MXPA02000268A

MXPA02000268A - Detergent compositions comprising a raw starch degrading enzyme.

Info

Publication number: MXPA02000268A
Application number: MXPA02000268A
Authority: MX
Inventors: Johan Smets
Original assignee: Procter & Gamble
Priority date: 1999-07-01
Filing date: 2000-06-30
Publication date: 2002-06-21
Also published as: EP1196530A1; CA2377942A1; CN1382204A; AR025849A1; WO2001002529A1; BR0012466A; AU6061500A; JP2003504456A; EP1065260A1

Abstract

The present invention relates to detergent compositions, including laundry, dishwashing, and/or hard surface cleaner compositions, comprising a raw starch degrading enzyme characterised by a ratio of activity to degrade raw corn starch (Ra) to activity to degrade gelatinised starch (Ga): [Ra/Ga] above 0.2, preferably above 0.35. Such compositions provide excellent removal of starch-containing stains and soils, and when formulated as laundry compositions, excellent whiteness maintenance and dingy cleaning.

Description

DETERGENT COMPOSITIONS THAT COMPRISE AN ENZYME THAT DEGRADES THE RAW STARCH FIELD OF THE INVENTION The present invention relates to detergent compositions comprising an enzyme that degrades raw starch. BACKGROUND OF THE INVENTION The operation of a detergent product is judged by many factors including the ability to remove soils. Therefore, detergent compositions such as surfactants, bleaching agents and enzymes have been incorporated into the detergents. A specific example of this is the use of proteases, lipases, amylases and / or cellulases. Proteases are enzymes that are commonly used in cleaning applications. Proteases are known for their ability to hydrolyze other proteins. This capacity has been exploited through the incorporation of naturally occurring or genetically engineered protease enzymes in laundry detergent compositions. The inclusion of lipolytic enzymes of detergent compositions is known to improve cleaning performance, for example, it increases the removal of dirt and stains containing triglycerides from the fabrics. The activity of the cellulase is one in which the cellulose fibers or substrates are attacked by the cellulase and depends on the particular function of the cellulase, which may be endo- or exocellulase, and of the respective hemi-cellulases. The cellulosic structures are depolymerized or divided into smaller fractions and thus are more soluble or dispersible. This particular activity on fabrics provides cleaning, rejuvenation, softening and tactile sensation characteristics generally improved to the fabric structure. Amiiase enzymes have long been recognized in detergent compositions that provide for the removal of starchy food residues or starch films from crockery or other hard surfaces or provide cleaning performance in dirty starch as well as other soiled ones that are typically found in laundry and dish washing applications. Indeed, starch materials such as amylose and amylopectin, constitute one of the main components of the dirty / stains encountered in washing clothes, dishes or hard surfaces. On the other hand, the textile industry uses starch materials in its textile finishing processes. Therefore, amylase enzymes have been incorporated for some time into detergent products for the removal of spots containing starch. However, it has surprisingly been found that such commonly used detergent amylases can not effectively hydrolyze raw starch materials. A substantial part of the starch material effectively remains in the raw form even when processed within the food or textile industries. In particular, it has been discovered that food stains such as rice, spaghetti, potatoes, corn, cereals, etc. recovered on fabrics, tableware and other hard surfaces contain a substantial amount of raw starch. Additionally, it has surprisingly been discovered that such crude starch remains on the surfaces, trapping additional dirt, and when it is on a cloth surface, it leads to a dirty appearance of the surface to be cleaned. It can be observed from the foregoing, that there is a need to formulate detergent products that solve the elimination of such soiled / stains containing raw starch. Accordingly, the aforementioned purpose has been met by the formulation of a detergent composition comprising a very efficient enzyme for degrading raw starch. Such enzymes are characterized by an activity ratio to degrade raw corn starch (Ra) to activity to degrade gelatinized starch (Ga): [Ra / Ga] greater than 0.2, preferably greater than 0.35. It has been further discovered that the operation of the detergent compositions of the present invention is improved by the addition of an additional enzyme that is selected from an iipase., a protease, an α-amylase and / or a pullulanase (a neopululanase, a pullulanase type 11) and / or by the addition of a detergent ingredient selected from nonionic surfactants and / or flocculating agents. EP 368 341 discloses detergent compositions comprising a surfactant and at least one starch debranching enzyme which is selected from the group consisting of pullulanase, isopululanase and isoamylase and preferably with an improved detergent a-amylase for starch fouling. GB 2 228 945 discloses an automatic washing machine washing composition comprising an enzyme capable of breaking α-1,6-glucosidic bonds. WO98 / 26078 is directed to enzymes of mutant α-amylase H with improved stability. EP 450 627 discloses a novel detergent composition containing an alkaline pullulanase with excellent detergency against starchy soils. W094 / 19468 discloses a DNA fragment containing a gene for alkaline pullulanase useful as a component of detergents. U.S. Patent 5,665,585 is directed to an amino acid and DNA sequence of a singular P-giucoamylase having a high debranching activity, a Trichoderma host cell transformed with such sequences, the expression of such recombinant glucoamylase P and the industrial uses in particular fermentation of alcohol, for recombinant enzymes and host transformed with them. U.S. Patent 3,640,877 discloses a detergent preparation containing a glucose and oxidase system of glucose or starch, amyloglucosidase and glucose oxidase as a precursor of hydrogen peroxide and a hydroxylamine which stabilizes the hydrogen peroxide formed during use of the detergent. W095 / 29996 discloses a novel glucose oxidase, a process for its production and its use in bleaching and detergent compositions as well as its use as a dough strengthener. Such an enzyme has many applications in the personal care area and the bakery industry, preferably in combination with another enzyme that is selected from amyloglucosidase, lactoperoxidase, α-amylase or a maltogenic exo-amylase. However, the use of a very efficient enzyme in the degradation of raw starch, ie, an enzyme that is characterized by a Ra / Ga greater than 0.2, for the elimination of dirty stains containing raw starch in a detergent composition of washing clothes has never been recognized before. SUMMARY OF THE INVENTION The present invention relates to detergent compositions, including laundry detergent compositions, dish washing, and / or hard surfaces, which comprise an enzyme that degrades raw starch which is characterized by an activity ratio to degrade starch from crude corn (Ra) to activity to degrade gelatinized starch (Ga): [Ra / Ga] greater than 0.2, preferably greater than 0.35. Such compositions provide excellent stain and stain removal containing starch, and when formulated as laundry detergent compositions, excellent whiteness maintenance and cleaning of soiled soil. DETAILED DESCRIPTION OF THE INVENTION The essential component of the detergent compositions of the present invention is an enzyme that degrades raw starch which is characterized by an activity ratio to degrade raw corn starch (Ra) to activity to degrade geiatinized starch (Ga) : [Ra / Ga] greater than 0.2, preferably greater than 0.35. The enzymes of the present invention are selected from enzymes having an activity on α-branched polysaccharides, more specifically starch substrates, on gelatinized starch. The ratio of activity to degrade raw corn starch [Ra] to the activity to degrade gelatinized corn starch [Ga] is defined as follows: The activity of the enzyme, which degrades α-branched polysaccharides, more specifically substrates of starch, on gelatinized or raw starch, is measured using normal tests to measure enzymatic activities. The degradation rate of crude starch is the ratio of the activities of the enzyme tested on raw starch and on gelatinized starch. The same test conditions for temperature, pH, ionic strength, buffer, and enzyme concentration are used in both tests on gelatinized and crude starches. The protocol of the test to obtain the Ra / Ga value of the enzymes is as follows:) The tests are carried out at a temperature of 40aC. 2) First, the pH profile of the enzyme is obtained over raw starch. The aforementioned profile is conventionally obtained from! plot of activity percentage versus pH. This optimum pH value will be used for the following enzyme tests. 3) The activity of the enzyme tested on gelatinized starch is then determined at the optimum pH mentioned above. 4) The type of starch that is used is Amylum corn starch, as it is representative of the starch commonly found in laundry. A 2% solution of crude starch is used. To obtain the gelatinized starch solution a crude starch solution is heated at 70 ° C for at least 60 minutes. 5) The composition of the buffer used in the test depends on the pH optimum of the enzyme. The composition and concentration of the buffer should be identical for further measurements of both the activity of the crude starch and the gelatinized starch. For example: for Rhizopus amyloglucosidase, a 0.1 M acetate buffer at pH 5.0 is used; for the alkaline amylase that degrades the crude starch of Bacillus sp. ÍMD 370, 0.1 M Tris of maleate buffer (Ver 2) is used). 6) The enzyme concentration used in the test should be identical for the measurements of both the activity of the crude starch and the gelatinized starch. 7) The enzymatic activity is measured by the determination of the reduction sugars in solution. Suitable methods are the following: The Bemfield method for determining reduction sugars using dinitrosalicylic acid is described in Bemfieid P., Amviase a. Methods Enzvmoloav 1, 149-158 (1955) and the method for determining reduction sugars with copper bicinconitate as described in Fox JD et al., Analvtical Biochemistry 195, 93-96 (1991) or in Waffenschmidt S. et al. , Anal. Biochem. 165 337-340 (1987). Prior to the determination of reducing sugars, the solution is boiled for 3 minutes and centrifuged to inactivate the enzyme. 8) The incubation time to measure the enzymatic activities is 6 hours. 9) Enzymatic activity is expressed as the number of reducing sugars produced per hour and per mg of pure active enzyme. 10) The rate of degradation of crude starch is defined as the ratio of the enzymatic activity as obtained in 9), in crude starch and gelatinized starch. For example, the glucoamylase activity in gelatinized starch is measured by measuring the release of glucose produced by the enzyme in a reaction mixture of 2% gelatinized corn starch. The activity is measured by the release of reducing sugars produced in μmol per hour per mg of pure active enzyme. The same test can then be used to measure the activity of the enzyme in crude starch, but replacing the 2% gelatinized corn starch. By "% of raw corn starch." In both tests, the temperature is 40SC, the same pH and buffer solution is used and the incubation time is 6 hours.An enzyme that degrades crude starch is generally comprised in the compositions detergents of the present invention at a level of from 0.0002% to 10%, preferably 0.001% to 2%, more preferably 0.001% to 1% pure enzyme by weight of the total detergent composition Enzymes that degrade the crude starch suitable have a [Ra / Ga] greater than 0.2 for the purpose of the present invention can be selected from the following classes of enzymes (IUPAC Classification): amyloglucosidase EC 3.2.1.3, a-amylase EC 3.2.1.1, beta-amylases EC 3.2.1.2, isoamiase EC 3.2.1.68, pullulanase type I EC 3.2.1.41, isopululanase EC 3.2.1.57, neopuiulanase EC 3.2.1.135, pullulanase type II, dextranase dextrin EC 2.4.1.24, glycosyltransferase cyclodextrin EC 2.4.1.19 and maltogenic alpha-amylase EC 3.2.1.133. Accordingly, the detergent compositions will comprise a combination of several enzymes that degrade the starch. Suitable for the purpose of the present invention is an amylogogyucosidase of the IUCAP Classification EC 3.2.1.3. Such amylogogyucosidase is a glucan 1,4-a-glucosidase; it is also referred to as "glucoamylase, α-amylase, lisomal α-glucosidase, acid maltase or exo-1,4-α-glucosidase" and its systematic name is 1,4-a-D-glucan glucohydrolase. The amyloglucosidases hydrolyze both a-1, 4 and a-1, 6 bonds in polysaccharides such as starch, releasing glucose units from non-reducing ends of polysaccharides. These two activities are different. By hydrolyzing the glycosidic linkages a-1, 4 as a-1, 6, the amyloglucosidases release β-D-glucose units from the terminal non-reducing ends of a glucose polymer such as starch. Amiioglucosidases suitable for the purpose of the present invention are Glucoamylase I (GAl) from Aspergillus awamori var. Kawachi expressed in Saccharomuces cerevisiae) Glucoamylase from Aspergillus awamori and ar. X100; Glucoamylase from Corticium rolfsii; Glucoamylase GA1 and GA2 with molecular weight of 74 and 96 kDa of Aspergillus niger, Glucoamylase of Rhizoctania solani; Glucoamylase from Chalare paradoxa; Glucoamylase from Aspergillus shirousami (Gaase) 68 kPa; Aspergillus sp. 10 K-27 glucoamylase with a molecular weight of 76 kDa kDa and 48 kDa kDa proteolysis product; Glycoamylase from Rhizopus sp. Glud 74 kDa; Glucoamylase from Clostridium thermohydrosulfuricum and Glucoamylase from Rhizopus niveus. The most preferred glucoamylases are Aspergillus sp. K-27 glucoamylase with molecular weight of 76 kDa kDa; Glucoamylase from ^ 15 Rhizopus niveus. . Alpha-amylases, EC 3.2.1.1, is a 1,4-a-D-glucan glucanohydrolase that provides endohydrolysis of 1,4-a-D-glycosidic linkages in polysaccharides containing three or more linked D-glucose 1,45 units. Alpha-amylases suitable for the purpose of the present invention 20 are α-amylase from Cryptococcus sp. S-2 molecular weight 66 kDa; α-amylase from Lipomyces konoenkoae expressed in Saccharomyces cerevisiae 76 kDa; Bacillus circulans F-2 α-amylase expressed in E. coli (RSDA); amylase from Aspergillus sp. K-27; a-amylase from Bacillus sp. IMD 434,! MD 370; a-amylase from Cytophaga sp. Beta-amylases, EC 3.2.1.2, is a 1,4-a-D-glucan maltohydrolase that provides endohydrrhysis of 1,4-a-D-glycosidic linkages in polysaccharides to eliminate successive maltose units of nonreducing ends of the chain. β-amyiases suitable for the purpose of the present invention are β-amylase from Emericella nidulans (Aspergillus); β-amylase from B. substituted R2 and expressed in E. coli and β-amylase from Clostridium thermosulfurogenes produced in Bacillus brevis. The isopululanase enzymes are classified under the IUPAC classification EC 3.2.1.57 and the systematic name Pullulan '4-glucanohydrolase. The enzymes of isopululanase hydrolyze puiulan to isopanosa (6-a-maltosilglucose). Isoamylase enzymes have the ability to debranch glycogen. These are classified under the IUPAC classification EC 3.2.1.68 and the systematic name glycogen 6-glucanohydrolase. Isoamyase enzymes hydrolyse the branched 1,6-a-D-glucosidic bonds in glycogen, amylopectin and their dextrin β-limit. Isoamylases are distinguished from the pullulanase enzyme by their inability to attack pullulan, by limited action on dextrins to-limit and by their total action on glycogen. Neopululanase enzymes are defined as enzymes that degrade pullulan to form panosa and these are classified under the IUPAC EC 3.2.1.135 classification. Neopululanase enzyme, which is puliulan 4-D-glucan hydrolase, has a capacity to divide both the 1,4- and 1, 6-glucosidic junctions found in common stained or dirty starch and carbohydrate types. For example, this enzyme hydrolyses pullulan to panosa (6-alpha-D-glucosylmaltose). Specifically, the neopululanase enzyme can catalyze can catalyze four types of reactions including hydrolysis of alpha- (1-> 4) -glucosidic linkage, hydrolysis of aI- (1-6) -glucosidic bond, transglycosylation to form the alpha- (1? 4) -glucosidic bond hydrolysis, and transglycosylation to form the hydrolysis of aifa- (1? 6) -glucosidic bond. In contrast, other known enzymes only catalyze one of these reactions or in case two reactions are catalyzed, the second is weak. In addition, the four types of reactions are catalyzed by the same mechanism. Type II pullulanase enzymes are defined as amilopuiulanases and randomly hydrolyze the a, 1-4 bonds in addition to the branch points (a-1 -6 bonds) in polysaccharides and dextrins, unlike pullulanase type I enzymes that only hydrolyze bonds a, 1-6 in branched polysaccharides. An additional suitable enzyme of the amylase class is dextrinase dextrinase. Dextrin dextranase (EC 2.4.1.2) is an enzyme that produces Dextran and low molecular weight oligosaccharides of starch. The cyclomaltodextrin glucanotransferase, EC 2.4.1.19, is an enzyme that cyclizes part of a 1,4-aD-glucan chain through the formation of a 1,4-aD-glucosidic bond and has the systematic name of 1, 4- aD-giucan 4-aD- (1, 4-aD-gIucan) -transferase (of cyclisation). Enzymes suitable for the purpose of the present invention are CGT-ase from Bacilius circulans 251; CGT-handle of Bacillus circulans E192; CGT-asa from Bacillus sp. B1018 and CGT-asa of Bacillus fírmus. Maltogenic alpha-amylase A maltogenic alpha amylase of the IUPAC Classification EC 3.2.1.133 that hydrolyzes 1,4-a-D-glucosidic bonds in polysaccharides to remove successive alpha-maltose units from the non-reducing ends of the chains is also suitable. Suitable maltogenic alpha-amylases are the cloned amylase from Bacillus as described in EP 120 693 commercially available under the trademark Novamyl from Novo Nordisk A / S; maltogenic alpha-amylase variants having CGT-asa activity and CGT-asa variants having maltogenic alpha-amylase activity, as well as manufactured hybrid enzymes described in W099 / 43793 and maltogenic alpha-amylase variants with improved properties (altered physical-chemical properties, eg, an altered optimal pH, improved thermostability, increased specific activity, an altered division configuration or an increased capacity to reduce retrogradation of starch or bread rancidity), based on the three-dimensional structure of the maltogenic alpha-amylase Novamyl described in W099 / 47394. A specific enzyme satisfying the criteria [Ra / Ga] of the present invention is for example the amyloglucosidase of Rhizopus niveaus marketed by Amano under the trademark Gluczyme and the alpha-amylase of Lipomyces konomenboae of the gel LKA1. In another embodiment of the present invention, the detergent compositions of the present invention may additionally comprise one or more domains that bind starch. Such a domain that binds starch may be added in the detergent compositions of the present invention, as is, or may be part of a chimeric amyloglucosidase hybrid. Indeed, the amiioglucosidases of the present inventions will preferably have or will be added a Starch Binding Domain (SBD). In general enzymes such as amylases, cellulases, and xylanases have a modular structure consisting of a catalytic domain and at least one non-catalytic domain whose function is generally described as that of a polysaccharide-binding domain (PBD), a domain that binds starch (SBD), cellulose binding domain (CBD) and xylan fixing domain. The function of these fixing domains is to selectively bind to the substrate of the enzyme, and in particular, the main function of the SBD is to bind to starch. It has surprisingly been found that the detergent compositions of the present invention comprising one or more SBDs and / or wherein the amyloglucosidases comprise such a SBD will provide a more efficient starch / stain removal. It has been additionally discovered that. such enzymes can be formulated in a cost-effective manner. Without wishing to be bound by theory, it is believed that such amyloglucosidases will be specifically targeted more effectively to their substrate from the washing solutions and thus have better deposition on stained / dirty spots containing starch for improved performance and / or new On the other hand, it is believed that the fixation of the SBD will break the surface of the starch resulting in a higher hydrolytic velocity. SBDs suitable for use in the present invention are the SBDs comprised in the glucoamyiase of Aspergillus niger (Sigma) and in the β-galactosidase of A. Awamori. The recovery and fusion of the SBDs can be achieved as described in Ford, C. et al., J. Cell. Biochem. (Suppl 14D: 30 (1990) and Chen, L. et al., Abst. Annu.Met.Am. Soc.Microbiol.90: 269 (1990) .The aforementioned enzymes may be of any suitable origin, such as plant, animal, bacterial, fungal and yeast origin, the origin can additionally be mesophilic or extromophilic (psychrophilic, psychrotropic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or unpurified forms of these enzymes can be used. in dayIt is a common practice to modify wild-type enzymes by protein / genetics engineering techniques in order to maximize their operating efficiency in the detergent compositions of the invention. For example, the variants can be designed so that the compatibility of the enzyme is increased to the commonly found ingredients of such compositions. Alternatively, the variant can be designed so that the optimum pH, bleach or chelating agent stability, catalytic activity and the like are adjusted to adjust the particular cleaning application. In particular, attention should be paid to oxidation-sensitive amino acids in the case of bleach stability and surface charges for surfactant compatibility. The isoelectric point of such enzymes can be modified by the replacement of some charged amino acids, e.g., an increase in the isoelectric point can help improve compatibility with anionic surfactants. The stability of the enzymes can be further improved by creating, for example, additional salt bridges and reinforcing the metal binding sites to increase the chelating stability. Detergent components The detergent compositions of the present invention should contain at least one additional detergent component. The precise nature of these additional components, and levels of incorporation of these will depend on the physical form of the composition, and the nature of the cleaning operation for which it is to be used. The detergent compositions of the present invention will preferably comprise an additional enzyme which is selected from a protease, a iipase, a conventional α-amylase, a conventional neopululase, a pullulanase type I or II conventional a flocculating agent and / or a non-ionic surfactant. In a preferred embodiment, the present invention relates to a laundry and / or fabric care washing composition comprising an amyloglucosidase (Examples 1-16). In a second embodiment, the present invention relates to dishwashing compositions or compositions for cleaning the home (Examples 17-23). The compositions of the invention can be formulated, for example, as hand washing and automatic dishwashing compositions, laundry detergent compositions by hand and in the washing machine including laundry additive compositions and compositions suitable for use in soaking and / or pretreatment of soiled fabrics, fabric softening compositions that are added in the rinse, and compositions for use in hard surface cleaning operations of the home. When formulated as compositions for use in hand dishwashing methods the compositions of the invention preferably contain a surfactant and preferably other detergent compounds which are selected from organic polymeric compounds, foam improvers, group II metal ions, solvents, hydrotropes and additional enzymes. When formulated as suitable compositions for use in a washing machine washing method, the compositions of the invention preferably contain both a surfactant and an improving compound and additionally one or more detergent components that are preferably selected from organic poiimeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap dispersants, suspending and antiredeposition agents and corrosion inhibitors. The laundry detergent compositions may also contain softening agents, as additional detergent components. Such compositions containing an amyloglucosidase provide for the removal of stains containing ahymidon, maintenance of whiteness and cleaning of the soiled soil when formulated as laundry detergent compositions. The compositions of the invention can also be used as detergent additive products. Such additive products are intended to complement or improve the operation of conventional detergent compositions. The detergent compositions according to the present invention can be liquid, in paste, gels, bars, tablets, sprays, foams, powders or granules. The granulated compositions may also be in "compact" form and the liquid compositions may also be in "concentrated" form. If necessary, the density of laundry detergent compositions in the present invention ranges from 400 to 1200 g / liter, preferably 600 to 950 g / liter of the composition measured at 20 aC. The "compact" form of the compositions in the present invention is best reflected by density and, in terms of the composition, by the amount of inorganic filler salt; Inorganic filler salts are conventional ingredients of the detergent compositions in powder form; In conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition. In compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, more preferably not exceeding 5% by weight of the composition. The inorganic filler salts, as it is desired to mean in the present compositions, are selected from alkali metal salts and alkaline earth metal sulfates or chlorides. A preferred filler salt is sodium sulfate. The liquid detergent compositions according to the present invention can also be in a "concentrated form", in which case, the liquid detergent compositions according to the present invention will contain a lower amount of water, as compared to conventional liquid detergents. Typically the water content of the concentrated liquid detergent is preferably less than 40%, more preferably less than 30%, more preferably even less than 20% by weight of the detergent composition. Detergent compositions suitable for use in the present invention are selected from the group consisting of the compounds described below. SURFACTANT SYSTEM The detergent compositions according to the present invention generally comprise a surfactant system wherein the surfactant may be selected from nonionic and / or anionic and / or cationic and / or ampholytic and / or zwitterionic and / or semi-polar surfactants. Preferably, the detergent compositions of the present invention will comprise a nonionic surfactant, preferably a nonionic surfactant based on polyoxyethylene condensates with alcohol. Indeed, it has surprisingly been found that the detergent compositions of the present invention additionally comprising a nonionic surfactant provide for the improved removal of starch from fabrics, tableware and other hard surfaces. Without wishing to be bound by theory, it is believed that the nonionic surfactant is absorbed onto the granulated surface of the starch thereby breaking the starch structure and influencing and preventing the retrogradation process of the starch. Such breaking of the structure increases the accessibility of the enzyme to its substrate. On the other hand, nonionic surfactants can also be used in a pretreatment process and therefore can reduce the starch retrogradation process. Accordingly, stained / soiled spots containing starch are more easily hydrolyzed by the enzyme and a synergistic decomposition of the starchy soil occurs by the amyloglucosidase and the non-ionic surfactant. The surfactant is typically present at a level of 0.1% to 60% by weight. More preferred levels of incorporation are 1% to 35% by weight, more preferably 1% to 30% by weight of the detergent compositions according to the invention. The surfactant is preferably formulated to be compatible with the enzymatic components present in the composition. In liquid or gel compositions the surfactant is more preferably formulated so as to promote, or at least not degrade, the stability of any enzyme in these compositions. Nonionic Surfactants: Polyethylene oxide, polypropylene, and polybutylene oxide condensates of alkylphenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with condensates of polyethylene oxide being preferred. These compounds include the condensation products of alkylphenols having an alkyl group containing from 6 to 14 carbon atoms, preferably from 8 to 14 carbon atoms, in 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 about 2 to 25 moles, more preferably about 3 to about 15 moles of ethylene oxide per mole of alkylphenol. Commercially available nonionic surfactants of this type include Igepal ™ CO-630, marketed by GAF Corporation; and Triton ™? -45, X-114, X-100 and X-102, all marketed by Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkylphenol ethoxylates). The condensation products of primary and secondary aiiphatic alcohols with 1 to 25 moles, approximately, of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl chain of the aliphatic alcohol may be straight or branched, primary or secondary, and generally contain from about 8 to about 22 carbon atoms. The condensation products of alcohols having an alkyl group containing from 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 are preferred. and more preferably 2 to 5 moles of ethylene oxide per mole of alcohol are present in the condensation products mentioned above. Examples of commercially available nonionic surfactants of this type include Tergitol ™ 15-S-9 (the linear alcohol condensation product C- | - | -Ci5 with 9 moles of ethylene oxide), Tergitol ™ 24-L-6 NMW (the condensation product of C12-C14 primary alcohol with 6 moles of ethylene oxide with a narrow molecular weight distribution), both marketed by Union Carbide Corporation; Neodol ™ 45-9 (the linear alcohol condensation product C14-C15 with 9 moles of ethylene oxide), Neodol ™ 23-3 (the linear alcohol condensation product C-12-C13 with 3.0 moles of ethylene oxide), Neodol ™ 45-7 (the linear condensation product of C14-C15 with 7 moles of ethylene oxide), Neodol ™ 45-5 (the linear condensation product of C14-C15 with 5 moles of ethylene oxide) marketed by Shell Chemical Company, Kyro ™ EOB (the condensation product of C13-C15 alcohol with 9 moles of 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. The preferred scale of HLB balance in these products is 8-11 and more preferred 8-10. Also useful as the nonionic surfactant of the surfactant systems of the present invention are the alkyl polysaccharides which are disclosed in U.S. Patent 4,565,647, Filling, issued January 21, 1986, which has a hydrophobic group containing from 6 to 30 carbon atoms, approximately, preferably from 10 to 16 carbon atoms, approximately and a polysaccharide, eg, a polyglucoside, a hydrophilic group containing from 1.3 to 10, approximately, preferably from 1.3 to 3, approximately, more preferably from 1.3 to 2.7, approximately, of saccharide units. Any reducing saccharide containing 5 or 6 carbon atoms can be used, eg, glucose, galactose and galactosyl moieties can be replaced by glucosyl moieties (optionally the hydrophobic group joins at 2-, 3-, 4-, etc. positions thus providing a glucose or galactose unlike a glucoside or galactoside). The intersaccharide linkages can be, e.g., between the one position of the additional saccharide unit and the 2-, 3-, 4-, and / or 6- positions in the previous saccharide unit. Preferred alkyl polyglycosides have the formula R2 (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 about 0 to 10, preferably 0; and x is from about 1, 3 to 10, preferably from about 1, 3 to 3, more preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpolyethoxyalcohol is first formed and then reacted with glucose, or a source of glucose, to form the glucoside (attachment in the 1-position). The additional glycosyl units can then be linked between their 1-position and the 2-, 3-, 4- and / or 6-position of the above glycosyl units, 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 systems of the present invention. The hydrophobic portion of these compounds will preferably have a molecular weight of about 1500 to 1800 and will exhibit insolubility in water. The addition of polyoxyethylene halides 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 to the point where the polyoxyethylene content is about 50% of the total product weight of the product. condensation, which corresponds to the condensation with up to 40 moles approximately of ethylene oxide. Examples of compounds of this type include some of the commercially available Plurafac ™ LF404 and Pluronic ™ surfactants, marketed by BASF. Other suitable nonionic surfactants are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylene diamine. The hydrophobic moiety of these products consists of the reaction product of ethylene diamine and excess propylene oxide, and generally has a molecular weight of about 2500 to 3000. This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to 80% by weight of polyethylene and has a molecular weight of from 5,000 to 11,000. Examples of this type of nonionic surfactant include certain commercially available Tetronic ™ compounds, marketed by BASF. It is preferred to use as the non-ionic surfactant of the surfactant systems of the present invention, the polyethylene oxide condensates of alkylphenols, the condensation products of primary and secondary aliphatic alcohols with 1 to 25 moles, approximately, of oxide. of ethylene, alkylpolysaccharides, and mixtures thereof. Most preferred are the C8-C1 alkylphenol ethoxylates having from 3 to 15 ethoxy groups and the C8-C-? 8 alcohol ethoxylates (preferably C0 on average) having from 2 to 10 ethoxy groups, and mixtures thereof. Highly preferred nonionic surfactants are the polyhydroxy fatty acid surfactants of the formula: R2-C-N-Z, II I, R1 wherein R "1 is H, or R" 1 is hydrocarbyl Cj-4, 2- hydroxyethyl, 2-hydroxypropyl or a mixture of these, R2 is C5.31 hydrocarbyl and Z is polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof. Preferably, R "is methyl, R2 is a C 1-15 alkyl or straight Cj Q-Q alkyl or an alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction.

Anionic surfactants: Anionic surfactants suitable for use are linear alkylbenzene sulphonate surfactants, alkyl ester sulfonate including the linear esters of C8-C20 carboxylic acids (ie, fatty acids) which are sulfonated with gaseous SO3 according to The Journal of the Americal Oil Chemists Societv. 52 (1975), pages 323-329. Suitable starting materials include natural fatty substances as derived from tallow, palm oil, etc. The preferred alkyl ester sulphonate surfactant, especially for fabric washing applications, comprises alkyl ester sulphonate surfactants of the structural formula: ## STR3 ## - CH-C 11 -QFT 4 I S03 wherein R3 is a C8-C20 hydrocarbyl, preferably an alkyl, or combination thereof, R4 is a C1-C6 hydrocarbyl, preferably an alkyl, or combination thereof, and M is a cation forming a water-soluble salt with alkyl ester sulfonate. Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethanolamine, and triethanolamine. Preferably, R3 is Cio-C-iß alkyl. and R 4 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 the water soluble salts or acids of the formula ROSO3M wherein R is preferably a hydrocarbyl Cj 0 -C24. preferably an alkyl or hydroxyalkyl having a C10-C20 alkyl component > more preferably a C 12 -C 18 alkyl hydroxyalkyl, and is H or a cation, eg, an alkali metal cation (eg, sodium, potassium, lithium), or ammonium or substituted ammonium cations (eg, methyl-, dimethyl-, and trimethylammonium and dimethylpiperdinium cations and quaternary ammonium cations which are derived from alkylamines such as ethylamine, diethylamine, triethiamine, and mixtures thereof, and the like). Typically, the C12-C16 alkyl chains are preferred for the lower wash temperatures (eg, less than 50dC) and the C-? S-18 alkyl chains are preferred for the higher wash temperatures (eg, greater than 50SC) . Other anionic surfactants useful for detersive purposes may also be included in the laundry detergent compositions of the present invention. These may include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di-, and triethanolamine salts), soap, primary or secondary alkane sulfonates, C8-C24 olefin sulfonates, sulfonated polycarboxylic acids which are prepared by sulfonation of the pyrolyzed product of alkali earth metal citrates, eg, as described in British Patent Specification No. 1, 082,179, C8-C24 alkyl polyglycol ether sulphates (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, acyl glycerol fatty sulphonates, oleyl glycerol fatty sulfates, ethylene oxide alkylphenol ether sulfates, paraffin sulphonates, alkyl phosphates, isethionates such as acyl isethionates, N-acyl taurates, alkyl succinamates and sulfosuccinamates, monoesters of sulfosuccinamates (especially C12-C18 saturated and unsaturated monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated Cß-C- | 2 diesters), acyl sarcosinates, aikidopolysaccharide sulfates such as alkyol polyol sucrose sulfates (non-sulphonated nonionic compounds) which are described below), branched primary alkyl sulphates, and alkylpolyethoxycarboxylates such as those of the formula RO (CH2CH2?) j < -CH2COO-M-r wherein R is a C8-C22 alkyl, k is an integer from 1 to 10, and M is a soluble salt-forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, "hydrogenated rosin, and resin acids and hydrogenated resin acids that are present in or derived from resin oil." Further examples are described in "Surfactants. and Detergents "(Vol. I and II by Schwartz, Perry and Perch). A variety of such surfactants are also generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975, to Laughiin, et al., In Column 23, line 58 to Column 29, line 23 ( which is incorporated herein by reference) When included therein, the laundry detergent compositions of the present invention typically comprise from 1% to 40%, approximately, preferably from 3% to 20%, by weight, of such anionic surfactants.

Highly preferred anionic surfactants include alkoxylated alkyl sulfate surfactants and water soluble salts or acids of these of the formula RO (A) mS03M wherein R is a substituted C 10 -C 24 alkyl or hydroxyalkyl group having a C 10- alkyl component C24, preferably a C12-C20 alkyl or hydroxyalkyl »more preferably C2-6 alkyl or hydroxyalkyl-A is an ethoxy or propoxy unit, m is greater than zero, typically between 0.5 and 6, approximately, more preferably between 0.5 and 3, approximately, and M is H or a cation which may be, for example, a metal cation (eg, sodium, potassium, lithium, calcium, magnesium, etc.), ammonium cation or substituted ammonium cation. The ethoxylated alkyl sulfates as well as the propoxylated alkyl sulfates are contemplated in the present invention. Specific examples of substituted ammonium cations include methyl-, dimethyl-, trimethylammonium cations and quaternary ammonium cations such as tetramethylammonium and dimethylpiperdinium cations and those which are derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like . Exemplary surfactants are polyoxylated C12-C18 alkyl sulfate (1.0) (C-j2-Ci8E (1.0) M), C-12-C18 poly-ethoxylated alkyl sulfate (2.25) (C12-C- | 8E (2.25) M), C12-C18 alkyl ethoxylated sulfate (3.0) (C12-C- | 8E (3 > 0) M). and C-12-C18 polyethoxylated alkyl sulfate (4.0) (C12-Ci8E (4.0) M), wherein M is conveniently selected from sodium and potassium. The detergent compositions of the present invention may also contain ampholytic, zwitterionic, and semipolar surfactants, as well as nonionic and / or anionic surfactants other than those already described in the present invention. Cationic Surfactants: Cationic Surfactants suitable for use in the detergent compositions of the present invention are those having a long chain hydrocarbyl group. Examples of such cationic surfactants include ammonium surfactants such as alkyltrimethylammonium halides, and those surfactants having the formula: [R2 (OR3) and] [R4 (OR3) and] 2R5N + X "wherein R2 is an alkyl group or alkyl benzyl having approximately 8 to 18 carbon atoms in the alkyl chain, each R3 is selected from the group consisting of -CH2CH2-, -CH2CH (CH3) -, - CH2CH (CH2? H) -, -CH2CH2CH2- and mixtures thereof, each R 4 is selected from the group consisting of C 1 -C 4 alkyl, C 1 -C 4 hydroxyalkyl, benzyl ring structures that are formed by the joining of two R groups -CH 2 CHOH-CHOHCOR 6 CHOHCH 2 OH wherein R6 is any hexose or a hexose polymer having a molecular weight less than about 1000, and hydrogen when and is not 0, R5 is the same as R4 or is an alkyl chain where the total number of carbon atoms of R2 plus R5 is not more than about 18, each y is from 0 to 10, approximately, and the sum of the values of y is from about 0 to 15; and X is any compatible anion. Monastic quaternary surfactant suitable for the present invention has the formula (I): Formula I wherein R-j is a short chain alkyl (C6-C10) or alkylamidoalkyl of the formula (II): Formula II and is 2-4, preferably 3. in which R2 is H or a C1-C3 alkyl, wherein x is 0-4. preferably 0-2, more preferably 0, wherein R3, R4 and R5 are the same or different and can be a short chain alkyl (C1-C3) or akoxylated alkyl of the formula III, wherein X- is a counterion , preferably a halide, eg, chloride or. metisulfate.

Formula III R6 is C- | -C4 and z is 1 or 2. Preferred quaternary ammonium surfactants are those defined in formula I in which R-j is Ce, Cio. or mixtures of these, x = o, R3, R4 = CH3 and R5 = CH CH OH. Most preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition having the formula: R R2R3R4N + X- (where R- is alkyl CSC-J Q, each of R2, R3, R4 is independently C1-C4 alkyl, C1-C4 hydroxyalkylene, benzyl, and - (C2H4o) HH where x has a value of 2 to 5, and X is an anion. No more than one of R2, R3 or R4 must be benzyl. The preferred alchemical chain length for R- | is C-J2-C15 particularly where the alkyl group is a mixture of chain lengths that are derived from coconut or palm kernel fat or are derived synthetically by means of the olefin accumulation or the OXO synthesis of alcohols. Preferred groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X can be selected from halide, methosulfate, acetate and phosphate ions. Examples of suitable quaternary ammonium compounds of the formula (i) for use in the present invention are: coconut trimethylammonium chloride or bromide; coconut methylhydroxyethylammonium chloride or bromide: decyltriethylammonium chloride; decildimethylhydroxyethylammonium chloride or bromide; C12-15 dimethylhydroxyethyl ammonium chloride or bromide coconut bromide or de-dimethylhydroxyethylammonium chloride; Myristyrytrimethylammonium methylisulfate: lauryldimethylbenzylammonium chloride or bromide; lauryldimethyl (ethenoxy) 4ammonium chloride or bromide; choline esters (compounds of the formula (i) wherein R-j is alkyl CH2-CH2-O-C-C12-14 and R2R3R4 are methyl); II or di-alkylimidazolines [compounds of the formula (i)]. Other cationic surfactants useful in the present invention are also disclosed in U.S. Patent 4,228,044, Cambre, issued October 14, 1980 and in European Patent Application EP 000,224. Typical preferred fabric softening cationic components include the water-insoluble quaternary ammonium fabric softening actives, which have been most commonly used are ammonium chloride or di-long alkyl chain methyl sulfate. Preferred cationic softeners among these include the following: 1) dimethyl ammonium chloride of ditallow (DTDMAC); 2) Dihydrogenated tallow dimethyl ammonium chloride; , 3) Dihydrogenated tallow dimethyl ammonium methylisulfate; 4) distearyl dimethyl ammonium chloride; 5) dimethylammonium dioleyl chloride; 6) dipalmityl hydroxy ethyl methylammonium chloride; 7) stearyl benzyl dimethyl ammonium chloride; 8) tallow trimethylammonium chloride; 9) Dihydrogenated tallow trimethylammonium chloride; 10) C12-14 alkylhydroxyethyl dimethylammonium chloride; 11) C12-18 alkyldihydroxyethyl methylammonium chloride; 12) di (stearoyloxyethyl) dimethylammonium chloride (DSOEDMAC); 02 13) dimethylammonium chloride of di (tallowyl oxyethyl); 14) imidazolinium methylisulfate of ditallow; 15) 1 - (2-seboii amido ethyl) -2-tallowyl imidazolinium methylisulfate. Biodegradable quaternary ammonium compounds have been presented as alternatives to traditionally used d-long alkyl chain ammonium chlorides and methylsulfates. Such quaternary ammonium compounds contain long chain alkyl (en) i) groups interrupted by functional groups such as carboxy groups. The aforementioned materials and fabric softening compositions containing them are disclosed in many publications such as EP-A-0,040,562, and EP-A-0,239,910. The quaternary ammonium compounds and amine precursors in 01. the present invention have the following formula (I) or (I l): wherein Q is selected from -C-C (O) -, -C (0) -0-, -0-C (0) -0-, -NR4-C (0) -C (0) -NR4-; R1 is (CH2) n-Q-T or T3; ze R2 is (CH2) m-Q-T4 or T5 or R3; R3 is C4 alkyl or hydroxyalkyl CrC or H; R 4 is H or C 1 -C alkyl or C 4 C hydroxyalkyl; T1, T2, T3, T4, T5 are independently C11-C22 alkyl or alkenyl. n and m are integers from 1 to 4; and X "is an anion compatible with the softener.Non-limiting examples of anions compatible with the softener include chlorine or methyl sulfate.The alkyl, or alkenyl, chain T1, T2, T3, T4, T5 must contain at least 11 atoms carbon, preferably at least 16 carbon atoms The chain can be straight or branched Sebum is a convenient and low cost source of long chain alkyl and alkenyl material Particularly preferred are compounds wherein T 1, T 2, T3, T4, T5 represent the mixture of long chain material which are typical for sebum Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening compositions in the present invention include: 1) N, N- Chloride di (tallowyloxyethyl) -N, N-dimethylammonium; 2) N, N-di (tallowyloxyethyl) -N-methyl-N- (2-hydroxyethyl) ammonium methylisulfate; N, N-di (2-tallowyloxy-2-oxo-ethyl) -N, N-dimethylammonium; 4) N, N-di (2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl) -N, N-dimethyl-ammonium chloride; 5) N- (2-tallowyloxy-2-ethyl) -N- (2-tallowyloxy-2-oxo-ethyl) -N, N-dimethylammonium chloride; 6) N, N, N-tri (tallowyl-oxyl-ethyl) -N-methylammonium chloride; 7) N- (2-Seboi-oxy-2-ethyl) -N-tallowyl-N, N-dimethylammonium chloride; 8) 1,2-Disboboyl-oxy-3-trimethylammoniopropane chloride; and mixtures of any of the above materials. When included inside, the detergent compositions of the present invention typically comprise from 0.2% to 25%, approximately, preferably from 1% to 8%, approximately, by weight of such cationic surfactants. Ampholytic Surfactants: Ampholytic Surfactants are also suitable for use in the detergent compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aiiphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight chain or branched chain. One of the aliphatic substituents contains at least 8 carbon atoms, typically about 8 to about 18 carbon atoms, and at least one contains an anionic group which is solubilized in water, e.g., carboxy, sulfonate, sulfate. See U.S. Patent No. 3,929,678, to Laughiin et al., Issued December 30, 1975 in column 19, lines 18-35, for examples of ampholytic surfactants. When included within, the detergent compositions of the present invention typically comprise from 0.2% to 15%, approximately, preferably from 1% to 10%, approximately, by weight of such ampholytic surfactants. Zwitterionic Surfactants: Zwitterionic surfactants are also suitable for use in detergent compositions. These surfactants can be broadly described as amine, secondary and tertiary derivatives, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See U.S. Patent No. 3,929,678, to Laughiin et al., Issued December 30, 1975 in column 19, line 38 to column 22, line 48, for examples of zwitterionic surfactants. When included therein, the detergent compositions of the present invention typically comprise from 0.2% to 15%, approximately, preferably from 1% to 10%, approximately, by weight of such zwitterionic surfactants. Semi-polar nonionic surfactants: Semi-polar nonionic surfactants are a special category of non-ionic surfactants that include water-soluble amine oxides containing an alkyl moiety of 10 to 18 carbon atoms, approximately, and 2 halves selected from the group consisting of of alkyl groups and hydroxyalkyl groups containing from 1 to about 3 carbon atoms; and water-soluble phosphine oxides containing an alkyl moiety of about 10 to about 18 carbon atoms, and two moieties which are 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 an alkyl moiety of about 10 to 18 carbon atoms, and a moiety which is selected from the group consisting of alkyl and hydroxyalkyl moieties of about 1 to about 3 carbon atoms. Semi-polar non-ionic detergent surfactants include amine oxide surfactants having the formula: wherein R3 is an alkyl, hydroxyalkyl, or alkylphenyl group or mixtures thereof containing from about 8 to about 22 carbon atoms; R 4 is an alkylene or hydroxyalkylene group containing from 2 to about 3 carbon atoms or mixtures thereof; x is from about 0 to 3; and each R 5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms, or a group of polyethylene oxide containing from about 1 to about 3 ethylene oxide groups. The R5 groups may be linked together, e.g., through an oxygen or nitrogen atom, to form a ring structure. These amine oxide surfactants include in particular oxides of aiquildimethylamine CIQ-O-I S and oxides of alkoxletiidihydroxyethylamine Cs-C12. When included therein, the detergent compositions of the present invention typically comprise from 0.2% to 15%, approximately, preferably from 1% to 10%, approximately, by weight of such semi-polar nonionic surfactants. Cosurfactants The cleaning composition of the present invention may additionally comprise a cosurfactant which is selected from the group of primary or tertiary amines. Primary amines suitable for use in the present invention include amines according to the formula R1NH2 wherein R- | it is an alchemical C6-C12 chain. preferably Cß-Cio ° R4X (CH2) n. X s s -O-, -C (0) NH- or -NH-, R4 is an alkyl chain CQ-C12 »n is between 1 and 5, preferably 3. The alkyl chains Rj can be straight or branched and can be interrupted with up to 12, preferably less than 5 ethylene oxide halves. Preferred amines according to the formula in the present invention are n-alkylamines. Suitable amines for use in the present invention can be selected from 1-hexyl amine, 1-octyiamine, 1-decylamine and laurylamine. Other preferred primary amines include C8-C10 oxy-propylamine, octyloxypropylamine, 2-ethylhexyloxypropylamine, lauryl-amidopropylamine and amidopropylamine. Tertiary amines suitable for use in the present invention include tertiary amines having the formula R-i R2R3N wherein R ^ y R2 are alkyl chains C-j -Cs or R3 is a C6-C12 alkyl chain »preferably C-C-io» or R3 is R4X (CH2) n. where C is -O-, -C (0) NH- or -NH-, R4 is a C4-C12 alkyl. n is between 1 to 5, preferably 2-3. R5 is H or alkyl C-j -C2 and x is between 1 to 6. R3 and R4 can be linear or branched; the alkyl chains R3 can be interrupted with up to 12, preferably less than 5, ethylene oxide moieties. Preferred tertiary amines are R-j R2R3N where R-j is a C6-C-12 alkyl chain. 2 and R3 are C1-C3 alkyl or where R5 is H or CH3 and x = 1 -2. Amidoamines of the formula are also preferred: 0 II R, - C NH - (CH2) n - N - (R2) 2 wherein R- (is C6-C-12 alkyl; n is 2-4, preferably n is 3; R2 and R3 is C1-C4 The most preferred amines of the present invention include 1-octylamine, 1-hexyl amine, 1-decylamine, 1-dodecylamine, C8-C10 oxypropylamine, coconut N-1 -3-diaminopropane, coconut alkyldimethylamine, lauryl dimethylamine, lauryl bis (hydroxyethi) amine, coconut bis (hydroxyethyl) amine, propoxylated lauryl amine 2 mole, propoxylated 2 mole octylamine, lauryl amidopropyl dimethyl amine, C8-10 amidopropyldimethylamine and C10 amidopropyldimethylamine The most preferred amines for use in the compositions in the present invention are: -hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine Especially desirable are n-dodecyldimethylamine and bishydroxyethylalkylamine of coconut and 7-fold ethoxylated oleylamine, lauryl amido propylamine and coconut amidopropylamine Conventional detergent enzymes The detergent compositions of the present invention can co In addition to the enzyme that degrades the raw starch, one or more enzymes that provide advantages of cleaning performance, fabric care and / or sterilization. The enzymes mentioned above include "enzymes that are selected from cellulases, hemicellulases, peroxidases, proteases, gluco-amylases, amylases, mannases, xyloglucans, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases , ligninases, pullulanases, tanases, pentosanas, malanases, ß-gluconases, arabinosidases, hyaluronidase, chondroitanases, laccase or mixtures thereof.

Preferably, the detergent compositions of the present invention will comprise an enzyme that is selected from a protease, a lipase, conventional α-amylase, a conventional neopululase and / or a pullulanases type I or II. By "conventional" it is meant an amyiase or a pullulanase which does not fall within the Ra / Ga ratio as defined in the present invention. Indeed, it has been found that the combination of an enzyme that degrades raw starch with a cysase-amylase enzyme, ie, a conventional α-amylase, a conventional neopululase and / or a type I or II puyulanases, within detergent compositions of the present invention, provides an excellent synergistic elimination of raw starch. Therefore, detergent compositions comprising such a combination of enzymes provide excellent stain and dirt removal containing starch and when formulated as a laundry detergent composition, excellent whiteness maintenance and cleaning of soiled soil. Additionally, the stains that are most commonly found in cleaning clothes, dishes and hard surfaces generally comprise a significant amount of proteins and triglyceride compounds. In particular, it has been discovered that starch materials are usually associated with lipid compounds. Therefore, the detergent compositions will preferably comprise a protease enzyme and / or lipase for the purpose of increasing the removal of such complex spots. Alpha-amylase As indicated above, the detergent compositions of the present invention will preferably comprise an α-amylase. α-Amylases suitable for the purpose of the present invention are described in the following: WO 94/02597, Novo Nordisk A / S, published February 3, 1994, discloses detergent compositions that incorporate mutant amylases. See also WO 95/10603, Novo Nordisk A / S, published April 20, 1995. Other amylases known to be used in cleaning compositions include both α-amylases and β-amylases. A-amylases are known in the art and include those described in U.S. Patent 5,003,257; EP 252,666; WO91 / 00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British Patent Specification No. 1, 296,839 (Novo). Other suitable amiiases are the amylases of improved stability which are described in WO 94/18314, published on August 18, 1994 and WO96 / 05295, Genencor, published on February 22, 1996, and amylase variants having additional modifications in immediate base enzyme available from Novo Nordisk A / S, which are disclosed in WO 95/10603, published in April 1995. Also suitable are the amylases described in EP 277 216, W095 / 26397 and W096 / 23873 ( all by Novo Nordisk). Examples of commercial α-amylases products are Purafect Ox Am® from Genencor and Termamyl®, Ban®, Fungamyl® and Duramyl®, all available from Novo Nordisk A / S Denmark. WO 95/26397 describes other suitable amylases: α-amylases which are characterized by having a specific activity in at least 25% higher than the specific activity of Termamyl® at a temperature range of 25aC to 552C and a pH on the scale from 8 to 10, as measured by the Phadebas® α-amylase activity test, which is described in W096 / 23873 (Novo Nordisk). Preferably, the variants are those that demonstrate improved thermal stability, more preferably those in which at least one amino acid residue equivalent to F180, R181, G182, T183, G184, or K185 has been deleted from the α-amylase base. Particularly preferred are those variants which have improved thermal stability comprising amino acid deletions R181 * + G182 * or T183 * + G184 *. Other amylolytic enzymes with improved properties relative to the activity level and the combination of thermal stability and a higher activity level are described in W095 / 35382. Additional suitable amylases are the enzymes of mutant α-amylases H that exhibit improved stability as described in WO98 / 26078 by Genencor. The amylolytic enzymes are incorporated in the detergent compositions of the present invention at a level of 0, 0001% to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition. Pullulanase type l Pullulanase type 1 is a starch debranching enzyme and can be obtained from different sources. However, it is usually derived from microorganisms. Pullulanase type I is generally included in the detergent composition of the invention in an amount of 0.0001% to 10% by weight, preferably 0.001% to 0.5% by weight. Type I pullulanase enzymes are classified under the classification IUPAC classification EC 3.2.1.41 and the systematic name of a-Dextrin 6-glucanohydrolase. The pullulanase enzymes hydrolyse the 1, 6-a-D-giucosidic bonds in pullulan, amylopectin and glycogen and in the limit dextrins of α-amylase and amylopectin β-amylase and glycogen as well as against branched oligosaccharides produced by their partial decomposition. Due to this characteristics, pullulanase is called a "debranching enzyme". Indeed, pullulanase is an enzyme that only breaks the 1-6-giicosidic linkage of the pullulan and finally produces maltotriose. Microbial sources include Aerobacter Aerogenes, Pseudomonas stutzeri, Bacillus polymyxa, B.maceranas, Klebsiella pneumonia and Streptomyces sp. The activity of this enzyme is normalized to 2O0 PUN / g (Unit of Puiulanasa Novo). 1UPN is defined as the amount of enzyme that under normal conditions hydrolyses pulalanase releasing reduced carbohydrate, with a reduction power equivalent to 1μmol of glucose per minute. It is also preferred to isolate puluyanase from a Bacillus spot No. 202-1 as described in Biochimica et Biophysica Acta. 397 (1985) 188-193. This pullulanase has an optimum pH of 8.55-9.0, and is therefore of particular interest in more alkaline detergent compositions. Puluianase was discovered for the first time from a strain that belongs to Aerobacter aerogenes by Bender and Wallensfeld in 1961 [Biochem. Z., 334, 79, (1961)]. Recently, different microorganisms capable of producing pullulanase have been reported. These microorganisms are, for example, Bacillus sp. rj. Jpn. Soc. Starch Sci .. 30, 200 (1983)]; Bacillus acidopullulyticus rAaric. Biol. Chem. 52, 2293, (1984)]; Bacillus stearqthermophilus fEur. J. Appl. Microbiol. Biotechnol .. 17, 24, (1983)]; Stftococcus mitis [Biochem. J .. 108, 33, (1968)]; Lactobacillus [Denpum Kagaku, 28, 72, (1981)]; Clostridium sp. ÍJ. Jpn. Soc. Starch Sci. 34, 1, (1987)]; and Clostridium thermosulfurogenes [Eur. J. APPI. Microbiol. Biotechnol .. 33, 511, (1990)]. Additionally, two publications have reported an alkalophilic strain of the genus Bacillus. { Bacillus sp. 202-i) and alkaline pullulanase produced (Japanese Patent Publication (Kokoku) No. 277786/1978); and the alkaline pullulanase of Bacillus sp. KSM-AP 1876 which is described in W094 / 19468 (Japanese Patent Application Exposed (Kokai) No. 8716/1991). Relevant pullulanase includes, for example, puluanas that can be obtained from Bacillus species (eg, acidopullulyticus as described in EP 063 909, such as Promozyme ™ from Novo Nordisk A / S.) Another pullulanase suitable for the detergent compositions herein invention is the alkaline pullulanase described in EP 450 627 by Kao Corporation, which has an optimum pH on the alkaline scale and is stable against surfactants. Such alkaline pullulanase includes an alkaline pullulanase A and an alkaline pullulanase B, both suitable for the purpose of the present invention. Another pullulanase suitable for detergents is described in W094 / 119468 by Kao Corporation. Also suitable are the pullulanase enzymes which are described in the following Japanese patents / applications: JP0407398 which is directed to a dishwashing detergent composition in automatic washing machine comprising a non-ionic surfactant, a calcium chelating agent, an ipase and a pullulanase alkaline for high detergency, JP06264094 which describes a laundry detergent composition comprising alkaline-resistant soaps, surfactants and pullulanase having high detergency; all by Kao Corporation. Promozyme (Novo trademark), isolated from Bacillus sp., Is particularly preferred. Pullulanase Also suitable are pullulanase enzymes which are described as starch debranching enzymes in the following Japanese patents / applications: JP 07179900, JP06172796, JPO6172792, JP04065494, JP04065494, JP02132193 and JP 02132192, all by Kao Corporation. Neopululanase An additional suitable enzyme of the amylase class for the purpose of the invention are neopululanase enzymes. Neopululanase enzymes are defined as enzymes that degrade Pullulan to form panose and these are classified under the IUPAC EC 3.2.1.135 classification. The enzyme neopuiulanase, which is Pullulan 4-D-glucan hydrolase, has a capacity to divide both the 1, 4-gIucosidic and 1, 6-glucosidic junctions found in common stained and dirty starch and carbohydrate. For example, this enzyme hydrolyses Pullulan to panosa (6-alpha-D-glucosylmaltose). Specifically, the neopululanase enzyme can catalyze four types of reactions including the hydrolysis of alpha- (1? 4) -glucosidic bond, the hydrolysis of alpha- (1? 6) -glucosidic bond, the transglycosylation to form the hydrolysis of aifa- (1? 4) -glucosidic bond, and transglycosylation to form the hydrolysis of alpha- (1? 6) -glucosidic bond. In contrast, other known enzymes only catalyze one of these reactions or in case two reactions are catalyzed, the second is weak. In addition, the four types of reactions are catalyzed by the same mechanism. Neopululanase enzymes are described in the following publications: Enzvme Chemistrv and Molecular Bioloav of Amylases and Related Enzvme. pages 28-32 (1995), edited by Amylases Research Society of Japan; H. Takata, et al. J. Biol. Chem. Volume 267, number 26, pages 15447-15452 (1992). The neopululanase enzyme can be produced by the so-called wild-type organism or by any host organism in which the gene responsible for the production of neopululanase, has been cloned and expressed. For example, the enzyme can be isolated from! Supemative culture of Bacillus stearothermophilus (B. stearothermophilus) TRS40 and purified to homogeneity using sodium dodecyl sulfate / polyacrylamide gel electrophoresis. Another enzyme having a molecular weight of 62,000 was cloned and expressed in Bacillus subtilis. This enzyme is quite thermostable, particularly at an optimum temperature of 60OC to 65SC at pH 6, and about 90% of the enzyme activity is retained. Bacteroides thetaiotaomicron 95-1 (B. thetaiotaomicron 95-1) is another type of enzyme, which is found in the human intestine in high numbers. B. thetaiotaomicron 95-1 can ferment a wide variety of polysaccharides. A pullulanase also suitable for use in the present invention is the new neopululase Y377F, S422V or M375L which originates from Bacillus staerotermophilus as described in JP07177891; is the neopululase of B. subtilisis as described in JP0612681; is the neopululase of Bacillus estearothermophilus TRS (FERM9690), Thermoactinomyces vulgaris, Bacillus stearothermophilus KP1064, Bacteroides thetiataomicron 95-1 and others as described in - JP05316992; is the neopululase type variation described in JP04020291 and the neopululanase described in JP02276578. The neopuluyanase is generally comprised in the detergent composition of the invention in an amount of 0.0001% to 10% by weight, preferably 0.001% to 0.5% by weight. Pullulanase type ll 10 Pullulanase type II enzymes are defined as amylopulianases and randomly hydrolyse the a-, 1-4-bonds in addition to the branch points (a-1 -6 bonds) in polysaccharides and dextrins, unlike pullulanase-type enzymes. I only hydrolyses bonds to, 1-6 in branched polysaccharides. Pullulanase type II can originate from extremophiles, , Especially thermophiles and extreme hyperthermophiles such as those which are isolated from Pyrococcus woesei, P. furiosus, Thermococcus aureus, Thermococcus celer, Desulfurococcus mucosus, Bacteroides thetiaotaomicron, Staphyloterrmus marinus, Purodictium abysii, Bacillus stearothermophilus such as described in "A New Bacterial World "Extromophiles. 1997, 1: 2-13. Another pullulanase suitable for the purpose of the present invention is alkaline puiulanase which exhibits Alkaline α-amylase activity is described in W096 / 35794. Also suitable is alkaline pullulanase Y which has an α-amylase activity as described in EP 418 835, which has an optimum pH on a higher alkaline scale than conventional alkaline puiulanases and exhibits excellent pH stability on a broad scale of pH and strong resistance to almost all detergent ingredients such as surfactants, chelating agents and proteases. A combined pullulanase-amylase enzyme produced by Bacillus subtilis TUAaric is also suitable. Biol. Chem. 51, 9. (1987); Japanese Patent Publication No. 18717/1989). Pullulanase type II is generally comprised in the detergent composition of the invention in an amount of 0.0001% to 10% by weight, preferably 0.001% to 0.5% by weight. Suitable iipase enzymes include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 1,154, as disclosed in British Patent 1, 372,034. Suitable lipases include those that show a positive cross-immunological reaction with the lipase antibody, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trademark Lipase P " Amano ", hereinafter referred to as" Amano-P ". Other suitable commercial lipases include Amano-CES, iipases ex Chromobacter viscosum, e.g., Chromobacter viscosum var. iipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A., and Disoynth Co., The Netherlands, and iipasas ex Pseudomonas gladioli. Especially suitable lipases are iipases such as M1 Lipase ^ and Lipomax® (Gist-Brocades) and Lipolase® and Lipolase Ultra® (Novo) which have been found to be very effective when used in combination with the compositions of the present invention. Also suitable are lipoiitic enzymes which are described in EP 258 068, WO92 / 05249 and WO 95/22615 by Novo Nordisk and in WO94 / 03578, W095 / 35381 and WO96 / 00292 by Unilever. Also suitable are cutinases [EC 3.1.1.50] that can be considered as a special class of lipase, specifically lipases that do not require interfacial activation. The addition of cutinases to detergent compositions have been described in, for example, WO-A-88/09367 (Genencor); WO 90/09446 (Plant Genetic System) and WO 94/14963 and WO 94/14964 (Uniiever). Lipases and / or cutinases are normally incorporated into the detergent composition at levels of 0., 0001% to 2% active enzyme by weight of the detergent composition. Suitable proteases are the subtilisins that are obtained from particular strains of B. subtilis and B. licheniformis (subtilisin BPN and BPN '). Another suitable protease is obtained from a Bacillus strain, which has a maximum activity throughout the pH range of 8-12, developed and marketed as ESPERASE® by Novo Industries A / S of Denmark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1, 243,784 to Novo. Other suitable proteases include ALCALASE®, DURAZYM® and SAVINASE® from Novo and MAXATASE®, MAXACAL®, PROSPERASE® and MAXAPEM® (designed Maxacal protein) from Gist-Brocades. Also suitable for the present invention are proteases which are described in patent applications EP 251 446 and WO 91/06637, BLAP® protease which is described in WO 91/02792 and its variants which are described in WO 95 / 23221. See also a high pH protease from Bacillus sp. NCIMB 40338 which is described in WO 93/18140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are disclosed in WO 92/03529 A to Novo. When desired, a protease having reduced adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter & amp; amp; amp;; Gamble. A recombinant protease similar to trypsin for detergents suitable in the present invention is described in WO 94/25583 to Novo. Other suitable proteases are described in EP 516 200 by Unilever. Proteolytic enzymes also comprise modified bacterial serine proteases, such as those described in European Patent Application Serial No. 87 303761.8, filed on April 28, 1987 (particularly pages 17, 24 and 98), and which is referred to as in the present invention "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine proteolytic enzyme which is referred to in the present invention as "Protease A" . What is referred to in the present invention as "Protease C" is suitable, which is a variant of a Bacillus alkaline serine protease in which lysine replaces arginine in position 27, tyrosine replaces valine in position 104, serine replaces asparagine in position 123, and alanine replaces threonine at position 274. Protease C is described in WO91 / 06637. Genetically modified variants, particularly of Protease C, are also included in the present invention. A preferred protease that is referred to as "Protease D" is a variant of carbonyl hydrolase having an amino acid sequence that is not found in nature, which is derived from a carbonyl hydrolase precursor by substitution of a different amino acid by a plurality of amino acid residues at a position in the aforementioned carbonium hydrolase equivalent to the +76 position, preferably also in combination with one or more positions of amino acid residues equivalent to those that are selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, + '126, +128, +135, +156, +166, +195, +197, +204, + 206, +210, +216, +217, +218, +222, +260, +265, and / or +274 according to the numeration of the subtilisin of Bacillus amyíollquefaciens, as described in WO 95/10591 and in the WO95 / 10592. The "Protease D" variants preferably have the amino acid substitution set 76/103/104, more preferably the substitution set N76D / S103A / V104I. Also suitable is a carbonyl hydrolase variant of the protease described in W095 / 10591, which has an amino acid sequence in the precursor enzyme corresponding to the +210 position in combination with one or more of the following residues: + 33, +62, +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +215, +217, +218, and +222, where the numbered position corresponds to subtilisin that occurs naturally from Bacillus amyloliquefaciens or to equivalent amino acid residues in other hydrolases of carbonyl or subtilisins, such as Bacillus lentus subtilisin (co-pending patent application published under W098 / 55634). More preferred proteases are the multiply substituted protease variants. These protease variants comprise a substitution of an amino acid residue with another amino acid residue occurring naturally at an amino acid residue position corresponding to position 103 of Bacillus amylollquefaciens subtilisin in combination with a substitution of amino acid positions corresponding to positions 1, 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21, 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 102, 102, 104, 106, 107, 109, 111, 114, 116, 117, 119, 121, 123, 126, 128, 130, 131, 133, 134, 137, 140, 141, 142, 146, 147, 158, 159, 160, 166, 167, 170, 173, 174, 177, 181, 182, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206, 209, 210, 2l1, 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 265, 268, 269, 270, 271, 27 2, 274 and 275 of subtilisin Bacillus amyloliquefaciens; wherein the aforementioned protease variant includes a substitution of amino acid residues at the positions corresponding to positions 103 and 76, there is also a substitution of an amino acid residue at one or more amino acid residue positions different from the positions of amino acid residues corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens subtiiysin and / or multiply substituted protease variants comprising a substitution of an amino acid residue with another naturally occurring amino acid residue at one or more amino acid residue positions corresponding to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaciens subtilisin as described in the PCT application publications Nos. PCT / US98 / 22588, PCT / US98 / 22482 and PCT / US98 / 22486 all registered on October 23, 1998, from Procter & Gamble Company. Preferred multiply substituted variants of proteases have the amino acid substitution set 101 ñ 03/104/159/232/236/245/248/252, more preferably 101 G / 103A / 1041/159 / D / 232V / 236H / 245R / 248D / 252K according to the subtilisin numbering of Bacillus amyloliquefaclens subtilisin. Protease enzymes are normally incorporated into the detergent composition at levels of 0.0001% to 2% pure enzyme by weight of the detergent composition. The detergent compositions of the present invention may additionally comprise other enzymes: Cellulases which can be used in the present invention include both bacterial and fungal cellulases. Preferably, they will have an optimum of pH between 5 and 12 and an activity greater than 50 CEVU (Unit of Viscosity of the Cellulase). Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al., J61078384 and WO96 / 02653 disclosing fungal cellulase produced respectively from Humicola insolens, Trichoderma, Thieiavia and -15 Sporotrichum. EP 739 982 describes isolated celuiases of new species of Bacilius. Suitable cellulases are also disclosed in patents GB-A-2.075-028; GB-A-2,095,275; DE-OS-2,247,832 and W095 / 26398. Examples of such cellulases are cellulases produced by a strain of Humicola insolens (Humicola grísea var. Thermoidea), 20 particularly the Humicola strain DSM 1800. Other suitable cellulases are cellulases originating from Humicola insolens having a molecular weight of approximately 50 KDa, an isoelectric point of 5.5 and containing 415 amino acids; and an ~ 43kD endoglucanase derived from Humlcola insolens DSM 1800, which exhibits cellulase activity; a preferred component of endoglucanase has the amino acid sequence that is disclosed in PCT Patent Application No. WO 91/17243. Also suitable are cellulases EGIli from Trochoderma longibrachatum which is described in WO 94/21801, Genencor, published September 29, 1994. Cellulases especially suitable are cellulases which have color care benefits. Examples of such cellulases are the cellulases which are described in European Patent Application No. 91292879.2, registered on November 6, 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A / S) are especially useful. See also .WO 91/17244 and WO91 / 21801. Other cellulases suitable for their fabric care and / or cleaning properties are described in WO96 / 34092, W096 / 17994 and W095 / 24471. The aforementioned cellulases are usually incorporated into the detergent composition at levels of 0.0001% to 2% active enzyme by weight of the detergent composition. Peroxidase enzymes are used in combination with oxygen sources, e.g., percarbonate, perborate, persulfate, hydrogen peroxide, etc. and with a phenolic substrate as a molecule that improves the bleaching action. They are used to "bleach in solution", i.e., to avoid the transfer of dyes or pigments removed from substrates during the washing operations to other substrates in the washing solution. Peroxidase enzymes are known in the art, and include, for example, horseradish peroxidase, ligninase, and haloperoxidase such as chloro- and bromoperoxidase. Peroxidase-containing detergent compositions are disclosed, for example, in PCT International Application WO 89/099813, WO 89/09813 and European Patent Application EP No. 91292882.6, filed on November 6, 1991, and in EP No. 96870013-8, filed February 20, 1996. Iaccase enzyme is also suitable. The improvers are generally included at a level of 0.1% to 5% by weight of the total composition. Preferred builders are substituted phenothiazine and phenoxazine 10-phenothiazinepropionic acid (PPT), 10-eti [phenothiazine-4-carboxylic acid (EPC), 10-phenoxazine-propionic acid (POP) and 10-methylphenoxazine (which is described in WO 94/12621) and substituted 3,5-dimethoxy-4-hydroxybenzoate (substituted C3-C5 alkyl-3,5-dimethoxy-4-hydroxybenzoate) and phenols. Percarbonate or sodium perborate are preferred sources of hydrogen peroxide. The aforementioned peroxidases are normally incorporated into the detergent composition at levels of 0, 0001% to 2% pure enzyme by weight of the detergent composition. The enzymes mentioned above may be of any origin, such as vegetable, animal, bacterial, fungal and yeast origin. The origin can additionally be mesophilic or extremophile (syphilitic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or unpurified forms of these enzymes can be used. Nays, it is common practice to modify wild-type enzymes via protein / genetics engineering techniques in order to maximize their operating efficiency in the detergent compositions of the invention. For example, the variants can be designed so that the compatibility of the enzyme is increased to the commonly found ingredients of such compositions. Alternatively, the variant can be designed so that the optimal pH, bleach or chelating stability, catalytic activity and the like, of the enzyme variant is adjusted to suit the particular cleaning application. In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface changes for surfactant compatibility. The isoelectric point of such enzymes can be modified by replacing some charged amino acids, e.g., an increase in the isoelectric point can help improve compatibility with anionic surfactants. The stability of the enzymes can be further increased by the creation of, for example, salt bridges and reinforcing the metal binding sites to increase the chelating stability. Special attention should be given to cellulases since most cellulases have different binding domains (CBD). Properties of such enzymes can be altered by modifying these domains.

The enzymes can be added as separate individual ingredients (agglomerates, granules, stabilized liquids, etc., containing an enzyme) or as a mixture of two or more enzymes (e.g., cogranulates). Other suitable detergent ingredients that may be added are the enzyme oxidation scavengers described in the co-pending European Patent Application 92870018.6 filed on January 31, 1992. Examples of such enzyme oxidation scavengers are the ethoxylated tetraethylene polyamines. A wide variety of enzymatic materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A to Genencor International, WO 8908694 A to Novo, and U.S. Patent 3,553,139, 5 January 1971, to McCarty et al. Enzymes are further disclosed in U.S. Patent 4,101, 457, Place et al., July 18, 1878 and U.S. Patent 4,507,219, Hughes, March 26, 1985. Enzymatic materials useful for formulas Liquid detergents, and their incorporation into such formulas, are disclosed in U.S. Patent 4,261, 868, Hora et al., April 14, 1981. Enzymes for use in detergents can be stabilized by various techniques. Enzyme stabilization techniques are disclosed and exemplified in U.S. Patent 3,600,319, August 17, 1971, Gedge et al., EP 199,405, and EP 200,586, October 29, 1986, Venegas. Enzyme stabilization systems are also described, for example, in U.S. Patent 3,519,570. A Bacillus, the sp. AC13 which provides proteases, xylanases and cellulases is described in WO 9401532 A to Novo. Bleaching agent A further preferred ingredient of the detergent compositions of the present invention include bleaching agents. Bleaching agents suitable for the purpose of the present invention include hydrogen peroxide, PB1, PB4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components may include one or more oxygen bleaching agents and, depending on the bleaching agent chosen, one or more bleach activators. When present oxygen bleach compounds will typically be present at levels of about 1% to 25%.

The bleaching agent component for use in the present invention can be any of the bleaching agents useful for detergent compositions including oxygen bleaching as well as others known in the art. The bleaching agent suitable for the present invention may be an activated or non-activated bleaching agent. A category of oxygen bleaching agent that can be used comprises percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include magnesium monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloroperbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxydecandioic acid. Such bleaching agents are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446, U.S. Patent Application 0,133,354, and U.S. Patent 4,412,934. Most preferred bleaching agents also include 6-noni! Amino-6-oxoperoxycaproic acid as described in U.S. Patent 4,634,551. Another category of bleaching agents that can be used comprises the halogen bleaching agents. Examples of hypohalite bleaching agents, for example, include trichloro-isocyanuric acid and the sodium and potassium dichloroisocyanurates and N-chloro and N-bromo alkanesulfonamides. Such materials are usually added to 0.5-10% by weight of the finished product, preferably 1-5% by weight. Hydrogen peroxide release agents can be used in combination with bleach activators such as tetraacetylethylene diamine (TAED), nonanoyloxybenzenesulfonate (NOBS, which is described in U.S. Patent 4,412,934). 3,5, -trimethylhexanoioxybenzenesulfonate (ISONOBS, which is described in EP 120,591) or pentaacetylglucose (PAG), or N-nonanoyl-6-aminocaproic acid phenolsulfate ester (NACA-OBS, which is described in WO94 / 28106) , which are perhydrolyzed to form a peracid as the active bleaching species, leading to an improved bleaching effect. Also suitable activators are the acylated citrate esters such as those disclosed in European Patent Application No. 91870207.7 and the non-symmetric acyclic imide bleach activator of the following formula as disclosed in the copending Patent Applications of the United States Serial No. 60 / 022,786 (registered July 30, 1996) and No. 60 / 028,122 (registered October 15, 1996) of Procter &; Gamble: O O RAAR3 wherein R ^ is a C7-C13 straight or branched chain, saturated or unsaturated alkyl group, R2 is a straight or branched, saturated or unsaturated chain CrC8 alkyl group and R3 is a straight or branched chain saturated or branched alkyl group or unsaturated. Useful bleaching agents, including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleach compounds for use in the detergent compositions according to the invention, are disclosed in our copending US Pat. Serial No. 08 / 136,626, PCT. / US95 / 07823, W095 / 27773, WO / 27774 and W095 / 27775.

Hydrogen peroxide may also be present by the addition of an enzymatic system (i.e., an enzyme and a substrate thereof) which is capable of generating hydrogen peroxide at the beginning or during the washing and / or rinsing process. Such enzyme systems are disclosed in Patent Application EP 91202655.6 filed October 9, 1991. Metal-containing catalysts for use in bleaching compositions include cobalt-containing catalysts such as cobalt pentaamine acetate (lll) acetate salts catalysts and catalysts containing manganese such as those described in EPA 549 271; EPA 549 272; U.S. Patent 5,246,621; ia EPA 458 398; U.S. Patent 5,194,416 and U.S. Patent 5,114,611. A bleaching composition comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent is disclosed in patent application No. 94870206.3 Bleaching compounds can be catalyzed by means of a manganese compound. Such compounds are well known in the art and include, for example, manganese-based catalysts which are disclosed in U.S. Patent 5,246,621; U.S. Patent 5,244,594; U.S. Patent 5,194,416; U.S. Patent 5,114,606; and European Patent Application Publication Nos. 549,271 A1, 549,272A1, 544,440A2, and 544,490A1. Preferred examples of these catalysts include Mn | V2 (u-0) 3 (1,4,7-trimethyl-1, 4,7-triaza-cyclononane) 2 (PF6) 2, Mnlll2 (u-0)? (U- OAc) 2 (1, 4,7-trimethyl-1, 4,7-triazacyclo-nonane) 2 (Cl 4) 2, Mn, V 4 (u-0) 6 (1, 4,7-triazacyclo-nonane) - (CI0) 4, Mnl "Mnl 4 (u-0)? (U-OAc) 2 (1, 4,7-trimetyl! -1, 4,7-triazacyclononane) 2 (Cl? 4) 3, Mn v (1, 4,7-trimetyl-1, 4,7-triazacyclononane) - (OCH 3) 3 (PFQ), and mixtures thereof Most preferred to use within are the transition metal bleach catalysts which are complexes of a transition metal and cross-linked macropoiicyclic ligands such as are described in patent applications WO98 / 39405, WO98 / 39406 and WO98 / 39098 by Procter &Gamble.More preferred is the Manganese Complex Bleach Catalyst of the formula [Mn (Bcyclam) CI2] that is illustrated as: "Bcyclam" (5,12-dimethyl-1, 5,8,12-tetraaza-bicyclo [6.6.2] hexadecane). Such a transition metal bleach catlizer can be prepared according to J.Amer.Chem.Soa. (1990), 112, 8604. Bleaching agents other than oxygen bleaching agents are also known in the art and can be used in the present invention. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as zinc and / or aluminum phthalocyanines. These materials can be deposited on the substrate during the washing process. When irradiated with light, in the presence of oxygen, as by the action of hanging clothes to dry in daylight, sulfonated zinc phthalocyanine is activated, and consequently, the substrate is bleached. A preferred zinc phthalocyanine and a photoactivated bleaching process is described in U.S. Patent 4,033,718. Typically, the detergent compositions will contain 0.025% to 1.25%approximately, by weight, of sulfonated zinc phthalocyanine. Advantages of color care and fabric care Technologies that provide a type of color care benefit can also be included. Examples of these technologies are metal catalysts for color maintenance. Such metal catalysts are described in the copending European Patent Application No. 92870181.2. Dye fixing agents, dispersion of polyolefins for anti-wrinkle agents and improved absorbency of! Water, perfume and aminofunctional polymer (PCT / US97 / 16546) for the treatment of color care and substantivity of perfume are additional examples of technologies for color care / fabric care and are described in the copending Patent Application No. 96870140.9, filed November 7, 1996. Fabric softening agents can also be incorporated into the fabric washing detergent compositions according to the present invention. These agents can be of inorganic or organic type. Inorganic softening agents are illustrated by smectitic clays which are disclosed in GB-A-1 400 898 and in U.S. Patent 5,019,292. Softening agents, organic fabrics include insoluble tertiary amines water as disclosed in GB-A1 514 276 and EP-B-0011340 and their combination with quaternary ammonium salts monkey C12-C14 is disclosed in EP-B -0 026 527 and EP-B-0 026 528 and di-long chain amides are disclosed in EP-B-0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials. as disclosed in EP-A-0 299 575 and EP-A-0 313 146. Smectite clay levels are usually in the range from 2% to 20%, more preferably from 5% to 15%, in weight, the material being added as a dry mixed component to the rest of the formulation. Organic fabric softening agents such as water insoluble tertiary amines or dilarga chain amide materials are incorporated at levels from 0.5% to 5% by weight, usually from 1% to 3% by weight, while the materials of high molecular weight polyethylene oxide and water soluble cationic materials are added at levels of 0.1% to 2%, usually 0.15% to 1.5% by weight. These materials are usually added to spray-dried portions of the composition, although in some cases it may be more convenient to add them as a dry mixed particulate material, or by spraying them as molten liquid over other solid components of the composition. Improving System The compositions according to the present invention may additionally comprise a builder system. Any builder system conventional detergency is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates, alkylsuccinic or alkenylsuccinic acid and fatty acids, materials such as ethylenediamine tetraacetate, pentametilenacetato of dietiientriamina, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediaminetetramethylene phosphonic acid and triaminepentamethylene phosphonic acid. Phosphate builders can also be used in the present invention.

Suitable detergency builders may be an inorganic ion exchange material, commonly a hydrated aluminosilicate material, more particularly a synthetic hydrated zeolite such as hydrated zeolite A, X, B, HS or MAP. Another suitable inorganic builder material is layered silicate, e.g., SKS-6 (Hoechst). SKS-6 is a layered crystalline silicate consisting of sodium silicate (Na2Si2? 5). Suitable polycarboxylates containing a carboxy group include lactic acid, glycolic acid and ether derivatives thereof as disclosed in Belgian Patents Nos. 831, 368, 821, 369 and 821, 370. Polycarboxylates Those containing two carboxy groups include the soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, malonic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in US Pat. German Offenlegenschrift 2,446,686 and 2,446,687, and in U.S. Patent No. 3,935,257 and the sulfinyl carboxylates described in Belgian Patent No. 840,623. Polycarboxylates that contain -15 three carboxy groups include, in particular, citrates, aconitrates and water-soluble citraconitrates, as well as also succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1, 379,241, Lactoxysuccinates which are described in the Application the Netherlands 7205873, and oxopolycarboxylate materials such as 2-oxa-1, 1, 3-propane tricarboxylates which are described in 20 British Patent No. 1, 387,447. Polycarboxylates containing four carboxy groups include the oxydisuccinates which are disclosed in British Patent No. 1, 261, 829, 1,1, 2,2-ethane-tetracarboxylates, 1,1, 3,3-propane-tetracarboxylates and 1, 1, 2,3-propane tetracarboxylates. Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives which are disclosed in British Patents Nos. 1, 398, 441 and 1,398, 422 and in US Pat. No. 3,936,448, and the sulfonated pyrolysed citrates which are described in British Patent No. 1. , 082,179 while polycarboxylates containing phosphon substituents are disclosed in British Patent No. 1, 439,000. Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis, cis, cis-tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5- 10 tetrahydrofuran-cis-cis-cis-tetracarboxylates, 2,5-tetrahydrofuran-cis-dicarboxylates, 2,2 , 5,5-tetrahydrofuranstra carboxylates, 1, 2,3,4,5,6-hexanohexacarboxylates and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include mellitic acid, pyromellitic acid and the italic acid derivatives disclosed in British Patent No. 1, 425, 433. Of the above, preferred polycarboxylates are hydroxy-15-carboxylates containing up to three carboxy groups per molecule, more particularly citrates. Preferred builders system for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder agent such as zeolite A or a layered silicate (SKS-6), and a soluble carboxylate chelating agent.

Water such as citric acid. Preferred builder systems include a mixture of a water-insoluble aluminosilicate builder agent such as zeolite A or a layered silicate (SKS-6), and a water-soluble carboxylate chelating agent such as citric acid. Other preferred builder systems include a mixture of a water insoluble aluminosilicate builder such as zeoite A, and a water soluble carboxylate chelating agent such as citric acid. Preferred builder systems for use in liquid detergent compositions of the present invention are soaps and polycarboxylates. Other builder materials that can be part of the builder system for use in granular compositions include inorganic materials such as carbonates, bicarbonates, alkali metal silicates, and organic materials such as organic phosphonates, aminopolyalkylene phosphonates and aminopolycarboxyiates. Other suitable water-soluble organic salts are the homo- or polypolymer acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from one another by not more than two carbon atoms. Polymers of this type are disclosed in GB-A-1, 596,756. Examples of such salts are polyacrylates of molecular weight of 2000-5000 and their copolymers with maleic anhydride, such copolymers have a molecular weight of 20,000 to 70,000, especially about 40,000. Builder salts are usually included in amounts of 5% to 80% by weight of the composition, preferably 10% to 70% and more usually 30% to 60% by weight. Chelating Agents The detergent compositions in the present invention also they may optionally contain one or more iron and / or manganese chelating agents. Such chelating agents can be selected from the group consisting of amino carboxylates, amino phosphonates, polyfunctionally substituted aromatic chelating agents and mixtures thereof, all as defined below in the present invention. Without the purpose of being limited by theory, it is believed that the advantage of these materials is due in part to their exceptional ability to remove iron and manganese ions from wash solutions by the formation of soluble chelates. Amino carboxylates useful as optional chelating agents include ethylenediaminetetraacetates, N-hydroxyethylethiaminetriacetates, nitrilotriacetates, ethylenediaminetetrapropionates, triethylenetetraamine hexaacetates, diethienthiaminepentaacetate, ethylenediamine disuccinates and ethanoldiglicines, the alkali metal, ammonium and substituted ammonium salts thereof and mixtures thereof. Amino phosphonates are also suitable for use as chelating agents in the compositions of the invention when at least low levels of total phosphorus are allowed in the detergent compositions, and include ethylene diamine tetrakis (methyl enf osphonates) as DEQUEST. Preferably, these amino phosphonates do not contain alkyl or alkenium groups with more than about 6 carbon atoms. Polyfunctionally substituted aromatic chelating agents are also useful in the compositions in the present invention. See United States Patent 3,812,044, issued May 21, 1974, to Connor et al. Preferred compounds of this type in acid form are dihydroxydisulfobenzenes such as 1,2-dihydroxy-3,5-disulfobenzene.

A preferred biodegradable chelating agent for use in the present invention is ethylenediamine disuccinate ("EDDS"), especially the [S, S] isomer as described in U.S. Patent 4,704,233, November 3, 1987, to Hartman and Perkins. The compositions in the present invention may also contain salts of methyl glycindiacetic acid (MGDA) (or the acid form) as a chelating agent or a useful creamer with, for example, insoluble improvers such as zeolites, layered silicates and the like. If used, these chelating agents generally 10 will comprise from about 0.1% to about 15% by weight of the detergent compositions in the present invention. More preferably, the chelating agents will comprise from about 0.1% to about 3.0% by weight of such compositions. Foam suppressing agent Another optional ingredient is a foam suppressing agent, exemplified by silicones, and silica-silicone blends. Silicones -15 can generally be represented by alkylated polysiloxane materials while silica is normally used in finely divided form exemplified by aerogels and silica zerogels and hydrophobic silicas of various types. These materials can be incorporated as particles wherein the suds suppressor agent is advantageously incorporated so that it can be released in a vehicle 20 substantially impermeable without detergent surfactant soluble in water or dispersible in water. Alternatively, the foam suppressing agent can be dissolved or dispersed in a liquid vehicle and applied by spraying on one or more of the other components.

A preferred silicone foam controlling agent is disclosed in Bartollota et al., U.S. Patent 3,933,672. Other particularly useful suds suppressors are the self-emulsifying silicone foam suppressors, which are described in German Patent Application DTOS 2 646 126, published on April 28, 1977. An example of such a compound is DC-544, which is commercially available from Dow Corning, which is a siloxane-glycol copolymer. Especially preferred foam controlling agents are the foam suppressant agent systems comprising a mixture of silicone oils and 2-alkylalkanols. Suitable 2-alkylalkanols are 2-butyloctanol which is commercially available under the. Isofol 12® trademark. Such a foam suppressant agent system is disclosed in European Patent Application Co-pending No. 92970174.7, filed on November 10, 1992. Especially preferred silicone foam controlling agents are disclosed in European Patent Application Co-pending No. 92201649.8. The aforementioned compositions may further comprise a mixture of silicone / silica in combination with fumed non-porous silica such as Aerosil®. The suds suppressors described above are normally employed at levels of 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight. Other Other components that are used in detergent compositions may be employed, such as soil suspending agents, soil release agents, optical brighteners, abrasives, bactericides, stain inhibitors, coloring agents, and / or encapsulated or non-encapsulated perfumes. Especially suitable encapsulation materials are water-soluble capsules consisting of a polysaccharide matrix and polyhydroxy compounds as described in GB 1, 464,616. Other suitable water-soluble encapsulation materials comprise dextrins which are derived from non-gelatinized starch acid esters of substituted dicarboxylic acids such as are described in U.S. Patent 3,455,838. These ester-acid dextrins are prepared, preferably, from starches such as waxy corn, waxy sorghum, sago, tapioca and potato. Suitable examples of the aforementioned encapsulation materials include N-Lok manufactured by National Starch. Matter! N-Lok encapsulation consists of modified corn starch and glucose. The starch is modified by the addition of substituted monofunctional groups such as octenisuccinic acid anhydride. Anti-redeposition and slurry agents suitable for use in the present invention include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or copolymeric polycarboxylic acids or their salts. Polymers of this type include the aforementioned polyacrylates and co-polymers of maleic anhydride-acrylic acid as builders, as well as copolymers of maleic anhydride with ethylene, methylvinylether or methacrylic acid, maleic anhydride constituting at least 20 mole percent of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, more preferably from 0.75% to 8%, more preferably from 1% to 6% by weight of the composition.

Preferred optical brighteners are anionic in nature, examples of which are 4,4-disodium-4-bis- (2-diethanolamino-4-aniiino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate; Disodium 4,4'-bis- (2-morpholino-4-anilino-s-triazin-6-ylamino) -salbene-2,2'-disulfonate; Disodium 4,4'-bis- (2-4-dianiiino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate; 4,4'-bis- (2,4-dianilino-s-triazin-6-ylamino) stilbene-2-sulfonate monosodium; 4,4'-bis- (2-anilino-s-triazin-4- ( N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene-2,2'-disulfonate disodium; 4,4'-bis- (4-phenyl-2,1,3-triazole-2-) il) -stilbene-2,2'-disodium disulfonate; 4,4'-bis- (2-ani-amino-4- (1-methyl-2-hydroxyethylamino) -s- triazin-6-ylamino) stilbene-2,2 ' disodium disulfonate; 2 (sti-bilo-4"- (naphtho-1,, 2,: 4,5) -1, 2,3-triazole-2" sodium sulfonate and 4,4-bis (2-sulphotyryl) biphenyl Very preferred brighteners are the specific brighteners disclosed in EP 753 567. Other useful polymeric materials are polyethylene glycols, particularly those of molecular weight 1000-1000 O, more particularly 2000 to 8000 and more preferably even about 4000. These are used for levels from 0.20% to 5%, more preferably from 0.25% to 2.5% by weight These polymers and the aforementioned homo- or copolymeric polycarboxylate salts are valuable to me. to maintain the whiteness, the sedimentation of the ash from the fabric, and the cleaning performance in dirty clays, proteinaceous and oxidizable in the presence of impurities of transition metals. Dirt release agents useful in the compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and / or propylene glycol units in various configurations. Examples of such polymers are disclosed in those commonly assigned U.S. Patent Nos. 4,116,885 and 4,71 1, 730, and in Published European Patent Application No. 0 272 033. A particularly preferred polymer according to EP-A 0272 033 has the formula: CH3 (PEG) 43) ?, 75 (POH) 0j25CT-PO) 2,8-s-PEG) or (4 ^ PO- H) ?, 25 ((PEG) 43CH3) 0) 75 where PEG is - (OC2H4) 0-, PO is (OC3H6O) and T is (PCOC6H4CO). Modified polyesters such as the random copolymers of dimethylterephthalate, dimethylsulfoisophthalate, ethylene glycol and 1-2-propanediol, end groups consisting mainly of sulfobenzoate and secondarily of monoesters of ethylene glycol and / or propanediol are also very useful. The aim is to obtain a polymer capped at both ends by sulfobenzoate groups, "mainly", in the present context most of the above mentioned copolymers in the present invention will be capped at the ends by sulfobenzoate groups. However, some copolymers will be less capped at the ends, and therefore their end groups may consist of monoesters of ethylene glycol and / or 1 -2-propanediol, therefore they consist "secondarily" of such species. The polyesters selected in the present invention contain 46% > approximately by weight of dimethylterephthalic acid, approximately 16% by weight of 1,2-propanediol, approximately 10% by weight of ethylene glycol, approximately 13% by weight of dimethylsulfo-benzoic acid, and approximately 15% by weight of sulfoisophthalic acid; molecular weight of approximately 3,000. Polyesters and their methods of preparation are described in detail in EPA 311 342.

It is well known in the art that free chlorine in the tap water rapidly deactivates the enzymes comprised in the detergent compositions. Therefore, the use of a chlorine scrubber such as perborate, ammonium sulfate, sodium sulfite, polyethylene imine at a level greater than 0.1% by weight of the total composition, in the formulas will provide improved stability throughout the washing of the detergent enzymes. Compositions comprising chlorine scrubbers are described in European Patent Application 92870018.6, registered on January 31, 1992. Aryoxylated polycarboxylates such as those prepared from polyacrylates are useful in the present invention to provide additional fat removal performance. Such materials are described in WO 91/08281 and PCT 90/01815 on page 4 and following, which is incorporated herein by reference. Chemically, these materials comprise polyacrylates having an ethoxy side chain for every 7-8 acrylate units. The side chains are of the formula - (CH2CH20) m (CH2) pCH3 where m is 2-3 and n is 6-12. The side chains are bonded from ester to the polyacrylate "backbone" to provide a "comb" type polymer structure. The molecular weight may vary, but typically it is on the scale of 2000 to 50,000, approximately. Such alkoxylated polycarboxylates may comprise from about 0.05% to about 10%, by weight, of the compositions in the present invention. Dispersants The detergent composition of the present invention may also contain dispersants: Suitable organic water-soluble salts are homo- or copolymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by no more than two carbon atoms. Polymers of this type are disclosed in GB-A-1, 596,756. Examples of such salts are polyacrylates of molecular weight of 2000-5000 and their copolymers with maleic anhydride, such copolymers have a molecular weight of 1,000 to 100,000. Especially, acrylate and methylacrylate copolymers such as 480N having a molecular weight of 4000, at a level of 0.5-20% by weight of the composition can be added in the detergent compositions of the present invention. The compositions of the invention may contain a compound 10 lime soap peptizer, having a lye soap dispersing power (LSDP), as defined below in the present invention not greater than 8, preferably not greater than 7, more preferably not greater than 6. The peptizing compound of lime soap is preferably present at a level of 0% to 20% by weight. A numerical measure of the effectiveness of the lime soap peptizing agent is provided by the dispersing power of lime soap -15 (LSDP), which is determined using the lime soap dispersion test as described in an article by H.C. Borghetty and C.A. Bergman, J ,, Am. Oil. Chem. Soc. Volume 27, pages 88-90, (1950). This lime soap dispersion test method is widely used by practitioners of this technique, and is mentioned in, for example, the following articles; W.N. Linfield, Surfactant Science Series, volume 7, 20 page 3; W.N. Linfield, Tenside Surf. Det. volume 27, pages 159-163, (1990); and M.K. Nagarajan, W.F. Masler, Cosmetics and Toiletries. volume 104, pages 71-73, (1989). The LSDP is the weight ratio of the dispersing agent to sodium oleate that is required to disperse the lime soap deposits formed by 0.025 g of sodium oleate in 30 ml of water of 333 ppm CaCo3 (Ca: Mg = 3: 2) of hardness equivalence. Surfactants having good pepetizing lime soap capacity will include certain amine oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated alcohols. Exemplary surfactants having an LSDP of not greater than 8 for use according to the present invention include dimethylamine oxide C? D-Cf8, C12-C-? S alkyl ethoxysulfates with an average degree of ethoxylation of 1-5, particularly ethoxysulfate surfactant of C-12-C15 alkyl with an ethoxylation degree of 3 (LSDP = 4), and ethoxylated C1-C15 alcohols with an ethoxylation degree of 12 (LSDP = 6) or 30, marketed under the trademarks Lutensol A012 and Lutensol A030 respectively, by BASF GmbH. Polymeric lime soap polymerizing agents suitable for use in the present invention are described in the article by M.K. Nagarajan, W.F. Masler, which can be found in Cosmetics and Toiletries. volume 104, pages 71 -73, (1989). They can also be used as hydrophobic lime soap peptizing bleaching compounds such as 4- [N-octanoyl-6-aminohexanoyl] benzene sulfonate, 4- [N-nonanoyl-6-aminohexane-yl] benzene sulfonate, sulfonate 4 - [N-decanoyl-6-aminohexanoyl] benzene and mixtures thereof; and nonanoyloxybenzene sulfonate together with hydrophilic / hydrophobic bleach formulations. Inhibition of dye transfer The detergent compositions of the present invention may also include compounds to inhibit dye transfer from one fabric to another of the solubilized or suspended dyes encountered during fabric washing operations comprising dyed fabrics. Polymeric agents inhibitors of dye transfer The detergent compositions according to the present invention also comprise from 0.001% to 10%, preferably from 0.01% to 2%, more preferably from 0.05% to 1% by weight of polymeric inhibitory agents of the transfer of the colorant. Such polymeric dye transfer inhibiting agents are normally incorporated in the detergent compositions in order to inhibit the transfer of the dyes from the dyed fabrics to fabrics washed therewith. These polymers have the ability to complex or adsorb fugitive dyes that are washed out of the dyed fabrics before the dyes have the opportunity to bind to other articles in the wash. Especially suitable dye transfer inhibiting polymeric agents are polyamine N-oxide polymers, copolymers of N-viny pyrrolidone and N-vinyiimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. The addition of such polymers also increases the functioning of the enzymes according to the invention, a) Polyamine N-oxide polymers The aforementioned polyamine N-oxide polymers contain units having the following structural formula: © R wherein P is a polymerizable unit, to which the group R-N-0 can be attached or wherein the group R-N-0 forms part of the polymerizable unit or a combination of both. 0 0 0 A is NC, CO, C, -0-, -S-, -N-; x is 0 or 1; R are aliphatic, aliphatic, ethoxylated, aromatic, heterocyclic or alicyclic groups or any combination thereof to which the nitrogen of the N-O group can be attached or where the nitrogen of the N-O group is part of these groups. The group can NOT be represented by means of the following general structures: o O (R1) x - N - (R2) and N- (R1) x (R3) z wherein R1, R2, and R3 are alicyclic, aromatic groups , or heterocyclic or alicyclic groups or combinations of these, xo / yyy / oz is 0 or 1 and where the nitrogen of the NO group can be fixed or where the nitrogen of the NO group forms part of these groups. The N-O group can be part of the polymerization unit (P) or it can be attached to the polyimic backbone or a combination of both.

Suitable polyamine N-oxides wherein the N-O group forms part of the polymerizable unit comprises polyamine N-oxides wherein R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups. A class of the aforementioned polyamine N-oxides comprises the group of polyamine N-oxides wherein the nitrogen of the group NO is part of the group R. The preferred N-oxides of poiiamine are those in which R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof. Another class of polyamine N-oxides comprises the group of polyamine N-oxides wherein the nitrogen of the N-O group is attached to the group R. Other suitable polyamine N-oxides are the polyamine oxides to which the N-O group is attached to the polymerizable unit. A preferred class of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group wherein the nitrogen of the functional group is NOT part of the R group before mentioned. Examples of these classes are polyamine oxides wherein R is a heterocyclic compound such as pyrridine, pyrrole, imidazole and derivatives thereof. Another preferred class of N-oxides of polyamine are the polyamine oxides having the general formula (I) wherein R are aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the functional group N-O is attached to the aforementioned R groups. Examples of these classes are polyamine oxides wherein the R groups can be aromatic such as phenyl.

Any polymer backbones can be used provided that the amine oxide polymer formed is soluble in water and has the inhibitory properties of dye transfer. Examples of suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates and mixtures thereof. The amine N-oxide polymers of the present invention typically have a ratio of amine to amine N-oxide from 10: 1 to 1: 1000000. However, the amount of amine oxide groups that are present in the polyamine oxide polymer can be varied by appropriate copolymerization or by the appropriate degree of N-oxidation. Preferably, the ratio of amine to amine N-oxide is from 2: 3 to 1: 1000000. More preferably from 1: 4 to 1: 1000000, more preferably still from 1: 7 to 1: 1000000. The polymers of the present invention actually comprise random or block copolymers where one type of monomer is an amine N-oxide and the other type of monomer is or is not an amine N-oxide. The amine oxide unit of the poiiamine N-oxides has a pKa < 10, preferably pKa < 7, more preferably pKa < 6. Polyamine oxides can be obtained in almost any degree of polymerization. The degree of polymerization is not critical as long as the material has water solubility and the desired dye suspension power. Typically, the average molecular weight is within the range of 500 to 1,000,000; preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000, more preferably even from 3,000 to 20. 000. b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole The copolymers of N-vinylpyrrolidone and N-vinylimidazole used in the present invention have an average molecular weight scale of 5,000-1,000,000, preferably 20,000-200,000. Most preferred polymers for use in detergent compositions according to the present invention comprise a polymer that is selected from copolymers of N-vinylpyrrolidone and N-vinylimidazole wherein the aforementioned polymer has a molecular weight scale 10 average of 5,000 to 50,000, preferably of 8,000 to 30,000, more preferably 10,000 to 20,000. The average molecular weight scale was determined by light diffusion as described in Barth H.G. and Mays J.W. Chemical Analvsis. Vol. 113, "Modern Methods of Characterization of Polymers". Copolymers of N-vinylpyrrolidone and N-vinylimidazo! most preferred have an average molecular weight scale of 5,000 to 50,000; plus -15 preferably from 8,000 to 30,000; more preferably still from 10,000 to 20,000. The copolymers of N-vinylpyrrolidone and N-vinylimidazole which are characterized by having the aforementioned average molecular weight scale provide excellent dye transfer inhibiting properties while not adversely affecting the 20 cleaning operation of the detergent compositions that are formulated therewith. The copolymers of N-vinylpyrrolidone and N-vinyiimidazole useful in the present invention have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, more preferably from 0.8 to 0.3, more preferably still from 0. , 6 to 0.4. c) Poivinylpyrrolidone The detergent compositions of the present invention can also use polyvinylpyrrolidones ("PVP") having an average molecular weight of 2,500 to 400,000, preferably 5,000 to 200,000, more preferably about 5,000 to 50,000, and more preferably still of 5,000 to 15,000. Suitable polyvinyl pyrrolidones are commercially available from ISP Corporation, New York, NY and Montreal, Canada, under the product names PVP K-15 (average molecular weight 10,000), PVP K-30 (average molecular weight 40.O00), PVP K-60 (average molecular weight of 160,000), and PVP K-90 (average molecular weight of 360,000). Other suitable polyvinyl pyrrolidones which are commercially available from BASF Corporation include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones which are known to persons with experience in the field of detergents (see, for example, EP-A-262,897 and EP-A-256,696). d) Polyvinyloxazolidone The detergent compositions of the present invention can also use polyvinyloxazolidones as a dye transfer inhibiting agent. The aforementioned polyvinyloxazolidones have an average molecular weight of about 2,500 to 400,000, preferably about 5,000 to about 200,000, more preferably about 5,000 to 50,000, and more preferably even about 5,000 to about 15,000. e) Polyvinylimidazole The detergent compositions of the present invention can also use polvinimidazoles. The aforementioned polyvinylimidazoles have an average molecular weight of about 2,500 to 400,000, preferably about 5,000 to 200,000, more preferably about 5,000 to 50,000, and more preferably even about 5,000 to about 15,000. F) Crosslinked Polymers Crosslinked polymers are polymers whose main chains are interconnected to a certain degree; These links can be of a chemical or physical nature, possibly with active groups in the main chain or branches; cross-linked polymers have been described in the Journal of Polvmer Science. Volume 22, pages 1035-1039. Washing Method The compositions of the invention can be used essentially in any washing or cleaning methods, including soaking methods, pretreatment methods and methods with rinse steps for which a separate rinse aid composition can be added. The process described in the present invention comprises the action of contacting fabrics, tableware or any other hard surface with a cleaning solution in the usual manner and which is exemplified below. A conventional method of washing clothes comprises treating soiled fabrics with an aqueous liquid having dissolved or dispersed within an effective amount of the laundry detergent composition and / or for the care of the fabric. A preferred automatic dishwashing method comprises treating the soiled articles with an aqueous liquid having dissolved or dispersed within an effective amount of the washing or rinsing composition in an automatic washing machine. A conventional effective amount of the machine dishwashing composition means 8-60 g of the product dissolved or dispersed in a wash volume of 3-10 liters. According to a method of washing dishes by hand, dirty dishes are contacted with an effective amount of the dishwashing composition, typically 0.5-20g (per 25 dishes being treated). Preferred hand dish washing methods include the application of a concentrated solution to the surfaces of the dishes or soaking in a large volume of diluted solution of the detergent composition. A conventional method of cleaning hard surfaces comprises treating dirty hard articles with for example a sponge, brush, cloth, etc. with an aqueous liquid having dissolved or dispersed within an effective amount of the hard surface cleaner and / or such undiluted composition. It also comprises soaking in a concentrated solution or in a large volume of the diluted solution of the detergent composition. The process of the invention is conveniently carried out in the course of the cleaning process. The method of cleaning preferably is carried out at 5dC to 95dC, especially between 10dC and 60SC. The pH of the treatment solution is preferably from 7 to 12. The following examples are for the purpose of exemplifying compositions of the present invention, but are not necessarily intended to limit or otherwise define the scope of the invention. In detergent compositions, the enzyme levels are expressed by the pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total compositions. The abbreviated identifications of the components have the following meanings: Sodium alkylbenzene sulfonate linear C11-13 TAS Sodium alkyl sulphate CX? AS Sodium alkyl sulfate C-j? - Ci? CxySAS C- | X-C? And secondary alkyl sodium sulphate (2,3). O ?? Ez Predominantly linear primary alcohol C ?? - C1? condensed with an average of z moles of ethylene oxide. CXYEZS Sodium alkyl sulphate C? - C? Y condensed with an average of z moles of ethylene oxide. CxEOy Alcohol Cy with an average ethoxylation of y. Nonionic Mixed ethoxylated / propoxylated fatty alcohol, for example Plurafac LF404 which has an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5. QAS Ra- N + (CH3) 2 (C2H4OH) with R2 = C12-C. QAS 1 R2- N + (CH3) 2 (C2H4OH) with R2 = C8-Cn. SADS C14-22 sodium alkyl disulfate of the formula 2- (R) -C4H7-1, 4- (S04) -2 where R = C10-18. MABS Intermediate Branched C12-18 alkyl sulfate surfactant with an average branching of 1.5 methyl or ethyl branching groups MES x-Sulfonyl ester of C18 fatty acid APA Amidopropyl dimethylamine C8-? 0. Sodium alkylcarboxylate soap lineo derived from an 80/20 mixture of tallow and coconut fatty acids. STS Sodium toluene sulfonate. TFAA Alkyl N-methylglucamide C-j6-Cl8. TPKFA Fatty acids of whole cut plugged C12- C14. DEQA Di- (tallowoxyethyl) dimethyl ammonium chloride. DEQA (2) Di- (tallowyloxy-ethyl-soft) methylisulfate - hydroxyethylmethylammonium. SDASA 1: 2 ratio of stearyldimethylamine: triple-pressed stearic acid DTMAMS 1: 2 ratio of stearyldimethylamine: triple-pressed stearic acid. Silicato Silicato Sodium Amorphous (Si? 2: Na2? Ratio = 1, 6-3.2) Metasilicate Sodium metasilicate (Si? 2: Na2? Ratio = 1.0) Zeoite A Sodium aluminosilicate Hydrate of the formula Na12 (AI02- Si02 ) 12-27H20 having a main particle size on the scale of 0.1 to 10 micrometers (weight expressed on anhydride basis). SKS-6 Layered crystalline silicate of the formula dNa2Si2? 5. * 5 Trisodium Citrate Citrate dihydrate activity 86.4% with a particle size distribution between 425 and 850 micrometers. Citrus citric acid anhydride. Carbonate Sodium Carbonate Anhydride with a particle size between 200 and 900 micrometers. 10 Bicarbonate Sodium bicarbonate anhydride with a particle size between 400 and 1200 micrometers. Sulphate Sodium sulphate anhydride. Sulfate Mg Magnesium anhydride sulfate. STPP Sodium tripolyphosphate TSPP Tetrasodium pyrophosphate. 5 MA / AA Copolymer of 1: 4 maleic acid / aerypic acid with average molecular weight of 70,000-80,000 approximately MA / AA 1 1: 4 random copolymer maleic acid / acrylic acid with average molecular weight of about 10,000 AA Polyacrylate polymer sodium with an average molecular weight of 4,500.

Polycarboxylate Copolymer comprising a mixture of carboxylated monomers such as acrylate, maleate and methylacrylate with a molecular weight ranging from 2,000-8O.00O, as commercially available from BASF, being a copolymer of acrylic acid of molecular weight 4,500. Bentonite clay or srnectite clay. PA1 Perborate sodium anhydride monohydrate of the nominal formula NaB02-H202. PA4 Sodium perborate tetrahydrate of the nominal formula NaB02- 3H20-H202. Percarbonate Sodium percarbonate anhydride of the nominal formula 2Na2C? 3 - 3H2O2 NaDCC Sodium dichloroisocyanurate. TAED Tetraacetylethylenediamine. NOBS Nonanoyloxybenzene sulfonate in the form of the sodium salt. NACA-OBS Sulfonate (6-nonamidocaproyl) -oxybenzene. LOBS Dodecanoyloxybenzene sulfonate in the form of the sodium salt. DOBA Dodecanoylbenzoic acid. DTPA Diethylenetriaminepentaacetic acid. HEDP 1, 1-hydroxyethanedifosphonic acid.

DETPMP Diethylenetriaminepenta (methylene) phosphonate, sold by Monsanto under the trademark Dequest 2060. EDDS Ethylenediamine-N, N-disuccinic acid, isomer (S, S) in the form of its sodium salt. MnTACN 1, 4,7-trimethyl-1, 4,7-triazacyclononane manganese. Photoactivated bleach Sulfonated zinc phthalocyanine encapsulated in soluble dextrin polymer. 10 PAAC Cobalt pentaamine acetate salt (lll). Paraffin Paraffin oil marketed under the trademark Winog 70 by Wintershall. NaBz Benzoate sodium. Protease Proteolytic Enzyme marketed under the trademark Savinase, Alcalase, by Í5 Novo Nordisk A / S, the "protease D" variant with the substitution set N76D / S103A / 104I and the protease described in PCT applications Nos. PCT / US98 / 22588, PCT / US98 / 22482 and PCT / US98 / 22486 with the set of 0 amino acid substitution 101 G / 103A / 1041 / 159D / 232V / 236H / 245R / 24 8D / 252K.4 Amylase Amylolytic enzyme marketed under the trademark Termamyl® and Duramyl® available from Novo Nordisk A / S and those variants having improved thermal stability with amino acid deletions R181 * + G182 * or T183 * + G184 * as described in WO 95/35382. Lipase Lipoic enzyme sold under the trademark Lipolase, Lipolase Ultra by Novo Nordisk A / S and Lipomax by Gist-Brocades. Ra / Ga-AMG Amyloglucosidase from Rhizopus niveaus marketed by Amano under the trademark Gluczyme. Ra / Ga-Amylase Alpha-amylase from Lipomyces konomenkoae of LKA1 gene. Cellulose Enzyme cellulose marketed under the trademark Carezyme, Celluzyme and / or Endolase by Novo Nordisk A / S. CMC Carboxymethylcellulose sodium. PVNO Poly (4-vinylpyridine) -N-Oxide PVPVI Poii (4-vinylpyridine) -N-Oxide / copolymer of vinylimidazole and vinylpyrrolidone. Brightener 1 4,4-bis (4-2-sulphotyryl) biphenyl disodium Brightener 2 4,4'-bis (4-anilino-6-morpholino-1, 3,5-triazin-2-H) styrene-2,2 Disodium disulfonate.

Polisher 3 4,4'-bis (4,6-dianilino-1,3,5-triazin-2-yl) disodium amino stilbene-2,2'-disulphonate Silicone foam agent Polydimethylsiloxane foam controller with siloxane copolymer -oxyalkylene as a dispersing agent with a ratio of the above-mentioned foam controlling agent to the aforementioned dispersing agent of 10: 1 to 100: 1. Suppressor of foam 12% Silicone / silica, 18% stearyl alcohol, 70% starch in granulated form. Thickener High molecular weight crosslinked polyacrylates such as Carbopol offered by B.F. Goodrich Chemical Company and Polygel. SRP 1 Polyesters ammonically capped end. SRP 2 Dirty Release Polymer selected from 1) non-cotton dirty release polymer according to U.S. Patent 5,415,807, Gosseiink, Pan, Kellett and Hall, issued May 16, 1995 and / or 2) non-cotton dirty release polymer according to U.S. Patent Application Serial No. 60/051517.

QEA: bis (C2H5?) (C2H4?) N (CH3) -N + -CβH12-N + - (CH3) bis (C2H50) - (C2H40n) n. wherein N = 20 to 30. PEI: Polyethyleneimine with an average molecular weight of 600-1800 and an average degree of ethoxylation of 7-20 ethyleneoxy residues per nitrogen. SCS: Sodium cumene sulfonate. HMWPEO: High molecular weight polyethylene oxide.

PEG X: Polyethylene glycol, with a molecular weight of x.

PEO: "Polyethylene oxide, with an average molecular weight of 5,000. TEPAE: Tetraethylene-pentaaminethoxylate BTA: Benzotriazole pH: Measured as a 1% solution in distilled water at 20SC Example 1 The following granular washing detergent compositions were prepared. clothes according to the present invention: I II III IV V Granules Dried by Spraying LAS 10,0 10,0 15,0 5,0 5,0 TAS - LO ¬ MBAS - - - 5.0 2.0 C45AS - - 1, 0 - 2.0 OtóAEgS - - - 1, 0 - QAS - - 1,0 1,0 - DTPA, HEDP and / or EDDS 0.3 0.3 0.5 0.3 • - Sulphate Mg 0.5 0.5 0.1 - - Citrate - - - 3.0 5.0 Carbonate 10.0 7.0.0.0.0 - - Sulphate 5.0 5.0 - - 5.0 Silicate - - - - 2,0 Zeolite A 16.0 18.0 20.0 20.0 - SKS-6 - - - 3.0 5.0 0 MA / AA or AA 1.0, 2.0 11, 0 - - PEG 4000 - 2.0 . - 1.0 - QEA 1, 0 - - - 1, 0 Rinse aid 1 or 2 or 3 0.05 0.05 0.05 - 0.05 Silicone Oil 0,01 0,01 0,01 - - Aalomerado Carbonato - - - - 4,0 -5 SKS-6 6,0 - - - 6,0 LAS 4.0 5,0 - - 5,0 Components in Particles Added in Dry Maleic Acid / Carbonate / 8.0 10.0 10.0 4.0 - Bicarbonate (40:20:40) 0 QEA - - - 0.2 0.5 NACA-OBS 3.0 - - 4,5 - NOBS 1, 0 3,0 3,0 - - TAED 2,5 - - 1,5 2,5 MBAS - -. - 8,0 - LAS (flakes) 10,0 10,0 - - - Added oor Spray Rinse aid 1 or 2 or 3 0.2 0.2 0.3 0.1 0.2 Perfume 1, 0 0.5 1, 1 0.8 0.3 Added in Dry Citrate - - 20.0 4.0 - Percarbonate 15,0 3.0 6.0 10.0 - Perborate - - - - 6.0 Photo-activated bleach 0.02 0.02 0.02 0.1 0.05 Enzymes (ceiulase, amiiase 0.04 0.01 0.02 0.02 0.05 protease and / or lipase) Ra / Ga-AMG 1.0 0.05 0.002 0.001 0.05 Carbonate 0.0 10.0 - - - Perfume (encapsulated) - 0.5 0.5 - 0.3 Foam Suppressor 1, 0 0.6 0.3 - 0.10 Soap 0.5 0.2 0.3 3.0 0.5 Citrus - - - 6.0 6.0 SKS-6 - - - 4,0 - Loads up to 100% Eiemolo 2 The following granular laundry detergent compositions were prepared according to the present invention: I II III IV MES blown powder, 0 0.5 1, 0 - SADS - - - 2.0 LAS 6.0 5.0 11.0.0 6.0 TAS 2.0 - - 2.0 Zeolite A 24.0 - - 2.0 STPP - 27.0 24.0 - Sulfate 4.0 6.0 13.0 - MA / AA 1.0 4.0 6.0 2.0 Silicate 1, 0 7.0 3.0 3.0 CMC 1, 0 1, 0 0.5 0.6 Rinse aid 1 0.2 0.2 0.2 0.2 Silicone antifoam 1, 0 1, 0 1, 0. 0.3 DTPMP 0.4 0.4 0.2 0.4 Added by Spraying Rinse aid 1 or 2 or 3 0,02 - - 0,02 C45E7 - - - 5,0 C45E2 2.5 2.5 2.0 - C45E3 2.6 2.5 2.0 - Perfume 0.5 0.3 0.5 0.2 Siiicone Anti-Foam 0.3 0.3 0.3 - Dry Additives QEA - - - 1, 0 EDDS 0.3 - - - Sulphate .2.0 3.0 5.0 10.0 Carbonate 6.0 13.0 15,0.0.0 Citrus 2,5 - - 2,0 QAS 0,5 - - 0,5 SKS-6 10,0 - - - Percarbonate 4,0 3,0 - 1,9 PB4 NOBS 0,5 - - 0,3 TAED 0 , 75 4.5 - 0.5 Clay - - 10.0 - Protease 0.03 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 0.004 Ra / Ga-AMG 0.001 0.01 0.01 0.004 10 Ra / Ga Amylase - 0.005 0.01 - Amylase 0.003 _ 0.003 - Brightener 1 0.05 0, O5 Miscellaneous / minor and colored dots up to 100% Example 3 The following granular laundry detergent compositions were prepared according to the invention: t5 I II III IV VI Blown Powder LAS 23.0 8.0 7.0 7.0 7.0 7.0 QAS 1.0 C45AS 6.0 6.0 5.0 8.0. C45AE11 S 1, 0 1, 0 1, 0 0 MON 2.0 2.0 4.0 Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0 MA / AA 0.5 2, 0 MA / AA 1 7.0 - - - - - AA - 3.0 3.0 2.0 3.0 3.0 Sulfate 5.0 6.3 11.1 11.0 11.0 18.1 Silicate 10.0 1.0 1.0 1.0 1.0 1.0 Carbonate 15.0 20.0 10.0 20.7 8.0 6.0 PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0 DTPA - 0.9 0.5 - - 0.5 Rinse aid 2 0.3 0.2 0.3 - 0.1 0.3 Added Odor Spray C45E7 - 2.0 - - 2.0 2.0 10 C25E9 3,0 - - - - - C23E9 - - 1,5 2,0 - 2,0 Perfume 0.3 0.3 0.3 2.0 0.3 0.3 Aalomerados C45AS - 5,0 5,0 2,0 - 5,0 LAS - 2.0 2.0 - - 2.0 Zeolite A - 7.5 7.5 8.0 - 7.5 td Carbonate - 4.0, 5.0 - 4.0 PEG 4000 - 0.5 0.5 - - 0.5 Miscellaneous (water, etc) - 2.0 2.0 2.0 - 2.0 Dry Additives QAS I - - - - 1,0 - Cítrico - - - - 2,0 0 PB4 - - - - 5,0 - PB1 - - 4,0 1,0 - - Percarbonate 2,0 _ - 1,0 - 2.0 Carbonate - 5.3 1, 8 - 4.0, 0 NOBS 0.5 - 0.4 0.3 - Clay - - - - - 10.0 TAED 0.6. 0.4 0.6 0.3 0.9 - Methylcellulose 0.2 - - - - 0.5 DTPA 0.7 0.5 1, 0.5 0.5 1, 2 Color spots - - - 0.2 0.5 -SKS-6 8.0 - - - - - Sulfonic acid 1.0 2.0 Cumeno Lipase 0.004 - - 0.004 - 0.004 0.008 Cellulase 0.0005 0.0005 0, 0005 0.0007 0.0005 0.0005 Amylase 0.003 - 0.001 Ra / Ga-Amylase 0.01 - - 0.001 0.01 Ra / Ga-AMG 0.01 - 0.05 0.002 0.001 0.05 Protease 0.01 0.015 0.015 0.009 0.01 0.01 PVPVI 0.5 0.1 PVP 0.5 PVNO ', 5 0.3 -QEA - - 1.0 SRP1 0.2 0.5', 3 - 0.2 Silicone Antifoam 0.2 0.4 0.2 0.4 0.1 Sulfate Mg - - 0.2 - 0.2 Miscellaneous / minor up to 100% Example 4 The following granular laundry detergent compositions were prepared according to the present invention: II III IV Base granule STPP - 22.0 - 15.0 Zeolite A 30.0 - 24.0 5.0 Sulfate 5.5 5.0 7.0 7.0 MA / AA 3.0 - - - AA - 1.6 2.0 - MA / AA 1 - 12.0 - 6.0 LAS 14.0 10.0 9.0 20.0 C45AS 8.0 7.0.0 7.0 7.0 C45AE11S - 1.0 - 1.0 MONTH 0.5 4.0 6.0 - SADS 2.5 - - 1.0 Silicate - 1.0 0.5 10.0 Soap - 2.0 - - Rinse aid 1 0.2 0.2 0.2 0.2 Carbonate 6.0 9.0 8.0 10.0 PEG 4000 - 1.0 1,5 - DTPA - 0.4 - - Added by Spraying C25E9 - - - 5,0 C45E7. 1.0 1.0 - - C23E9 - 1.0 2.5 - Perfume 0.2 0.3 0.3 - Dry Additives Carbonate 5.0 10.0 13.0 8.0 PVPVI / PVNO 0.5 - 0.3 - Protease 0.03 0.03 0.03 B, 015 La 0.008 - - 0.0O8 Ra / Ga-AMG 0.01 - 0.05 0.005 Ra / Ga-Amylase - 0.01 0.02 0.001 Amylase 0.002 - - 0.002 Cellulase 0.0002 0.0005 0.0005 0.0O03 DTPA 0.5 0.3 0.5 1.0 LOBS - 0.8 - 0.3 PB1 5 3.0 10 4.0 DOBA 1, 0 - 0.4 - TAED 0.5 0.3 0.5 0.6 Sulfate 4.0 5.0 - 5.0 SRP 1 - 0.4 - - Foam Suppressant - 0.5 - - Color Dots 0.9 2.7 1.2 Miscellaneous / Minors up to 100% Example 5 The following granular laundry detergent compositions were prepared according to the invention : I II III IV V VI VII LAS C13 12.0 16.0 23.0 19.0 18.0 20.0 16.0 AS C45 - 4,5 - - - - 4,0 AE C45 (3) S - - 2.0 - 1, 0 1, 0 1.0 AE C ^ (3.0) 2.0 2.0 - 1, 3 - - 0.6 Salt of alkyldimethylhydroxy- - - - - 1.0 0.5 2.0 quaternary ethylammonium C8- C? 4 Fatty acid of sebo - - - - - - 1,0 STPP 23.0 25.0 24.0 22.0 20.0 15.0 20.0 Carbonate 15,0 12.0 15,0 10.0 13.0 11.0 10.0 AA 0.5 0.5 0.5 0.5 - - - MA / AA - - 1.0 1.0 1.0 2.0 0.5 Silicate 3.0 6.0 9.0 8.0 9.0 6.0 8.0 Sulfate 25.0 18.0 20.0 18.0 20.0 22.0 13.0 10 Sodium Perborate 5.0 5.0 10.0 8.0 3.0 1.0 2.0 PEG 4000 1.5 1.5 1.0 1.0 - - 0.5 CLM 1.0 1.0 1.0 - 0.5 0.5 0.5 Citrus - - - - - - - NOBS / DOBS 0.5 1.0 0.5 0.5 1.0 0.7 0.3 TAED 1.5 1.0 2.5 3.0 0.3 0.2 0.5 SRP 2 1.5 1.5 1.0 1.0 1.0 1.0 1.0 T5 Humidity 7.5 7.5 6.0 7.0 5.0 3.0 5.0 Mg - - - - 1.0 0.5 1.5 DTPA, HEDP and / c i EDDS - - - - 0.8 0.6 1.0 Ra / Ga-AMG 0.01 0.01 0.005 0.05 1.0 1.0 0.001 Enzymes (amylase, - - - - 0.05 0.04 0.05 cellulase and / or protease) 0 Minors, eg, perfume, up to 100% polish, photobleach, colored dots Example 6 The following granular laundry detergent compositions were prepared according to the present invention: 1 11 III IV LAS 13.3 13.7 10.4 8, 0 AS C45 3.9 3.9 4.5 - 10 AE C45 (0.5) S 2.0 2.0 - - AE C45 (6.5) 0.5 0.5 0.5 5.0 Salt of alkyldimethylhydroxy- 1, 0 - - 0.5 quaternary ethylammonium C9-C-? 4 Fatty acid of tallow 0.5 - - - Ethoxylated (50) of alcohol of - - 1, 0, 0 tallow ≤5 STPP - 41, 0 - 20.0 Zeolite A 26.3 - 21, 3 1, 0 Carbonate 23.9 12.4 25.2 17.0 AA 3.4 0.0 2.7 - MA / AA - - 1.0 0 , 5 Silicate 2,4 6,4 2,1 6,0 0 Sulfate 10,5 10,9 8,2 15,0 Sodium Perborate 1, 0 1, 0 1, 0 2,0 PEG 4000 1, 7 0 , 4 1, 0 - CMC 1, 0 - - 0.3 Citrus -. - 3.0 - NOBS / DOBS 0.2 0.5 0.5 0.1 TAED 0.6 0.5 O, 4.3 SRP 2 1, 5 1, 5 1, 0 1, 0 Humidity 7.5 3.1 6.1 7.3 Sulfate Mg - - - 1, 0 DTPA, HEDP. and / or EDDS - - - 0,5 Enzymes (amylase, cellulase, - 0.025 - 0.04 protease and / or le) Ra / Ga-AMG 0.02 - I 0.005 0.008 Mise / Minors including up to 100% perfume, brightener, photo-bleach Example 7 The following laundry detergent compositions in the form of a tablet or granulated formulation were prepared according to the invention: I II III IV V VI LAS C13 20.0 16.0 8.5 5 20.0 6.0 AS C45 > 0 - - - - AE C45 (3) S 1, 0 1, 0 - - - - AE C45 5.0 5.5 4.0 - - Salt of alkyldimethyl- 0.5 2.0 - - - - hydroxyethylammonium quaternary C8-C? 4 Fatty acid tallow - 1.0 - - - - STPP / Zeolite 10.0 20.0 30.0 20.0 25.0 25.0 Carbonate 41.0 30.0 30.0 25.0 45.0 24.0 AA - - - - - - MA / AA 2.0 0.5 0.5 1.0 - - Silicate 6.0 8.0 5.0 • 6.0 8.0 5.0 Sulfate 2.0 3.0 - - - 8.0 10 Perborate / Percarbonate 1.0 - 20.0 14.0 - - Sodium PEG 4000 - 0.5 - - - 0.5 CMC 0.5 0.5 0.5 0.5 - 0.5 Citrus - - - - - - NOBS / DOBS 0.7 - - - - - TAED / Perácido 0,7 - 4,5 5,0 - - T5 preformed DTPA, HEDP and / or EDDS - - 0,5 0,5 - - SRP 1.0 - 1.0 1.0 - - Clay 4.0 3.0 7.0 10.0 6.0 8.0 PEO 1.0 0.5 2.0 0.5 1.0 0.5 Moisturizer 0.5 - - 0.5 - - 0 Wax 0.5 - - 0.5 - - Cellulose 2.0 - • - 1.5 - 1.0 Sodium Acetate - - 1.0 0.5 4.0 1.0 Humidity 3.0 5.0 5.0 5.0 8.0 10.0 Sulfate Mg 0.5 1, 5 Soap / Suppressor 0.6 1, 0 1, 0 0.8 0.5 Foam Enzymes (amylase, 0.04 0.04 0.01 0.02 0.02 0.03 cells, protease and / or le) Ra / Ga-AMG 0.03 0.01 0.05 Ra / Gs- Ami lasa 0.02 0.003 0.1 0.002 Minor, eg, perfume, Up to 100% PVP, PVPVI / PVNO , polish, photo-bleach, colored dots. Example 8 The following laundry detergent compositions were prepared according to the invention: I II III IV V LAS C13 12.0 16.0 23.0 19.0 18.0 AS C45 4.5 AE C45 (3) S 2.0 1, 0 AE C45 2.0 2.0 1, 3 Salt of alkyldimethylhydroxy-1, 0 quaternary etiiamonium C9-C? 4 STPP / Zeoite 23.0 25, 0 14,0 22,0 20,0 Carbonate 25,0 22,0 35,0 20,0 28,0 AA 0.5 0.5 0.5 0.5 - MA / AA - - 1.0 1.0 1.0 Silicate 3.0 6.0 9.0 8.0 9.0 Perborate / Percarbonate 5.0 5.0 10.0 • - 3.0 Sodium PEG 4000 1.5 1.5 1.0 1.0 - CMC 1.0 1.0 1.0 - 0.5 NOBS / DOBS - 1.0 - - 1.0 TAED / Perácido preformed 1,5 1,5 2,5 - 3,0 10 DTPA, HEDP and / or EDDS 0.5 0.5 0.5 - 1.0 SRP 1.5 1.5 1.0 1.0 - Clay 5.0 6.0 12.0 7.0 10.0 Flocculating agent PEO 0.2 0.2 3.0 2.0 0.1 Moisturizer - - - - 0,5 Wax 0,5 - - - - Cellulose 0,5 2,0 - - 3,0 ? 5 Sodium Acetate 2.0 1.0 3.0 - - Humidity 7.5 7.5 7.0 7.0 5.0 Soap / Foam Suppressor - - 0.5 0.5 0.8 Ra / Ga-Amylase 0.005 0.02 - - 0.01 Ra / Ga-AMG - - 0.005 0.005 0.01 Enzymes (amylase, cellulase, - - - - 0.04E 0 protease and / or lipase) Minors, e.g., perfume, PVP, Up to 100% PVPVI / PVNO, brightener, photo-bleach, colored dots. EXAMPLE 9 The following laundry detergent liquid compositions were prepared according to the invention: 1 II III IV V VI LAS - - - 1.0 2.0 - C25AS 16.0 13.0 14.0.0.0.0.0 5.0 - 6.5 10 C25AE3S 5.0 1, 0 - 10.0 19.0 3.0 C25E7 2.0 3.5 - 2.5 2.0 5.0 TFAA 5.0 4.5 4.5 6.5 4, 0 - APA 2.0 1, 0 - 3.0 - 0.5 QAS - - 2.0 - 1, 5 - TPKFA 4,5 8,0 15,0 - 5,0 5,0 Citrus 2,2 3 , 0 - 0.5 1, 0 2.0 f5 Seed Fatty Acid 2.0 - - 3.0 6.0 1.5 Raza Ethanol 3.2 2.0 2.5 2.2 - 0.5 1, 2 Propanediol 5.7 8.5 6.5 7.0 7.0 5.5 Monoethanolamine 5.0 7.5 - 5.0 1.0 2.0 TEPAE - 1, 2 - 0.5 0, 5 - 0 PEI2 - 1, 5 - 1, 0.8 - DTPMP 1, 3 0.5 0.8 0.5 - 0.2 HEDP - 0.5 0.2 1, 0 - - Protease 0.02 0.03 0.02 0.02 0.02 0.01 Ra / Ga- Ami lasa 0.01 - 0.01 0.005 - - Ra / Ga-AMG - 0.02 - 0.01 0.005 0, O02 Lipase 0.002 0.001 0.001 - 0.001 - Amylase - .0006 - - 0.001 - Cellulase 0.002 0.002 - 0.002 0.001 - SRP1 0.20 0.15 0.10 - 0.17 0.04 PVNO - - - 0.05 0.10 - Polisher 3 0.20 0.15 0.10 0.05 - 0.05 Foam Suppressor 0.25 0.20 0.15 0.15 0.30 0.10 Calcium Chloride 0.02 0.02 - 0.01 0.01 - Boric Acid 2.5 2.0 1, 5 2.2 1, 5 1, 2 B - ntonite clay - - 5,5 - - - NaOH at pH 8.0 7.5 7.7 8.0 7.0 7.0 7.5 Water / Children up to 100% Eiemolo 10 The following non-aqueous liquid detergent compositions were prepared according to the present invention: I II III LAS 16.0 16.0 16.0 C23 E05S 21, 5 21, 5 19.0 Butoxl Propoxy Propanol 18.5 - 16.0 Hexylene glycol - 18.5 5.0 Citrated Sodium Dihydrate 6.8 6.8 3, 8 Sodium salt of [4- [N-nonanoyl-6-6.06,0-aminohexanoyloxy] benzenesulfonate] 1,3-methylisulfate 1,3-1,3-methylisulphate salt of methylated hexamethylenediamine, polysubstantialized EDDS 1, 2 1 , 2 1, 2 MA / AA - - 3.0 Sodium Carbonate 10.0 10.0 10.0 Protease 0.05 0.02 0.02 Ra / Ga-Amylase 0.01 - 0.05 Ra / Ga AMG - 0.01 0.02 Amylase 0.01 0.01 0.01 10 Cellulase 0.0001 0.0001 0.0001 PB1 - 12.0 12.0 12.0 Silicone Antifoam 0.75 0.75 1 , 1 Perfume 1, 7 1, 7 1, 7 Titanium dioxide 0.5 0.5 0.5 Dichloro-5, 12-Dimethyl-1, 5,8,12- - 0,03 0,03 tetraazabicyclo [6.6 .2] I5 Manganese hexadecane (II) Polisher 2 0.2 0.2 0.2 C16-18 hydrogenated soap of 1 1 0.5 sodium Color spots 0.4 0.4 0.4 Miscellaneous up to 100% Eiemolo 11 The following detergent compositions; Washing clothes in the form of a tablet were prepared according to the present invention: i) A detergent-based powder of composition I was prepared in the following manner: all the particulate material of the base composition 1 were mixed in between Yes in a mixer drum to form a homogeneous particulate mixture. During this mixing action, spraying additions were made. ii) Tablets were elaborated in the following way: 50g of the matrix was introduced inside a mold of circular shape with a diameter of 5.5 cm, and compressed to produce a tensile strength in the tablet (or diametral fracture effort) of 10kPa. iii) The tablets were then immersed in a solution comprising 90 parts of sebacic acid and 10 parts by weight of Nymcel-ZSB16 ™ by Metsa Serla at. 140 aC. The duration of the tablet in immersion in the heated solution was adjusted to allow the application of 4g of the solution mixture. The tablet was then allowed to cool to room temperature of 25OC for 24 hours. The tensile strength of the coated tablet was increased to a tensile strength of 30 kPa. i Anionic agglomerates 1 (40% anionic, 27% zeolite and 33% 21, 5 carbonate) Anionic agglomerates 2 (40% anionic, 28% zeolite and 32% 13.0 carbonate) Cationic agglomerates (20% cationic, 56% zeolite and 24%) % 5.5 sulphate) Layered silica (95% SKS-6 and 5% Silicate) 10.8 Sodium percarbonate 14.2 Brightening activator agglomerates (81% TAED, 17% 5.5 acrylic / maleic copolymer (acid form) and 2% water) Carbonate 10.98 EDDS / Sulphate particle (58% EDDS, 23% sulphate and 19% 0.5 water) HEDP 0.8 SRP 0.3 Fluorescence agent 0.2 Photoactivated bleach (zinc phthalocyanine sulfonate 10% 0, 02 active) 0 Soap powder 1, 4 Foam suppressor (11, 5 Siiicone oil, 59% zeolite and 1, 29.5% water) Citrus 7.1 Ra Ga-Amiiase 0.05 Protease 0.03 Lipase 0.006 -5 Cellulase 0.0005 Amylase 0.02 Binder system added by spraying (25% of Lutensit K-4.0 HD 96, 75% by weight of PEG Example 12 The following laundry detergent compositions in the form 0 of a tablet were prepared according to the invention: I II III IV V VI First Percarbonate Phase 45.0 45.0 45.0 45.0 45.0 45.0 TAED 9.7 9.7 9.7 9.7 9.7 9.7 Citric acid 10.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0.0 6.0 , 0 1, 0 5,0 Silicate - - - - 6,0 - Bicarbonate 15,0 15,0 10,0 15,0 15,0 15,0 Carbonate 5,0 Brightener 1 or 2 0,1 0,1 0.1 0.1 0.1 0.1 Perfume 0.2 0.2 0.2 0.2 0.2 0.2 10 Fatty Acid C12-16 - - 1.0 Protease 0.03 0.03 .0.03 0.03 0.03 0.03 Amylase 0.02 0.02 - 0.02 Second Phase Ra / Ga-AMG 0 , 01 0.02 0.04 0.01 0.1 0.5 Protease 0.04 0.04 0.04 0.04 0.04 0.04 Amillase 0.02 0.02. . . . fd Color dots 0.09 0.09 0.09 0.09 0.09 0.09 PEG 4000 0.33 0.33 0.33 0.33 0.33 0.33 Citrus 1.06 1, 06 1 , 06 1, 06 1, 06 1, 06 Bicarbonate 2.87 2.87 2.87 2.87 2.87 2.87 Example 13 The following laundry detergent compositions were prepared according to the present invention. levels are presented in parts by weight, the enzyme is expressed in pure enzyme): I II III IV V VI VII VII S - - 19.0 15,0 21, 0 6.75 8.8 - C28AS 30.0 13, 5 - - - 15.75 11, 2 22.5 Laurato Na 2.5 9.0 - - - - - - Zeolite A 2.0 1, 25 - - - 1, 25 1, 25 1, 25 Carbonate 20.0 3.0 13.0 8.0 10.0 15.0.0.0.0.0.0 Carbonate Ca 27.5 39.0 35.0 - - 40.0 - 40.0 Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0 TSPP 5,0 - - - - 5,0 2,5 - STPP 5,0 15,0 10,0 - - 7,0 8,0 10,0 Bentonite clay - 10.0 - - 5,0 - - - 10 DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7 CMC -. 1, 0 1, 0 1, 0 1 '°. - - 1, 0 Talcum - - 10.0 15,0 10,0 - - - Silicate - - 4,0 5,0 3,0 - - - PVNO 0,02 0,03 - 0,01 - 0,02 - - MA / AA 0.4 1, 0 - - 0.2 0.4 0.4 0.4 SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 t5 Amylase - - 0.01 - - -, 002 - Ra / Ga-AMG 0.01 0.1 0.02, 002 - 0.01 0.01, 002 Ra / Ga-Amylase - - - - 0.05 - 0.02, 001 Protease -, 004 -, 003, 003 - -, 003 Lipase -, 002 -, 002 - - - - Cellulase "* .000 - ~ .000 .000" - 0 3 3 2 PEO - 0.2 - 0.2 0.3 - - 0.3 Perfume 1, 0 0.5 0.3 0.2 0.4 - - 0.4 Sulfate Mg - 3.0 33,, 00 33,, 00 - Polisher 0.15 0.1 0.15 0.1 Bleaching 15,0 15,0 15,0 15,0 15,0 Photoactivated (ppm) Example 14 The following granular detergent compositions of fabrics that provide "softening through washing" capability were prepared according to the present invention: C45AS - 10.0 The 7,6 - C68AS 1, 3 - C45E7 4,0 - C25E3 - 5,0 Coconut-aiquiidimethyl 1,4,4,1-hydroxy-ethylammonium chloride Citrate 5,0 3,0 Na-SKS-6 - 1 1, 0 Zeoiite A 15,0 15.0 MA / AA 4.0 4.0 DETPMP 0.4 0.4 PB1 15,0 - Percarbonate - 15,0 TAED 5,0 5,0 Smectite Clay 10.0 10.0 HMWPEO - 0.1 Protease 0.02 0.01 Lipase 0.02 0.01 Ra / Ga-AMG - 0.02 Ra / Ga-Amiiase 0.05 - Amylase 0.03 0, O0 £ Cellulase 0.001 - Silicate 3.0 5.0 Carbonate 10.0 10.0 Foam Suppressor 1, 0 4.0 CMC 0.2 0.1 Miscellaneous and minor up to 100% Example 15 The following softener compositions that are added in the rinse were prepared according to the present invention: DEQA (2) 20.0 Cellulase 0.001 Ra / Ga-AMG 0.005 HCL 0.03 Antifoaming agent 0.01 Blue coloring 25ppm CaCI2 0.20 Perfume 0.90 Miscellaneous and water up to 100% Example 16 The following fabric softening and fabric conditioning compositions that are added in the dryer were prepared according to the invention: I II III IV V DEQA 2,6 19,0 - - - DEQA (2) - - - - 52,0 DTMAMS - - - 26,0 - SDASA - - 70,0 42,0 40,2 Stearic acid of IV = 0 0.3 - - - - C45E01-3 - - 13.0 - - HCL 0.02 0.02 - - - Ethanol - - 1, 0 - - Perfume 0.3 1, 0 0, 75 1, 0 1, 5 Glycoperse S-20 - - - - 15,4 Glycerol monostearate - - - 26.0 - Digeranii Succinate - - 0.38 - - Siiicone antifoam 0.01 - - - Electrolyte - 0.1 - - - Amylase - 0.2 - 0.2 0 ,2 Ra / Ga-AMG 1, 0 0.2 0.1 0.01 0.01 Clay - - - 3,0 - Colorant 10ppm 25ppm 0,01 - - Water and minors 100% 100% - - - Eiemolo 17 The following compact detergent compositions of high density (0.96Kg / l) to wash dishes were prepared according to the invention: I II III IV V VI STPP - 51, 0 51, 0 - - 44.3 Citrate 17,0 - - 50,0 40,2 - Carbonate 17,5 14,0 20,0 - 8,0 33,6 Bicarbonate - - - 26,0 - - Silicate 15,0 15,0 8,0 - 25,0 3,6 Metasilicate 2.5 4.5 4.5 - - - PB1 10.0 8.0 8.0 - - - PB4 - - - 10.0 - - Percarbonate - - - - 11, 8 4.8 Non-ionic 2.0 1, 5 1, 5 3.0 1, 9 5.9 TAED 2.0 - - 4.0 - 1, 4 HEDP 1, 0 - - - - - DETPMP 0.6 - - - - - MnTACN - - - - 0.01 - PAAC - 0.01 0.01 - - - Paraffin 0.5 0.4 0.4 0, 6 - - Protease 0.07 0.05 0.05 0.03 0.06 0.01 Amylase 0.01 - 0.01 - 0.02 - Ra / Ga-AMG 0.02 0.2 - - 0.002 0.02 Ra / Ga-Amylase - - 0.02 0.02 - - Lipase - 0.001 - 0.005 - - BTA 0.3 0.2 0.2 0.3 0.3 0.3 0.3 Polycarboxylate 6.0 - - - 4.0 0.9 Perfume 0.2 0.1 0.1 0.2 0.2 0.2 H 11, 0 11, 0 11, 3 9.6 10.8 10, 9 Miscellaneous, sulphate up to 100% and water Eiemolo 18 The following granular detergent compositions of c densit; Volumetric 1, 02Kg / L were prepared according to the invention: I II III IV V VI STPP 30.0 33.5 27.9 29.6 33.8 22.0 Carbonate 30.5 30.5 30.5 23.0 34.5 45.0 Silicate 7.0 7.5 12.6 13.3 3.2 6.2 Metasilicate - 4,5 - - - -.

PB1 4.4 4.5 4.3 - - - NADCC - - - 2.0 - 0.9 Non-ionic 1, 0 0.7 1, 0 1, 9 0.7 0.5 TAED 1, 0 - - - 0.9 - PACC - 0.004 - - - - Paraffin 0.25 0.25 - - - - Protease 0.036 0.021 0.03 - 0.006 - Amylase 0.03 - 0.004 - 0.005 - Ra / Ga -AMG 0.2 0.02 - - 0.02 0.005 Ra / Ga-Amylase - - 0.01 - - - Lipase 0.005 - 0.001 - - - BTA 0.15 0.15 - - 0.2 - Perfume 0.2 0.2 0.05 0.1 0.2 - PH 10.8 11, 3 11, 0 10.7 11, 5.10.9 Miscellaneous, sulfate and up to 100% water Example 19 The following tablet detergent compositions were prepared according to the present invention by compression of a granular washing detergent composition plates at a pressure of 13KN / cm2 using a normal 12-head rotary press: I II III IV V VI VII VIII STPP - 48.8 54.7 38.2 - 52.4 56.1 36.1 Citrate 20.0 - - - 35.9 - - - Carbonate 20.0 5.0 14.0 15.4 8.0 23.0 20.0 28.0 Silicate 15.0 14.8 15.0 12.6 23.4 2.9 4.3 4.2 Protease, 042, 072, 042, 031, 052, 023, 023, 029 Amylase, 012, 012, 012, 007, 015 - -, 002 Ra / Ga-AMG 0.02 0.01, 002, 05, 008, 002 - 0.02 Ra / Ga-Amylase, 001 - - - - 0.03 0.01 - Lipase, 005 - - - - - - - PB1 14.3 7.8 11, 7 12.2 - - 6.7 8.5 PB4 - - - - 22,8 - 3,4 - Percarbonate - - - - - 10,4 - - Non-ionic 1, 5 2,0 2,0 2,2 1, 0 4,2 4,0 6,5 PAAC - - 0,02, 009 - - - - MnTACN - - -, 007 - - - TAED 2,7 2,4 - - - 2,1 0,7 1, 6 HEDP 1, 0 - - 0.9 - 0.4 0.2 - DETPMP 0.7 - - - - - - - Paraffin 0.4 0.5 0.5 0.5 - - 0.5 BTA 0.2 0.3 0.3 0.3 0.3 0.3 0.3 Polycarboxylate 4.0 - - - 4.9 0.6 0.8 PEG 4.000-30.000 - - - - - 2.0 2.0 Glycerol - - - - - 0,4 0,5 Perfume - - - 0.05 0.2 0.2 0.2 0.2 Weight of tablet 20g 25g 20g 30g 18g 20g 25g 24g PH 10.7 10.6 10.7 10.7"10.9 11.2 11.0 10.8 Miscellaneous, up to 100% sulfate and water Eiemolo 20 The following liquid detergent and dishwashing compositions of density 1.40Kg / L were prepared according to the present invention: 1 II III IV STPP 17.5 17.2 23.2 23.1 Carbonate 1 2,4 - - Silicate 6,1 2,4 - - NaOCI 1,1 1,1 1,1 1,2 Thickener 1.0 1.1 1.1 1.0 Non-ionic - 0.1 0.06 0.1 NaBz 0.7 - - - Ra / Ga-AMG 0.005 1.0 0.005 0.02 NaOH 1.9 - - - KOH 3.6 3.0 - - Perfume 0.05 - - -pH 11.7 10.9 10.8 11.0 Water up to 100% Example 21 The following dishwashing compositions in the form were prepared according to the invention (The levels are indicated in grams): I II III IV V VI Phase 1 STPP 9.6 9.6 10.4 9.6 9.6 1 1, 5 Silicate 0.5 0.7 1, 6 1, 0 1, 0 2.4 SKS-6 1, 5 1, 5 - 2,3 2,25 - Carbonate 2,3 2,7 3,5 3,6 4,1 5,2 HEDP 0.2 0.2 0.2 0.3 0.3 0.3 PB1 2.4 2.4 2.4 3.7 3.7 3.7 PAAC 0.002 0.002 0.002 0.003 0.004 0.004 Ra / Ga-AMG 0.01 0.02 0.05 0.002 0.001 Ra / Ga-Amylase 0.01 - 0.01 Amylase 0.002 0.001 - Protease 0.002 0.002 0.002 0.003 0.003 0.003 Non-ionic 0.4 0.8 0.8 1, 2 1, 2 1, 2 PEG 6000 0.4 0.3 0.3 0.4 0.4 0.4 0.4 BTA 0.04 0.04 0.04 - 0.06 0.06 Paraffin 0.1 0.1 0.1 0.15 0.15 0.15 Perfume 0.02 0.02 0.02 0.01 0.01 0.01 Sulfate - - - 0,5 0,05 2,3 Phase 2 Ra / Ga-AMG 0.003 0.003 0.002 0.01 0.01 1, 01 Amylase .0005 .0005 .0004 .0005 .006 .0004 Protease 0.009 0.008 0.01 0.009 0.008 0.01 Citrus 0.3 - 0.3 0.3 - 0.30 Sulfamic acid - 0.3 - - 0.3 - Bicarbonate 1.1 0.4 0.4 1.1 0.4 0.4 Carbonate - 0,5 - - 0,5, - Silicate - - 0,6 - - 0,6 CaCl - 0.07 - - 0.07 - PEG 3000 0.06 0.06 0.06 0.06 0.06 0.06 The multi-phase tablet compositions are prepared in the following manner. The active detergent composition of phase 1 is prepared by mixing the granular and liquid components together and then passing into the mold of a conventional rotary press. The press includes a shaped die suitable for forming the mold. The cross section of the mold is approximately 30x38mm. The composition is then subjected to a compression force of 940 kg / cm 2 and the die is then raised by exposing the first phase of the tablet containing the mold on its top surface. The active detergent composition of phase 2 is prepared in a similar manner and passed into the mold. The active particulate composition is then subjected to a compression force of 170 kg / cm2, the die is raised, and the multi-stage tablet is ejected from the tablet press. The resulting tablets are dissolved or disintegrated in an automatic washing machine as described above before 12 minutes, phase 2 of the tablets dissolves within 5 minutes. The tablets provide excellent dissolution and cleaning characteristics together with good integrity and resistance of the tablet. EXAMPLE 22 The following hand dishwashing compositions were prepared according to the present invention: I II III IV V VI VII VII C12-14E0-3S 26.0 34.2 25.0 26.0 37.0 26.0 22.0 32.0 C11 LAS 13.0 Amine oxide 2.0 4.9 2.1 6.5 5 , 5 6.5 1 C12-14 Betaine C12-14 2.0 5.0 2.1 - 4.0 Glucosamine 1.5, 1.5 3.1 C12-14 C9-11 E8-9 4.5 1 4 , 1 3.0 1, 0 3.0 1, 0 Alkylpolyglycoside 12.0 3.0 Monoethanolamine 1.5, C1-20 DTPA 0.1 0 0- 0-0-000 500p 500p 500p pm pm pm Succinic acid - - - - - 1 to 6 - Sulfonate of - 5,0 - - 4,0 - 2,5 Xylene Ca or Na Sales Mg (in% 0,5 0,7 0,5 0,04 0,6 0,04 0.3 0 Mg) 1, 3 bis (methyl- - - 0.5 - 0.5 -amino) cyclohexane homopolymer of - - - 0.2 - 0.2 N, N-dimethylamino ethyl methacrylate Citrus - - - 0 - - 0- ~ - 3.5 3.5 Ethanol 6-8 5-8 6-9 4-10 7.0 4-10 4.0 4.0 Protease - - - 0-0- - 0- "- 08 0.08 Ra / Ga-AMG 0.05 .002 .005 0.01 0.4 0.05 .002 0.01 Amylase - - - 0.00 - 0.00 0.04 0.05 2 5 Carbonate - - - - - 2,5 - - Polypropylene glycol - - - 0 to 2 - - - - (molecular weight 2000-4000) pH 7-8 7-8 7-8 8.5- 7-8 8.5- 7 7 11 11 Perfume 0.1 - 0.7 Balance (water and up to 100% less) Example 23 The following composition of fabrics and surfaces Hardness was prepared according to the present invention: Sulfate 18.5 Bicarbonate 18.6 Polycarboxylate 4.1 Alpha-olefin C18 0.2 Enzyme (lipase, protease, and / or cellulase 0.004

Claims

Amylase 0.003 Ra / Ga-AMG 0.05 Rinse aid 2 0.1 Photoactivated bleach 0.04 Coated sodium percarbonate 45.0 TAED 8.8 Citrus 2.5 Perfume 0.1 Miscellaneous and water up to 100% CLAIMS

1. A detergent composition comprising a detergent ingredient and an enzyme that degrades raw starch which is characterized by an activity ratio to degrade raw starch (Ra) to activity to degrade geiatinized maize starch (Ga): [Ra / Ga] higher 0.2, preferably greater than 0.35. . A detergent composition according to Claim 1 wherein the enzyme which degrades the aforementioned crude starch is comprised at a level of 0.0002% to 10%, preferably 0.002% to 2%, more preferably 0.002% to 1% pure enzyme in weight of the total detergent composition. A detergent composition according to Claims 1-2 wherein the enzyme which degrades the aforementioned crude starch is selected from an amyloglucosidase EC 3.2.1.3, an α-amylase EC 3.2.1.1, a beta-amylases EC 3.2.1.2, an isoamylase EC 3.2.1.68, a pullulanase type I EC 3.2.1.41, an isopululase EC 3.2.1 .57, a neopululase EC 3.2.1.135, a pullulanase type II, a dextranase dextrin EC 2.4.1.24, a glycosyltransferase cyclodextrin EC 2.4 .1.19, a maltogenic alpha-amylase EC 3.2.1.133 and / or mixtures of these. A detergent composition according to Claims 1-3 wherein the enzyme which degrades the aforementioned crude starch has or has been added a starch binding domain. A detergent composition according to Claims 1-4 further comprising an enzyme that is selected from a lipase, a protease, a conventional amylase, an enzyme that degrades conventional starch, a conventional type 1 or II puiulase, and / or mixtures thereof . A detergent composition according to any of the preceding Claims wherein the aforementioned detergent ingredient is selected from nonionic surfactants, flocculating agents, and / or mixtures thereof. The use of an enzyme that degrades raw starch in a detergent composition for the hydrolysis of raw starch. The use according to Claim 7 for the elimination of stains and soils containing starch, and when they are formulated as laundry compositions, excellent maintenance of whiteness and the cleaning of the soiled dirt.