Austria), PURASTAR™ ST, PURASTAR™ HPAmL, PURAFECT™ OxAm, RAPIDASE™ TEX (Genencor Int. Inc. USA), KAM (KAO, Japan) The alpha-amylase may be present in a concentration of from about 0.05-150 KNU/L treating solution, preferably 1-100 KNU/L treating solution, especially 2-20 KNU/L treating solution or 0.05-150 KNU/Kg fabric, preferably, 1-100 KNU/kg fabric, especially 2-20 KNU/kg fabric Hybrid enzyme The alpha-amylase may in a preferred embodiment be an alpha-amylase comprising a carbohydrate-binding domain (CBD). 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. Hybrid enzymes or a genetically modified wild type enzymes as referred to herein include species comprising an amino acid sequence of an alpha-amylase enzyme (EC 3.2.1.1) linked (i.e. covalently bound) to an amino acid sequence comprising a carbohydrate-binding domain (CBD). 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 Greenwood et al. Biotechnology and Bioengineering 44 (1994) pp. 1295-1305]. They may, e.g., be prepared by transforming into a host cell a DNA construct comprising at least a fragment of DNA encoding the carbohydrate-binding domain ligated, with or without a linker, to a DNA sequence encoding the enzyme of interest, and growing the transformed host cell to express the fused gene. The resulting recombinant product (hybrid enzyme) - often referred to in the art as a "fusion protein - may be described by the following general formula: A-CBD-MR-X In the latter formula, A-CBD is the N-terminal or the C-terminal region of an amino acid sequence comprising at least the carbohydrate-binding domain (CBD) per se. MR is the middle region (the "linker"), and X is the sequence of amino acid residues of a polypeptide encoded by a DNA sequence encoding the enzyme (or other protein) to which the CBD is to be linked. The moiety A may either be absent (such that A-CBD is a CBD per se, i.e. comprises no amino acid residues other than those constituting the CBD) or may be a sequence of one or more amino acid residues (functioning as a terminal extension of the CBD per se). The linker (MR) may be a bond, or a short linking group comprising from about 2 to about 100 carbon atoms, in particular of from 2 to 40 carbon atoms. However, MR is preferably a sequence of from about 2 to about 100 amino acid residues, more preferably of from 2 to 40 amino acid residues, such as from 2 to 15 amino acid residues. The moiety X may constitute either the N-terminal or the C-terminal region of the overall hybrid enzyme. It will thus be apparent from the above that the CBD in a hybrid enzyme of the type in question may be positioned C-terminally, N-terminally or internally in the hybrid enzyme. Linker sequence The linker sequence may be any suitable linker sequence. In preferred embodiments the linker sequence is derived from the Athelia rolfsii glucoamylase, the A.niger glucoamylase, the A. kawachii alpha-amylase such as a linker sequence selected from the group consisting of A. niger glucoamylase linker: TGGTTTTATPTGSGSVTSTSKTTATASKTSTSTSSTSA (SEQ ID NO:22), A. kawachii alpha-amylase linker: TTTTTTAAATSTSKATTSSSSSSAAA T T S S S (SEQ ID NO:23), Athelia rolfsii glucoamylase linker: GATSPGGSSG S (SEQ ID NO:24), and the PEPT linker: PEPTPEPT (SEQ ID NO:25). In another preferred embodiment the hybrid enzymes has a linker sequence which differs from the amino acid sequence shown in SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, or SEQ ID NO:25 in no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position. Carbohydrate-binding domain A carbohydrate-binding domains (CBD), or as often referred to, a carbohydrate-binding modules (CBM), is a polypeptide amino acid sequence which binds preferentially to a poly- or oligosaccharide (carbohydrate), frequently - but not necessarily exclusively - to a water-insoluble (including crystalline) form thereof. CBDs derived from starch degrading enzymes are often referred to as starch-binding domains (SBD) or starch-binding modules (SBM). SBDs are CBDs which may occur in certain amylolytic enzymes, such as certain glucoamylases, or in enzymes such as cyclodextrin glucanotransferases, or in alpha-amylases. Likewise, other sub-classes of CBDs would embrace, e.g. cellulose-binding domains (CBDs from cellulolytic enzymes), chitin-binding domains (CBDs which typically occur in chitinases), xylan-binding domains (CBDs which typically occur in xylanases), mannan-binding domains (CBDs which typically occur in mannanases). CBDs are found as integral parts of large polypeptides or proteins consisting of two or more polypeptide amino acid sequence regions, especially in hydrolytic enzymes (hydrolases) which typically comprise a catalytic domain containing the active site for substrate hydrolysis and a carbohydrate-binding domain (CBD) for binding to the carbohydrate substrate in question. Such enzymes can comprise more than one catalytic domain and one, two or three CBDs, and optionally further comprise one or more polypeptide amino acid sequence regions linking the CBD(s) with the catalytic domain(s), a region of the latter type usually being denoted a "linker". Examples of hydrolytic enzymes comprising a CBD - some of which have already been mentioned above - are cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. CBDs have also been found in « algae, e.g., in the red alga Porphyra purpurea in the form of a non-hydrolytic polysaccharide-binding protein. In proteins/polypeptides in which CBDs occur (e.g. enzymes, typically hydrolytic enzymes), a CBD may be located at the N or C terminus or at an internal position. That part of a polypeptide or protein (e.g. hydrolytic enzyme) which constitutes a CBD per se typically consists of more than about 30 and less than about 250 amino acid residues. The "Carbohydrate-Binding Module of Family 20" or a CBM-20 module is in the context of this invention defined as a sequence of approximately 100 amino acids having at least 45% homology to the Carbohydrate-Binding Module (CBM) of the polypeptide disclosed in figure 1 by Joergensen et al (1997) in Biotechnol. Lett. 19:1027-1031. The CBM comprises the last 102 amino acids of the polypeptide, i.e. the subsequence from amino acid 582 to amino acid 683. The numbering of Glycoside Hydrolase Families applied in this disclosure follows the concept of Coutinho, P.M. & Henrissat, B. (1999) CAZy - Carbohydrate-Active Enzymes server at URL: http://afmb.cnrs-mrs.fr/-cazy/CAZY/index.html or alternatively Coutinho, P.M. & Henrissat, B. 1999; The modular structure of cellulases and other carbohydrate-active enzymes: an integrated database approach. In "Genetics, Biochemistry and Ecology of Cellulose Degradation", K. Ohmiya, K. Hayashi, K. Sakka, Y. Kobayashi, S. Karita and T. Kimura eds., Uni Publishers Co., Tokyo, pp. 15-23, and Bourne, Y. & Henrissat, B. 2001; Glycoside hydrolases and glycosyltransferases: families and functional modules, Current Opinion in Structural Biology 11:593-600. Examples of enzymes which comprise a CBD suitable for use in the context of the invention are alpha-amylases, maltogenic alpha-amylases, cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. Further CBDs of interest in relation to the present invention include CBDs derived from glucoamylases (EC 3.2.1.3) or from CGTases (EC 2.4.1.19). CBDs derived from fungal, bacterial or plant sources will generally be suitable for use in the context of the invention. Preferred are CBDs of fungal origin, more preferably from Aspergillus sp., Bacillus sp., Klebsiella sp., or Rhizopus sp. In this connection, techniques suitable for isolating the relevant genes are well known in the art. Preferred for the invention is CBDs of Carbohydrate-Binding Module Family 20. CBDs of Carbohydrate-Binding Module Family 20 suitable for the invention may be derived from glucoamylases of Aspergillus awamori (SWISSPROT Q12537), Aspergillus kawachii (SWISSPROT P23176), Aspergillus niger (SWISSPROT P04064), Aspergillus oryzae (SWISSPROT P36914), from alpha-amylases of Aspergillus kawachii (EMBL:#AB008370), Aspergillus nidulans (NCBI AAF17100.1), from beta-amylases of Bacillus cereus (SWISSPROT P36924), or from CGTases of Bacillus circulans (SWISSPROT P43379). Preferred is a CBD from the alpha- amylase of Aspergillus kawachii (EMBL:#AB008370) as well as CBDs having at least 50%, 60%, 70%, 80% or even at least 90%, 95%, 96%, 97%, 98%, or 99% identity with the CBD of the alpha-amylase of Aspergillus kawachii (EMBL:#AB008370), i.e. a CBD having at least 50%, 60%, 70%, 80% or even at least 90%, 95%, 96%, 97%, 98%, or 99% identity with the amino acid sequence of SEQ ID NO:2. Also preferred for the invention are the CBDs of Carbohydrate-Binding Module Family 20 having the amino acid sequences shown in SEQ ID NO:5, SEQ ID NO:6, and SEQ ID NO:7 and disclosed in PCT application no. PCT/DK2004/000456 (or Danish patent application PA 2003 00949) as SEQ ID NO:1, SEQ ID NO:2 and SEQ ID NO:3 respectively. Further preferred CBDs include the CBDs of the glucoamylase from Hormoconis sp. such as from Hormoconis resinae (Syn. Creosote fungus or Amorphotheca resinae) such as the CBD in SWISSPROT:QQ3Q45 (SEQ ID NO:8), from Lentinula sp. such as from Lentinula edodes (shiitake mushroom) such as the CBD of SPTREMBLQ9P4C5 (SEQ ID NO:9), from Neurospora sp. such as from Neurospora crassa such as the CBD of SWISSPROT:P14804 (SEQ ID NO:10), from Talaromyces sp. such as from Talaromyces byssochlamydioides such as the CBD from NN005220 (SEQ ID NO:11), from Geosmithia sp. such as from Geosmithia cylindrospora, such as the CBD of NN48286 (SEQ ID NO: 12), from Scorias sp. such as from Scorias spongiosa such as the CBD of NN007096 (SEQ ID NO:13), from Eupenicillium sp. such as from Eupenicillium ludwigii such as the CBD of NN005968 (SEQ ID NO:14), from Aspergillus sp. such as from Aspergillus japonicus such as the CBD from NN001136 (SEQ ID NO:15), from Penicillium sp. such as from Penicillium cf. miczynskii such as the CBD of NN48691 (SEQ ID NO:16), from Mz1 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 SPTREMBLQ12623 (SEQ ID NO:19). Most preferred CBDs include the CBDs of the glucoamylase from Aspergillus 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 according to the invention are any CBD having at least 50%, 60%, 70%, 80% or even at least 90%, 95%, 96%, 97%, 98%, or 99% identity to any of the afore mentioned CBD amino acid sequences. Further suitable CBDs of Carbohydrate-Binding Module Family 20 may be found at URL: http://afmbcnrs-mrs.fr/-cazy/CAZY/indexhtml). Once a nucleotide sequence encoding the substrate-binding (carbohydrate-binding) region has been identified, either as cDNA or chromosomal DNA, it may then be manipulated in a variety of ways to fuse it to a DNA sequence encoding the enzyme of interest. The DNA fragment encoding the carbohydrate-binding amino acid sequence and the DNA encoding the enzyme of interest are then ligated with or without a linker. The resulting ligated DNA may then be manipulated in a variety of ways to achieve expression. In an embodiment the alpha-amylase comprised in the hybrid is an alpha-amylase described above in the "Alpha-amylase"-section. In a preferred embodiment the alpha-amylase is of fungal origin. In a more preferred embodiment the alpha-amylase is an acid alpha-amylase. 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 the alpha-amylase is derived from a strain of Aspergillus oryzae or Aspergillus niger. In a specific embodiment the alpha-amylase is the A.oryzae acid alpha-amylase disclosed in SEQ ID NO:39. In a specific embodiment the linker sequence may be derived from a strain of Aspergillus, such as the A. kawachii alpha-amylase (SEQ ID NO: 23) or the A. rolfsii glucoamylase (SEQ ID NO: 24). In an embodiment the CBD is derived from a strain of Aspergillus or Athelia. In a specific embodiment the CBD is the A. kawachii alpha-amylase shown in SEQ ID NO:1 or the A. rolfsii glucoamylase shown in SEQ ID NO:21. Preferred is the embodiment wherein the hybrid enzyme comprises an alpha-amylase sequence derived from the A.niger acid alpha-amylase catalytic domain having the sequence shown in SEQ ID NO:38, and/or a linker sequence derived from the A. kawachii alpha-amylase shown in SEQ ID NO: 23 or the A. rolfsii glucoamylase shown in SEQ ID NO: 24, and/or the CBD is derived from the A. kawachii alpha-amylase shown in SEQ ID NO: 2, the A. rolfsii glucoamylase shown in SEQ ID NO: 21 or the A.niger glucoamylase shown in SEQ ID NO: 22. In a preferred embodiment the hybrid enzyme comprises the A.niger acid alpha-amylase catalytic domain having the sequence shown in SEQ ID NO:38, the A. kawachii alpha-amylase linker shown in SEQ ID NO: 23, and A. kawachii alpha-amylase CBD shown in SEQ ID NO:2. In a specific embodiment the hybrid enzyme is the mature part of the amino acid sequence shown in SEQ ID NO: 28 (A. niger acid alpha-amylase catalytic domain-A. kawachii alpha-amylase linker-A niger glucoamylase CBD), SEQ ID NO:30 (A. niger acid alpha-amylase catalytic domain-A kawachii alpha-amylase linker-A rolfsii glucoamylase CBD), or SEQ ID NO:32 (A. oryzae acid alpha-amylase catalytic domain-A. kawachii alpha-amylase linker-A-cawachill alpha-amylase CBD) , or SEQ ID NO:34 (A. niger acid alpha-amylase catalytic domain-A rolfsii glucoamylase linker-A rolfsii glucoamylase CBD), or SEQ ID NO: 36 (A. oryzae acid alpha-amylase catalytic domain-A rolfsii glucoamylase linker-A. rolfsii glucoamylase CBD) or the hybrid consisting of A. niger acid alpha-amylase catalytic domain (SEQ ID NOS: 4 or 38, respectively)-^, kawachii glucoamylase linker (SEQ ID NO: 23) -A.kawachi glucoamylase CBD (SEQ ID NO: 2) or a hybrid enzyme that has an amino acid sequence having at least 50%, 60%, 70%, 80% or even at least 90%, 95%, 96%, 97%, 98%, or 99% identity to any of the afore mentioned amino acid sequences. In another preferred embodiment the hybrid enzyme has an amino acid sequence which differs from the amino acid sequence amino acid sequence shown in SEQ ID NO:28 (A. niger acid alpha-amylase catalytic domain-A kawachii alpha-amylase linker-A niger glucoamylase CBD), SEQ ID NO:30 (A. niger acid alpha-amylase catalytic domain-A. kawachii alpha-amylase linker-A rolfsii glucoamylase CBD), SEQ ID NO:32 (A. oryzae acid alpha-amylase catalytic domain-A. kawachii alpha-amylase linker-A.kawachii alpha-amylase CBD) , SEQ ID NO:34 (A. niger acid alpha-amylase catalytic domain-A. rolfsii glucoamylase linker-A. rolfsii glucoamylase CBD) or SEQ ID NO:36 (A. oryzae acid alpha-amylase catalytic domain-A. rolfsii glucoamylase linker-A.ro/fe// glucoamylase CBD) or the hybrid consisting of A. niger acid alpha-amylase catalytic domain (SEQ ID NOS: 4 or 38, respectively)-A. kawachii glucoamylase linker (SEQ ID NO: 23) -A.kawachi glucoamylase CBD (SEQ ID NO: 2) in no more than 10 positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position. Preferably the hybrid enzyme 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 sequence 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:!!, 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. In yet another preferred embodiment the CBD sequence has an amino acid sequence which differs from the amino acid sequence amino acid sequence 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 in no more than 10 amino acid positions, no more than 9 positions, no more than 8 positions, no more than 7 positions, no more than 6 positions, no more than 5 positions, no more than 4 positions, no more than 3 positions, no more than 2 positions, or even no more than 1 position. In a most preferred embodiment the hybrid enzyme comprises a CBD derived from a glucoamylase from A. rolfsii, such as the glucoamylase from A. rolfsii AHU 9627 disclosed in US patent 4,727,026. The invention described and claimed herein is not to be limited in scope by the specific embodiments herein disclosed, since these embodiments are intended as illustrations of several aspects of the invention. Any equivalent embodiments are intended to be within the scope of this invention. Indeed, various modifications of the invention in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description. Such 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 are cited herein, the disclosures of which are incorporated by reference in their entireties. Materials & Methods Enzymes - Acid Alpha-Amylase A: Wild-type acid alpha-amylase derived from Aspergillus nigerdisclosed in SEQ ID NO: 38. - Acid Alpha-Amylase B: hybrid acid alpha-amylase consisting of A. niger acid alpha-amylase catalytic domain (SEQ ID NO: 38)-A kawachii glucoamylase linker (SEQ ID NO: 23) - A. kawachii glucoamylase CBD (SEQ ID NO: 2). - Alpha-Amylase C: Hybrid alpha-amylase shown in SEQ ID NO: 44 comprising a catalytic domain (CD) from Rhizomucor pusillus alpha-amylase having a carbohydrate-binding domain (CBD) from the Athelia rolfsii glucoamylase. - Alpha-Amylase D: wild-type Rhizomucor pusillus alpha-amylase disclosed in SEQ ID NO: 43. Enzyme classification numbers (EC numbers) referred to in the present specification with claims are in accordance with the Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology, Academic Press Inc, 1992. Eabric - Vlisco fabric from Vlisco BV, NL Buffer Citrate Buffer 10mM Citrate buffer (pH4.0) 1.376 g of Citric acid monohydrate and 1.015 g of Sodium Citrate dihydrate are dissolved in 1 L of de-ionized water. Methods: Determination of homology/identity For purposes of the present invention, the degree of homology is determined as the degree of identity between two amino acid sequences as determined by the Clustal method (Higgins, 1989, CABIOS 5: 151-153) using the LASERGENE™ MEGALIGN™ software (DNASTAR, Inc., Madison, Wl) with an identity table and the following multiple alignment parameters: Gap penalty of 10, and gap length penalty of 10. Pairwise alignment parameters were Ktuple=1, gap penalty=3, windows=5, and diago-nals=5]. Acid alpha-amylase activity (AFAU Assay) When used according to the present invention the activity of any acid alpha-amylase may be measured in AFAU (Acid Fungal Alpha-amylase Units), which are determined relative to an enzyme standard. 1 FAU is defined as the amount of enzyme which degrades 5.260 mg starch dry matter per hour under the below mentioned standard conditions. Acid alpha-amylase, an endo-alpha-amylase (1,4-alpha-D-glucan-glucano-hydrolase, E.C. 3.2.1.1) hydrolyzes alpha-1,4-glucosidic bonds in the inner regions of the starch molecule to form dextrins and oligosaccharides with different chain lengths. The intensity of color formed with iodine is directly proportional to the concentration of starch. Amylase activity is determined using reverse colorimetry as a reduction in the concentration of starch under the specified analytical conditions. Alpha-amylase activity (KNU) The amylolytic activity may be determined using potato starch as substrate. This method is based on the break-down of modified potato starch by the enzyme, and the reaction is followed by mixing samples of the starch/enzyme solution with an iodine solution. Initially, a blackish-blue color is formed, but during the break-down of the starch the blue color gets weaker and gradually turns into a reddish-brown, which is compared to a colored glass standard. One Kilo Novo alpha amylase Unit (KNU) is defined as the amount of enzyme which, under standard conditions (i.e. at 37°C +/- 0.05; 0.0003 M Ca2+; and pH 5.6) dextrinizes 5260 mg starch dry substance Merck Amylum solubile. A folder EB-SM-0009.02/01 describing this analytical method in more detail is available upon request to Novozymes A/S, Denmark, which folder is hereby included by reference. Determination of Acid Amylolytic Activity (FAU) One Fungal Alpha-Amylase Unit (1 FAU) is defined as the amount of enzyme, which breaks down 5.26 g starch (Merck Amylum solubile Erg. B.6, Batch 9947275) per hour at Novozymes' standard method for determination of alpha-amylase based upon the following standard conditions: Substrate Soluble starch Temperature 37°C pH 4.7 Reaction time 7-20 minutes A detailed description of Novozymes' method for determining KNU and FAU is available on request as standard method EB-SM-0009.02/01. Desizing (Tegewa method) The starch size residue is determined visually by comparing an iodine stained fabric swatch to a standard set of photos with 1-9 scale where 1 is dark blue and 9 has no color stain. The iodine stain solution is made by dissolving 10 g Kl in 10 ml water, add 0.635g l2, and 200mL ethanol in deionized water to make total 1L 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 Verband TEGEWA, Karlstrasse 21, Frankfurt a.M., Germany. EXAMPLES Example 1 Desizing cotton fabric with wild-type acid Alpha-Amylase A A 100% cotton fabric (270g/m2) was from Boras Wafveri Kungsfors AB, Sweden. It was made in 2003 with Cupper 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 dry size pick up on the warp yarn was 8%. The size contained mainly Kollotex 5, Solvitose XO, and beef tallow wax with emulsifier. Kollotex 5 is a low viscous potato starch ester. Solvitose XO is a high viscous starch ether with DS about 0.07. Fabric swatches were cut to about 25g each. Three buffers were made for this study. Buffer pH2 was made by dissolving 11.53g 85% phosphoric acid in 4.5 liter pure water, titrating with 5N HCI to pH 1.95, then adding water to 5 liter. Buffer pH3 was made by dissolving 11.53g 85% phosphoric acid in 4.5 liter pure water, titrating with 5N NaOH to pH 2.95, then adding water to 10 liter. Buffer pH4 was made by dissolving 6.005g acetic acid in 4.5 liter pure water, titrating with 5N HCI to pH 3.95, then adding water to 10 liter. A 2g/l nonionic surfactant (wetting agent) was added in each buffer. The measured final pH values of these three buffers were 2, 2.99, and 3.98, respectively. For each treatment, a 1 liter buffer solution was taken. A given amount of wild type Acid Alpha-Amylase A was added in the buffer. A fabric swatch was immersed in the solution for 30 seconds and then padded through a padder (Werner Mathis) to achieve 85% wet pickup. The fabric swatch was rolled and sealed in a plastic bag. It was then incubated at 50°C oven for 2 hours. The fabric swatch was washed in a pad-steam range (Werner Mathis) which contained four small rinsing boxes. The water temperature in rinsing boxes is 95, 95, 90, and 90°C, respectively. After drying 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 color stain. Thus higher number indicates a better starch removal. The visual evaluation was done by at least three professionals and an average TEGEWA value was given for each fabric sample. The results are shown in Table 1. The wild type acid Alpha-Amylase A treated fabric gave higher TEGEWA value than the fabric treated with no enzyme control at all three pH conditions, indicating that acid Alpha-Amylase A hydrolyzed and removed starch size on fabric. Increased enzyme activity resulted in higher TEGEWA indicating increased starch removal. Example 2 Desizing cotton fabric with Acid Alpha-Amylase B The same fabric swatch and buffers were prepared as in Example 1. Acid Alpha-Amylase B was different from the wild-type Acid Alpha-Amylase A used in Example 1 in that the enzyme protein was constructed to comprise the wild-type Acid Alpha-Amylase A from A niger (Example 1) linked with a CBD from Aspergillus kawachii acid alpha-amylase. The enzyme used in this study has an activity of 316 AFAU/g. The same treatments and measurements were conducted as in Example 1. swatch was sequentially washed with water in the same beaker three times at 95, 75, and 40°C, respectively. After dry overnight in air, the swatch was evaluated the same way as in Example 1. The results are shown in Table 2. The same conclusions in Example 1 can be drawn. A TEGEWA value of above 5 was achieved in lab equipment, indicating desizing at acidic condition is viable approach. The residue of metal ions on fabric was also evaluated. The fabric was first cut through 1 mm sieve with a Thomas-Wiley mill. Fabric mash 4.00 (+/-0.01) g was mixed with 80 mL 1g/L EDTA solution. The mixture was incubated at 70°C and 200 ' rpm in a shaker (new Brunswick Scientific Co. Inc, Series 25) for 15 hours. After cooled down for about 30 minutes, the mixture was centrifuged at 2500 rpm at 20°C for 10 minutes. The supernatant was collected for metal content analysis with a Perkinelmer atomic absorption spectrophometer. n/a = not measured Example 5 The same type of fabric from Boras Wafveri Kungsfors AB (Sweden) as in Example 1 was used and the swatch was cut to about 62g each. Buffer pH4 was made by dissolving 12.01g acetic acid in 4.5 liter pure water, titrating with 5N HCI to pH 3.95, then adding water to 10 liter. A 2g/l nonionic surfactant (wetting agent) was added the buffer. The final pH value of the buffer was 3.99. For each treatment, a 1.2 liter buffer solution was taken. A given amount of alpha-amylase enzyme was added in the buffer. A fabric swatch was immersed in the solution for 30 seconds and then padded through a padder (Werner Mathis) to achieve 90% wet pickup. The fabric swatch was cut into two equal size swatches. Both were rolled and sealed in plastic bags. One bag was incubated at 40°C oven and the other at room temperature (20°C). Both swatches were treated for 16 hours. The fabric swatch was washed in a pad-steam range (Werner Mathis) which contained four small rinsing boxes. The water temperature in rinsing boxes is 95, 95, 90. and 90°C. resoectivelv. Example 6 Alpha-Amylase D for desizing fabric at pH 4.0 De-ionized water was filled into beakers, up to 13 cm from the bottom. The water temperature was adjusted to 60°C. 200 ml of 10 mM Citrate buffer (pH 4.0) was added to each beaker and placed in a Lab-o-Mat. The solutions were heated to 60°C. Different amounts of Alpha-Amylase D were added to the buffer. The final enzyme concentrations were 50FAU/L, 100FAU/L, 200FAU/L and 400FAU/L, respectively. Two swatches of Vlisco fabric were fixed in a pair of forceps and dipped in the impregnation bath for 30 seconds and then padded. The dipping and squeezing was repeated. The wet pick up was about 100%. One swatch was placed in a two-layer plastic bag, the air was squeezed out and the bag was placed in water bath at 60°C for 2 hours. The other swatch was placed in a two-layer plastic bag, the air was squeezed out, and the bag was kept at room temperature for 24 hours. The samples were removed from the water bath after the required time was reached. The samples were fixed in the forceps, dipped in a hot rinse solution (90°C) for 30 seconds and squeezed. The dipping and squeezing was repeated twice. The fabric was dipped in cold tap water for around 60 seconds and water was squeezed off with hands. The swatches were placed on a shelf and dried at room temperature. The residual starch content on the fabric was checked by TEGEWA rating. The result of the tests is shown in Fig. 1 Example 7 Alpha-Amylase C desizing at pH 4,Q The desizing procedure described in Example 6 was repeated, except that Alpha-Amylase C was used. The result of the tests is shown in Fig. 2. CLAIMS 1. A process for desizing of a sized fabric containing starch or starch derivatives during manufacture of a fabric, which process comprises incubating said sized fabric in an aqueous treating solution having a pH in the range between 1 and 5 which aqueous treating solution comprises an alpha-amylase. 2. The process of claims 1, wherein the pH is in the range between pH 1 and 4, especially between pH 2 and 4. 3. The process of claims 1 or 2, wherein the alpha-amylase is of bacterial or fungal, such as filamentous fungus origin 4. The process of any of claims 1-3, wherein the alpha-amylase is an acid alpha-amylase. 5. The process of claims 3 or 4, wherein the alpha-amylase is a derived from a strain of Aspergillus, preferably Aspergillus niger, Aspergillus awamori or Aspergillus oryzae, or a strain of Rhizomucor, preferably Rhizomucor pusillus, or a strain of Meripilus, preferably a strain of Meripilus giganteus. 6. The process of claim 5, wherein the Aspergillus alpha-amylase is the acid Aspergillus niger alpha-amylase disclosed in SEQ ID NO: 38, or a variant thereof. 7. The process of claim 5, wherein the Rhizomucor alpha-amylase is the Rhizomucor pusillus alpha-amylase disclosed in SEQ ID NO: 43, or a variant thereof. 8. The process of any of claims 1-7, wherein the alpha-amylase, preferably an acid alpha-amylase 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. 9. The process of claims 1-8, wherein the bacterial alpha-amylase is derived from a strain of the genus Bacillus, preferably derived from a strain of Bacillus sp., more preferably a strain of Bacillus licheniformis Bacillus amyloliquefaciens, Bacillus stearothermophilus, Bacillus subtilis, or Bacillus sp., such as Bacillus sp. NCIB 12289, NCIB 12512, NCIB 12513, DSM 9375, DSMZ 12648, DSMZ 12649, KSM AP1378, KSM K36 or KSM K38. 10. The process of claim 9, wherein the bacterial alpha-amylase is the AA560 alpha-amylase disclosed as SEQ ID NO: 40. 11. The process of claims 9 or 10, wherein the Bacillus alpha-amylase has one or more deletions in position D183 and G184, preferably wherein said Bacillus alpha-amylase variant further has a substitution in position N195F (using the SEQ ID NO: 40 numbering). 12. The process of claim 9, wherein the Bacillus alpha-amylase has one or more deletions in position D183 and G184, preferably wherein said Bacillus alpha-amylase variant further has one or more of the following substitutions: R118K, N195F, R320K, R458K, especially wherein the variant has the following mutations: A(D183+G184)+R118K+N195F+R320K+R458K (using the SEQ ID NO: 40 numbering). 13. The process of any of claims 1-12, wherein the alpha-amylase is present in a concentration of 0.05-150 KNU/L treating solution, preferably, 1-100 KNU/L treating solution, especially 2-20 KNU/L treating solution or 0.05-150 KNU/kg fabric, preferably, 1-100 KNU/kg fabric, especially 2-20 KNU/kg fabric. 14. The process of any of claims 1-13, wherein the alpha-amylase is a hybrid enzyme comprising a carbohydrate-binding domain (CBD). 15. The process of any of claims 1-14, wherein the alpha-amylase comprises a starch-binding domain of fungal or bacterial origin. 16. The process of claims 14 or 15, wherein the carbohydrate-binding domain (CBD) is derived from a strain of Aspergillus, preferably derived from a strain of Aspergillus sp., a strain of Athelia, or a strain of Talaromyces. i 17. The process of claim 16, wherein the amino acid sequence of the carbohydrate- binding domain (CBD) is derived from Aspergillus kawachii, such as the CBD having the amino acid sequence shown in SEQ ID NO: 2, or the amino acid sequence of the carbohydrate-binding domain (CBD) is derived from Aspergillus niger, preferably the CBD having the amino acid sequence shown in SEQ ID NO: 20, or the amino acid sequence of the carbohydrate-binding domain (CBD), derived from Athelia sp., preferably from Athelia rolfsii, especially the CBD amino acid sequence shown in SEQ ID NO: 21. 18. The process of claim 15, wherein the alpha-amylase comprising a CBD comprises a linker between the alpha-amylase and CBD or starch-binding domain. 19. The process of claim 18, wherein the linker is derived from is derived from a strain of Athelia, preferably an Athelia rolfsii glucoamylase linker (SEQ ID NO: 24), a strain of Aspergillus, preferably an Aspergillus niger glucoamylase linker (SEQ ID NO: 22) or an Aspergillus kawachii alpha-amylase linker (SEQ ID NO: 23). 20. The process of any of claims 1-19, wherein the alpha-amylase is the hybrid alpha-amylase shown in SEQ ID NO: 44 comprising a catalytic domain (CD) from Rhizomucor pusillus alpha-amylase having a carbohydrate-binding domain (CBD) from the Athelia rolfsii glucoamylase. 21. The process of any of claims 1-20, wherein the process is carried out at a temperature in the range from 5-90°,in particular 20 to 90°C. 22. The process of claim 21, wherein the process is carried out at a temperature between 20 and 40°C for a suitable period of time, preferably between 8 and 24 hours. 23. The process of claim 21, wherein the process is carried out at a temperature between 40 and 90°C for a suitable period of time, preferably between 1 and 6 hours. 24. The process of any of claims 1-23, wherein the process is carried out in the presence of a surfactant, preferably the surfactant is present in a concentration of 0.1-10 g/L, preferably around 1 g/L. 25. The process of any of claims 1-24, wherein the fabric is made from fibres of natural or man-made origin. 26. The process of any of claims 1-25, wherein the fabric is cotton fabric, denim, linen, ramie, viscose, lyocell, or cellulose acetate. 27. The process of any of claims 1-26, wherein the fabric is made of fibres from animal origin, in particular silk or wool. 28. The process of any of claims 1-27, wherein the fabric is made of polyester fibers of man-made or natural origin, such as poly(ethylene terephthalate) or poly(lactic acid). 29. The process of any of claims 1-28, wherein the fabric is made of fibers of nylon, acrylic, or polyurethane. 30. The process of any of claims 1-29, wherein the fabric is a polyester containing fabric or garment consists of essentially 100% polyester. 31. The method of claim 1-30, wherein the polyester fabric is a polyester blend, such as a polyester and cellulosic blend, including polyester and cotton blends; a polyester and wool blend; a polyester and silk blend; a polyester and acrylic blend; a polyester and nylon blend; a polyester, nylon and polyurethane blend; a polyester and polyurethane blend, rayon (viscose), cellulose acetate and tencel..

Documents:

2366-CHENP-2007 AMENDED PAGES OF SPECIFICATION 26-02-2013.pdf

2366-CHENP-2007 AMENDED CLAIMS 26-02-2013.pdf

2366-CHENP-2007 OTHER PATENT DOCUMENT 26-02-2013.pdf

2366-CHENP-2007 OTHER PATENT DOCUMENT 1 26-02-2013.pdf

2366-CHENP-2007 OTHERS 26-02-2013.pdf

2366-CHENP-2007 CORRESPONDENCE OTHERS 26-11-2012.pdf

2366-CHENP-2007 EXAMINATION REPORT REPLY RECEIVED 26-02-2013.pdf

2366-CHENP-2007 FORM-1 03-10-2013.pdf

2366-CHENP-2007 FORM-1 26-02-2013.pdf

2366-CHENP-2007 FORM-3 03-10-2013.pdf

2366-CHENP-2007 FORM-3 26-02-2013.pdf

2366-CHENP-2007 POWER OF ATTORNEY 26-02-2013.pdf

2366-CHENP-2007 POWER OF ATTORNEY 03-10-2013.pdf

2366-CHENP-2007 EXAMINATION REPORT REPLY RECEIVED 03-10-2013.pdf

2366-chenp-2007-abstract.pdf

2366-chenp-2007-claims.pdf

2366-chenp-2007-correspondnece-others.pdf

2366-chenp-2007-description(complete).pdf

2366-chenp-2007-drawings.pdf

2366-chenp-2007-form 1.pdf

2366-chenp-2007-form 3.pdf

2366-chenp-2007-form 5.pdf

2366-chenp-2007-pct.pdf