JP2002513563A - Laundry detergent and / or fabric care composition containing modified transferase - Google Patents

Abstract

  (57) [Summary] The present invention relates to a modified enzyme comprising a catalytically active amino acid sequence of transferase linked to an amino acid sequence containing a cellulose binding domain (CBD). The invention further relates to laundry detergent and / or fabric care compositions containing such modified enzymes for improved fabric care and cleaning effectiveness.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

FIELD OF THE INVENTION

The present invention relates to laundry detergent and / or fabric care compositions containing a modified enzyme composed of a transferase catalytically active amino acid sequence linked to an amino acid sequence containing a cellulose binding domain (CBD).

[0002]

BACKGROUND OF THE INVENTION

Laundry detergents and / or fabric care compositions are now active ingredients that meet certain special needs: surfactant systems, enzymes that exert cleaning and fabric care benefits, bleaches, builder systems, foam inhibitors. Contains a complex combination of soil suspending agents, soil release agents, optical brighteners, softeners, dispersants, dye transfer inhibiting compounds, abrasives, bactericides, and fragrances. Has been improved over the years.

[0003] However, the complex nature of daily "body" stains typically found in pillowcases, T-shirts, collars and socks has led to the difficulty of continuous and careful cleaning with detergents. These stains are difficult to completely and completely remove the residue that accumulates on the fabric and turns black and yellow. In addition, detergent removal of stains from plant, wood, mud-clay based soils and fruits is one of the most difficult cleaning tasks, especially when there is a tendency to shift to lower wash temperatures and shorter wash cycles. These stains typically contain a complex mixture of fibrous materials, mainly based on carbohydrates and their derivatives, fibers and cell wall components. Such stains are usually associated with amylose, sugars and their derivatives.

[0004] In recent years, there has been an increasing desire of consumers for fabric conditioning compositions.
Fabric softening compositions impart some desirable properties to the treated garment, including softness and static control. Fabric flexibility of the washed garment is typically obtained by delivering a quaternary ammonium compound to the surface of the fabric. Consumers' desire for durable press fabric garments, especially cotton fabric garments, has also increased.
Durable press garments include those that resist fabric wrinkles both during wear and during the washing process. Durable press garments can significantly reduce the manual work involved in washing by eliminating ironing, which is sometimes needed to prevent wrinkling of the garments. However, in most commercially available durable press fabrics, the ability of the fabric to resist wrinkles is:
As clothing is worn and washed many times, it gradually decreases. In addition, colored clothing tends to wear out and lose appearance. Part of this fading may be due to abrasion in the washing process, especially in automatic washing machines and automatic washing and drying machines. Moreover, the tensile strength loss of the fabric appears as an unavoidable result of mechanical / chemical action due to use / wear or washing.

[0005] As mentioned above, laundry detergent compositions capable of cleaning fabrics and / or fabric stains and / or maintaining fabric whiteness and / or colour appearance and / or dye transfer inhibition, especially against body stains and plant based stains The need for things continues.

In addition, it imparts tensile strength, anti-wrinkle, anti-pilling and anti-shrink properties to fabrics, refreshes or restores, and provides static suppression, fabric flexibility, color appearance and fabric wear resistance and effectiveness. There is a continuing need for laundry detergent compositions and / or fabric care compositions.

[0007] The above object is to formulate a laundry detergent and / or fabric care composition containing a modified enzyme consisting of a transferase catalytically active amino acid sequence linked to an amino acid sequence containing a cellulose binding domain (CBD). By being satisfied.

[0008] Transferase enzymes have been described in the art: using sugar chain transferases such as cyclodextrin glycosyltransferase or α-amylase in isolated and highly pure form such as maltose and malt oligosaccharides. A process for producing saccharides of constant chain length is disclosed in EP560982 for pharmaceuticals. US 5,516,689 describes an enzyme composition containing transglucosidase and / or pectinase and a means for reducing the stickiness of sugar-enriched cotton in order to avoid some problems during cotton spinning. I have. Microbial transglutaminases, their production and their use for various industrial purposes are described in WO 96/06931. JP7-107
971 belongs to the genus Bacillus and relates to a microorganism capable of producing alkali-resistant cyclodextrin glucanotransferase for dish washing, which degrades and removes food soil, and the produced cyclodextrin is used as a masking deodorant. Works, and it improves foaming and soil emulsification. A dishwashing detergent composition containing a cyclodextrin glucanotransferase having a cleaning and deodorizing effect is described in JP 7-109488.

[0009] Enzymes linked to the cellulose binding domain have also been described in the art: WO9
1/10732 discloses that the core region derived from the endoglucanase produced by the strain of Bacillus spp. A novel derivative of the cellulase enzyme is described which combines a core region derived from the cellulase enzyme with CBD derived from the endoglucanase. WO94 / 07998
Describes a cellulase variant of cellulase classified into family 45, comprising a CBD, a catalytically active domain (CAD) and a region connecting the CBD to the CAD, wherein one or more amino acid residues are added or deleted. Or has been substituted and / or another CBD has been added to the opposite end of the CAD. WO9
5/16782 discloses a Trichode, which contained a different core region with several CBDs.
Cloning and high-level expression of a novel truncated cellulase protein or its derivative in rma longibrachiatum. WO97 / 01629 is
A cellulolytic enzyme product is described in which the mobility of the cellulase component has been reduced, for example, by adsorption to an insoluble or soluble carrier, via an existing or newly introduced CBD. WO 97/28243 discloses a modified enzyme comprising a catalytically active amino acid sequence of a non-cellulolytic enzyme selected from amylase, protease, lipase, pectinase and oxidoreductase, linked to an amino acid sequence containing a cellulose binding domain; A process for the removal or bleaching of stains or stains from cellulosic fabrics, in which the fabric is contacted, and detergent compositions containing such modified enzymes and surfactants are described.

However, all of these documents disclose laundry detergent and / or fabric care compositions containing a modified enzyme composed of a transferase catalytically active amino acid sequence linked to an amino acid sequence containing a cellulose binding domain. I haven't.

[0011]

[Summary of the Invention]

The present invention relates to a modified enzyme comprising a catalytically active amino acid sequence of transferase linked to an amino acid sequence containing a cellulose binding domain (CBD). In a second aspect, the present invention relates to laundry detergent and / or fabric care compositions containing such modified transferase enzymes for improved fabric care and cleaning effectiveness. In a third aspect, the invention relates to a method comprising the step of contacting a fabric with a laundry detergent and / or fabric care composition as described above.

[0012]

DETAILED DESCRIPTION OF THE INVENTION

The present invention relates to a modified enzyme (enzyme hybrid) composed of a transferase catalytically active amino acid sequence linked to an amino acid sequence containing a cellulose binding domain (CBD).

[0013] Transferase enzymes and substrates transferase enzyme catalyzes the transfer of functional compounds to a certain substrate. In particular, the transferases of the present invention have the ability to transfer chemical moieties, such as methyl or glycosyl groups, from small substrates to form oligomer molecules or extend polymer compounds. When using small substrates, the enzyme can bind to functional groups such as methyl, hydroxymethyl, formyl, carboxyl, aldehyde, ketone, acyl, amino and phosphorous functions and / or attach glycosyl residues to clothing surfaces. Transfer improves the properties of the garment. The properties of the garment to be improved include tensile strength to the fabric, anti-wrinkle, anti-pilling and anti-shrinkage, static control, fabric flexibility, color appearance and fabric wear resistance and effectiveness. When the transferase level is high and the substrate concentration is low, the functional groups are transferred to water molecules to exert a cleaning effect.

[0014] Without being bound by theory, the addition of the cellulose binding domain to the transferase enzyme results in a higher concentration of transferase to the fabric, ie, closer and / or more sustained contact, resulting in more efficient It is thought that it exerts various enzyme activities. The transferase so modified has a high affinity (compared to the unmodified enzyme) in binding to cellulose fibers or textiles. The transferases described above, when combined with CBD, have improved fabric cleaning and / or fabric stain removal and / or fabric stain whiteness and / or fabric whiteness maintenance and / or color appearance and / or color transfer inhibition, especially when combined with CBD. It was surprisingly found that I could do. In addition, such modified enzymes provide improved fabric care, i.e., they impart tensile strength, anti-wrinkle, anti-pilling and anti-shrink properties to the fabric, refresh or restore, and improved antistatic, fabric Provides flexibility, color appearance and fabric wear resistance properties and benefits.

[0015] Transferases suitable for the present invention are the enzymes that transfer the EC2.1 1 carbon group, E
C2.2 enzymes that transfer aldehyde or ketone residues, EC2.3 acyltransferase, EC2.4 glycosyltransferase, EC2.5 enzymes that transfer alkyl or aryl groups other than methyl groups, EC2.6 enzymes that transfer nitrogen groups, and EC2 .7 represented by an enzyme transferring phosphorus-containing groups.

Examples of suitable transferases are: EC 2.1.1.15 fatty acid O-methyltransferase EC 2.1.1.18 polysaccharide O-methyltransferase EC 2.1.2.1 glycine hydroxymethyltransferase EC 2.1.2.4 glycine formimino Transferase EC 2.2.1.3 Formaldehyde transketolase EC 2.3.1.3 Glucosamine N-acetyltransferase EC 2.3.1.18 Galactoside acetyltransferase EC2.3.1.57 Diamine N-acetyltransferase EC2.3.1.75 Long-chain alcohol O-fatty acyl Transferase EC2.3.1.79 Maltose O-acetyltransferase EC2.3.1.84 Alcohol O-fatty acetyltransferase EC2.3.1.88 Peptide α-N-acetyltransferase EC2.3.1.96 Protein N- palmitoyl transferase EC2.3.1.142 glycoprotein O- fatty acyltransferase EC2.5.1.10 geranyltransferase EC2.5.1.20 rubber cis - poly Premier Rushisu transferase EC2.6.1 aminotransferase

For certain applications, preferred transferases exhibit some / most of their activity under alkaline conditions, ie at least 10%, preferably at least 10% of the maximum activity at a pH of 7 to 12, preferably 10.5. At least 25%, more preferably at least 4
It is an enzyme having 0% enzyme activity. More preferred transferases are 7-
It is an enzyme having a maximum activity at a pH of 12, preferably 10.5. Other preferred transferases are those that have at least 50% of their maximum activity at 10-50 ° C.

Preferred transferases for the laundry detergent and / or fabric care compositions of the present invention are included in the class of acyltransferases (EC2.3) and glycosyltransferases (EC2.4). Of particular interest is the group of acyltransferases, especially aminoacyltransferases (EC 2.3.2). These are enzymes that transfer an amino group, usually an amino acid, from a donor to an acceptor. Even more preferred is protein-glutamine γ-glutamyltransferase (EC 2.3.2.13), also commercially available under the name transglutaminase.
Without being bound by theory, it is believed that enzymatic cross-linking of amino acids, di / tri / poly-peptides and / or proteins occurs in the fabric, resulting in increased tensile strength and improved appearance. Furthermore, hydrolysis of the substrate present in the stain / stain by the aminoacyltransferase exerts a cleaning effect.

The group of glycosyltransferases is also of particular interest. The general property of these enzymes is to transfer a sugar from an oligosaccharide to another carbohydrate as an acceptor. Both hexosyltransferases and pentosyltransferases can be used in the present invention. Glycosyltransferases catalyze both hydrolysis and transfer reactions upon incubation with oligosaccharides. As a result of the enzymatic activity, oligosaccharides are converted to a new class of polysaccharides. It has been surprisingly found that glycosyltransferases linked to the cellulose binding domain improve the tensile strength and appearance of the fabric, for example, reduce fabric wrinkles. Without being bound by theory, because of the glycosyltransferase activity, the oligosaccharides are bound to the cellulose polymer of the cotton fabric, resulting in improved tensile strength and exerting an aesthetic effect, especially after multiple washing cycles. Is actually considered.

Without being bound by theory, it is believed that glycosyltransferase activity has three possible modes of action in exerting a fabric care effect:
-Enzymatic stitching (enzymes are thought to bind oligosaccharides to cellulose fibers with reduced tensile strength);-Enzymatic crosslinks (glycosyltransferases bind cellulose fibers with reduced tensile strength to each other) And enzymatic polymer binding (polymer bound to cellulose fibers with reduced tensile strength) In addition, in the presence of low levels of substrate and high levels of glycosyltransferase, glycosyl groups are transferred to water molecules. Being brought a cleaning effect.

For example, transglucosidase is an enzyme that catalyzes both hydrolysis and transfer reactions in a solution containing α-D-glucooligosaccharide. As a result of the transglucosidase enzymatic reaction, malt oligosaccharides are converted to isomalt oligosaccharides, a new class of polysaccharides characterized by a high proportion of saccharides linked by α-D-1,6 linkages from the non-reducing end. Bring sugars. These transglucosidases were found to exhibit fabric care performance.
The improved tensile strength, reduced wrinkles and good appearance are believed to be due to the oligosaccharides attached to the cellulosic polymer fibers of cotton.

Examples of suitable glycosyltransferases are galactosyltransferase and fructosyltransferase, such as 1,4-β-galactosyltransferase; 1,3-α-fructosyltransferase; 2,3-sialyltransferase; cyclodextrin glycosyltransferase; N-acetylgluco or galactosaminyltransferase; and EC 2.4.1.2 1,4-α-D-glucan: 1,6-α-D-glucan 6-α-D-glucosyltransferase EC 2.4.1.4 Sucrose: 1,4-α-D-glucan 4-α-D-glucosyltransferase EC 2.4.1.5 sucrose: 1,6-α-D-glucan 6-α-D-glucosyltransferase EC 2.4.1.9 sucrose: 2, 1- -D-fructan 1-β-D-fructosyltransferase EC 2.4.1.10 Sucrose: 2,6-β-D-fructan 6-β-D-fructosyltransferase EC 2.4.1.11 UDP glucose: glycogen 4-α -D-glucosyltransferase EC2.4.1.12 UDP glucose: 1,4-β-D-glucan 4-β-D-glucosyltransferase EC2.4.1.13 UDP glucose: D-fructose 2-α-D-glucosyltransferase EC2 .4.1.16 UDP-N-acetylglucosamine: chitin 4-β-N-acetylglucosaminyltransferase EC 2.4.1.18 1,4-α-D-glucan: 1,4-α-D-glucan 6-α -D- (1,4-α-D-glucano) transferase EC 2.4.1.19 1,4-α-D-glucan 4 -Α-D- (1,4-α-D-glucano) transferase (cyclization) EC 2.4.1.21 ADP-glucose: 1,4-α-D-glucan 4-α-D-glucosyltransferase EC2.4.1. 24 1,4-α-D-glucan: 1,4-α-D-glucan (D-glucose) 6-α-D-glucosyltransferase EC 2.4.1.25 1,4-α-D-glucan: 1, 4-α-D-glucan 4-α-D-glycosyltransferase EC2.4.1.29 GDP glucose: 1,4-β-D-glucan 4-β-D-glucosyltransferase EC2.4.1.34 1,3-β -Glucan synthetase EC 2.4.1.35 UDP glucose: phenol β-D-glucosyltransferase EC2.4.1.49 1,4-β-D-oligo-D-glucan: orthophosphate α-D-glucosyltrans EC2.4.1.67 1-α-D-galactosyl-myo-inositol: raffinose galactosyltransferase EC2.4.1.71 UDP glucose: arylamine ND-glucosyltransferase EC2.4.1.75 UDP galacturonic acid β-D-galacturonosyltransferase EC 2.4.1.82 1-α-D-galactosyl-myo-inositol: sucrose 6-α-D-galactosyltransferase EC2.4.1.90 UDP galactose: N-acetyl-D-glucosamine 4-β-galactosyltransferase EC2.4.1. 93 Inulin D-fructosyl-D-fructosyltransferase EC2.4.1.99 Sucrose: 1F-fructosyltransferase EC2.4.1.100 1,2-β-D-fructan: 1,2-β-D-fructan 1-β- -Fructosyltransferase EC2.4.1.113 ADP glucose: protein 4-α-D-glucosyltransferase EC2.4.1.121 UDP glucose: indole-3-acetic acid β-D-glucosyltransferase EC2.4.1.125 Sucrose: 1,6 -Α-D-glucan 3 (6) -α-D-glucosyltransferase EC 2.4.1.140 Sucrose: 1,6 (1,3) -α-D-glucan 6 (3) -α-D-glucosyltransferase EC2 .4.1.161 1,4-α-D-glucan: 1,4-α-D-glucan 4-α-D-glucosyltransferase EC 2.4.1.168 UDP glucose: xyloglucan 1,4-β-D-glucosyl Transferase EC 2.4.1.169 UDP-D-xylose: xyloglucan 1,6-β-D-xylosyltran Luciferase EC2.4.1.183 UDP-glucose: α-D- (1,3) - a glucan 3-alpha-D-glucosyltransferase. Of particular interest is EC 2.4.1.24, 1,4-α-D-glucan: 1,
4-α-D-glucan (D-glucose) 6-α-D-glucosyltransferase. A specific example of this enzyme is commercially available under the name Transglucosidase L-500.

In addition to the glycosyltransferases described above, mutant glycosyltransferases and / or mutant glycosidases (examples of which include SGWithers et al., PCT Application Publication No. WO 97/21822, Canadian Canadian Patent 2,165)
U.S. Pat. No. 5,041, and its U.S. Pat. No. 5,716,812) improve the tensile strength and appearance of fabrics, e.g., reduce fabric wrinkles, enhance shape retention, and reduce shrinkage. all right. Variant forms of glycosyltransferases and / or glycosidases carry out enzyme patching, enzyme cross-linking and enzyme polymer conjugation, as described in further detail above.

The mutant glycosyltransferase and / or mutant glycosidase each have only one nucleophilic amino acid at the active site of the enzyme, rather than two, such as a non-mutant glycosyltransferase and / or non-mutant glycosidase. ing. In other words, a mutant glycosyltransferase and / or mutant glycosidase has been formed in which one of the standard nucleophilic amino acids in the active site has been changed to a non-nucleophilic amino acid. As a result, the mutant glycosyltransferase and / or mutant glycosidase show only transferase activity, and no hydrolytic activity is shown by either mutant glycosyltransferase or mutant glycosidase. Thus, unlike non-mutated glycosyltransferases and / or non-mutated glycosidases, the mutated glycosyltransferases and / or mutated glycosidases do not have the adverse reverse hydrolysis of new classes of polysaccharides to oligosaccharides, or acceptors of transfer reactions It converts oligosaccharides to a new class of polysaccharides without the water acting as a.

[0025] These mutant glycosyltransferases and / or mutant glycosidases can be extracted from plants, yeast, bacteria or other organisms. The DNA for the mutant glycosyltransferase and / or mutant glycosidase is thus obtained and cloned and expressed in bacteria, yeast or fungi. These mutant glycosyltransferases and / or mutant glycosidases can be used in heavy liquid detergents,
It can be incorporated into heavy granular detergents, fabric care compositions and the like. The novel features and properties of mutant glycosyltransferases and / or mutant glycosidases make them highly suitable for use in laundry detergents and fabric care compositions because the lack of hydrolytic activity makes the donor enzyme of the transferase reaction ineffective. This is because loss of tensile strength of the fabric does not occur even in the presence. When a mutant glycosyltransferase and / or mutant glycosidase is present in a composition of the present invention, the sugar concentration in the composition may be from about 0.01 to 30% by weight of the total composition, more preferably from 1 to 10% of the total composition. % By weight. Further, in the composition of the present invention, a high molecular weight saccharide may be added to the composition in order to obtain the above-mentioned effects.

Other enzymes of particular interest are described in J. Plant Res. 108, 137-148, 1995, Nishitani, K.
agoma University, Int.Review of Cytology, Vol. 173, p. 157, 1997,
Endoxyloglucan transferase ("EXT"), currently referred to as "EXGT" at Nishitani, Kagoma University, and Novo Nordisk patent application WO
Xyloglucan endotransglycosylase "described in US Pat.
XET ". Like the mutant glycosyltransferases described above, this endoxyloglucan transferase improves the tensile strength and appearance of fabrics, for example, reduces fabric wrinkles, enhances shape retention, and reduces shrinkage. Glucan transferase repairs cellulosic fibrils, these patching properties of the enzymes in the cellulose fibrils have the above effects Endoxyloglucan transferase is responsible for the xyloglucan chains between the cellulose fibrils during the formation of the plant cell wall, i. It is involved in recombining the xyloglucan chains.By recombining the cellulosic fibrils with xyloglucan bonds, the cellulosic structure results in improved strength of the fibers. The enzyme is mending with fine fibers The has. Shape retention,
Anti-shrink and anti-wrinkle effects are also explained by the mending properties of the enzyme.

Endoxyloglucan transferase is available from Novo Nordisk A / S WO97 /
Xyloglucan endotransglycosylase described in 23683 (“XE
T transferase ") differs in activity. The difference is that xyloglucan endotransglycosylase exhibits both transferase and hydrolase activity. Conversely, endoxyloglucan transferase exhibits only transferase activity. Is not indicated by an endoxyloglucan transferase. Thus, unlike xyloglucan endotransglycosylase, endoxyloglucan transferase converts oligosaccharides to a new type without the adverse reverse hydrolysis of a new class of polysaccharides to oligosaccharides. In addition, endoxyloglucan transferase exhibits stringent donor specificity for high Mr (molecular weight) xyloglucan polymers, It does not act on the over.

[0028] The novel features and properties of endoxyloglucan transferase make it highly compatible for use in laundry detergents and fabric care compositions, since the absence of a donor in the transferase reaction will increase the This is because there is no loss in tensile strength. In addition, low levels of substrate donor can be used. Without being bound by theory, it is believed that if the endoxyloglucan transferase uses xyloglucan on the main wall of the cotton fiber in the fabric, a high effect is obtained even in the absence of a donor substrate. Endoxyloglucan transferase can be extracted from plants and other organisms. Endoxyloglucan transferase includes, but is not limited to, A. thaliana
And from a number of plants, including V.angularis. On the other hand, the DNA of the enzyme
Can be cloned and expressed in bacteria, yeast or fungi and thus obtained. Endoxyloglucan transferase is a heavy liquid detergent, heavy granular detergent,
It can be incorporated into fabric care compositions and the like. When an endoxyloglucan transferase is present in the composition of the present invention, the concentration of xyloglucan in the composition may range from about 0.01 to 30% by weight of the total composition,
More preferably, it is 1 to 10% by weight of the total composition. Further, in the composition of the present invention, a high-molecular-weight xyloglucan polymer may be added to the composition to obtain the above-mentioned effects.

Yet another enzyme of particular interest is cyclomaltodextrin glucanotransferase (“CGTase”) (EC 2.4.1.19), commercially available from Amano and Novo Nordisk A / S. Covalent attachment of carbohydrates, oligos and polysaccharides to cotton surfaces, such as fabrics, by transferases has effects such as anti-wrinkle, color retention, dye fixation and stain removal. The covalent attachment of glucose units to the cellulose surface on the physical absorption of the polymer, generated in situ by the transferase (or other), prolongs the observed effect. Cyclomaltodextrin glucanotransferase is a transferase that exhibits several different actions on starch. It produces α, β and γ-cyclodextrin from starch, hydrolyze starch and crosslink the starch. In these reaction types, the alpha sugar is both a donor and an acceptor for the transferase reaction. Until now, it was unknown whether these transferase enzymes could covalently link sugar units to cotton. Surprisingly, it has been found that cyclomaltodextrin glucanotransferase can covalently link glucose units from α-cyclodextrin to the cotton surface of the fabric at the non-reducing end of the cellulose polymer. Therefore, cyclomaltodextrin glucanotransferase has the ability to prolong the above effects.

As described above, when a cellulose polymer is covalently bonded with a cross-linking agent, an effect such as an anti-wrinkle effect is exerted on a fabric. Are known. This physical absorption of the polymer at the cotton surface makes it more durable because one of the polymer units is covalently attached to the cotton surface by the action of cyclomaltodextrin glucanotransferase. Because these longer-lasting effects are obtained enzymatically and covalent bonds occur at much lower temperatures, much lower temperatures can be used in the wash cycle compared to conventional wash cycles. In addition, the cross-linking chemicals commonly used in the textile industry, some of which may be toxic, cannot be used at low temperatures in the wash cycle. Other effects, such as dye fixation and improved soil release, are obtained by covalent attachment of cationic or anionic glucose units to the cotton surface. Thus, the use of cyclomaltodextrin glucanotransferase in laundry detergents and fabric care compositions provides improved anti-wrinkle, shape retention, anti-shrinkage, dye fixation, stain elimination and tensile strength effects for fabrics. Cyclomaltodextrin glucanotransferase can be incorporated into heavy liquid detergents, heavy granular detergents, fabric care compositions and the like. When cyclomaltodextrin glucanotransferase is present in the composition of the present invention, the starch concentration in the composition may range from about 0.01 to 30% by weight of the total composition, more preferably 1 to 10% by weight of the total composition. It is desirable that Furthermore,
In the composition of the present invention, a cyclodextrin or a type of starch and sucrose may be added to the composition to obtain the above-mentioned effects.

Yet another group of enzymes of particular interest is glucansucrase, of which dextransucrase (EC 2.4.1.5) and glycosyltransferases are examples. Other glucansucrases suitable for use in the compositions described herein include, but are not limited to, various dextransuclases, alternan sucrase, and levansucrase (commercially available from Genencor).

The dextran sucrase enzyme may be obtained from any suitable source known in the art and is used in combination with a suitable substrate (sucrose +/- maltose). Dextransclase catalyzes the transfer of glycosyl residues between polysaccharides. As a result of the dextran sucrase reaction, high molecular weight dextran is produced on the fabric surface. In dextran, glucose residues are linked by 1,6-α bonds. Modification of cotton fibers with carbohydrates, oligos and polysaccharides prevents wrinkles, preserves color,
It has effects such as dye fixing and stain removal. Sustaining these effects may require covalent attachment of oligosaccharides.

Dextran sucrase has been shown to be able to link oligosaccharides to cotton cellulose polymers. This conjugation by a dextran sucrase-catalyzed transfer reaction results in improved fabric appearance effects, i.e., improved anti-wrinkle, shape retention, anti-shrinkage, color retention, dye fixation, stain rejection and tensile strength effects. . When the reaction products are bound to the cotton (whether or not covalently), they modify the cotton surface and fibrils to provide the fabric care benefits described above. Dextransucrase, together with sucrose, also provides an improved whitening effect (dye from other colored garments does not adhere to white fabric). The dextran sucrase / sucrose combination forms high molecular weight dextran (and smaller oligomers when other sugars such as maltose, cellobiose, etc. are present). Furthermore, it was found that the adhesion of the reaction product to the fabric was high and the reaction product was not washed off in the next washing cycle.

When glucansucrase is present in the composition of the present invention, the concentration of the substrate (typically sucrose or other disaccharide) in the composition is about 0.01 to 3 of the total composition.
It is preferably 0% by weight, more preferably 1 to 10% by weight of the total composition. Further, in the composition of the present invention, sucrose, maltose,
Smaller polysaccharides may be added to the composition, such as maltodextrin, cellosaccharides and starch types.

[0035] These modified transferase enzymes are preferably present in 0.000% of the total composition.
1-10% by weight, more preferably 0.0005-5%, most preferably 0.005%
At a pure modified enzyme level of 1 to 1%, it is incorporated into a laundry detergent and / or fabric care composition according to the present invention.

[0036] Fabric care and / or cleaning benefits are obtained with the laundry detergent and / or fabric care compositions of the present invention in the presence or absence of the corresponding natural enzyme substrate. In general, the first part of the enzyme name indicates the substrate for the enzymatic reaction, and the second part is the acceptor from which the group is transferred. The substrate for the transferase enzyme is added during the textile industry and / or during any treatment, including before or after treatment of the washing and / or fabric care processes, and / or is added with the transferase-containing composition. There are also stains and / or stains on the fabric fibers themselves. Examples of substrates suitable for some of the above transferases are S-adenosyl-L-methionine, 5,10-methylenetetrahydrofolate or formiminotetrahydrofolate (a hydroxymethyl or formyl group transfers to glycine), formaldehyde, acetyl-CoA , Methyl-α, ω-diamine, palmityl CoA, and geranoyl diphosphate. In particular, substrates for aminoacyltransferases are amino-containing compounds such as amino acids, di / tri / polypeptides and / or proteins.

In glycosyltransferases, the transfer group is a glycosyl residue, but specific examples of substrates for each enzyme are known from the first part of the name. In the case of glycosyltransferases in particular, the natural substrate may be any α-glucosyl sugar selected from dimeric, oligomeric and / or polymeric starchy substances. Examples are preferably different forms of starch (gelatinized, liquefied, solubilized), partial starch hydrolysates, more preferably malt oligosaccharides, most preferably maltose. Substituted starch / sugar substrates, including methylated and carboxylated substitutions, are also of interest. On the other hand, the following substrates can also be used for the glycosyltransferases: dextrin, sucrose, raffinose, fructosyl polymer, UDP glucose, xyloglucan, GDP glucose, arylamine, UDP galacturonic acid, ADP glucose, indole-3-acetic acid, α-D- Glucan, UDP-
Xylan.

The transferase substrate preferably comprises from 0.01 to 30% by weight of the total composition,
More preferably at a level of 0.1-20%, most preferably 1-10%, is incorporated into the composition according to the invention.

The above enzymes may be of any suitable origin, such as plant, animal, bacterial, fungal and yeast sources. The origin may also be mesophilic or extremophilic (cryophilic, eutrophic, thermophilic, barophilic, alkaline, acidophilic, halophilic, etc.). Purified or unpurified forms of these enzymes may also be used. At present, it is customary to modify wild-type enzymes by protein / gene engineering techniques to maximize performance efficacy with the cleaning compositions of the present invention. For example, variants are designed to increase the compatibility of the enzyme with the common components of such compositions. On the other hand, the optimal pH of the enzyme variant
Variants may be designed such that the bleed and / or chelant stability, catalytic activity, etc., are tailored for a particular fabric conditioning and / or cleaning application.

In particular, attention should be paid to amino acids that are susceptible to oxidation in terms of bleach stability and surface charge in terms of surfactant compatibility. The isoelectric point of such enzymes may be modified by substitution of some charged amino acids, for example, increasing the isoelectric point helps to improve compatibility with anionic surfactants. Enzyme stability may be further enhanced, for example, by forming additional salt bridges and reinforcing metal binding sites to increase the stability of the chelant.

The catalytically active amino acid sequence of the transferase enzyme may comprise or consist of all—or substantially all—of the entire amino acid sequence of the mature enzyme in question, or may be a catalyst substantially similar to the entire sequence ( (Enzyme) Consists of a part of the entire sequence that retains its properties.

A detailed description of modifying enzymes of the type in question (enzyme hybrids) and their production and purification is known in the art [eg WO 90/00609.
WO 94/24158 and WO 95/16782, and Greenwood et al.
, Biotechnology and Bioengineering , 44 (1994) pp. 1295-1305]. The preparation of enzyme hybrids is described in WO 91/10732, in which Bacillus NIC
Combining a core region derived from B40250 endoglucanase with CBD derived from another cellulase enzyme, or combining a core region derived from another cellulase enzyme with CBD derived from Bacillus NICB 40250 endoglucanase, Novel derivatives of cellulase enzymes have been constructed. WO95 / 1678
2 shows different core regions and several Cs in Trichoderma longibrachiatum.
It describes the combination with BD and the cloning and high level expression of these novel truncated cellulase proteins or derivatives thereof.

They comprise, for example, a DNA construct in a host cell which is composed at least of fragments of the DNA coding for the cellulose-binding domain, linked with or without a linker to the DNA sequence coding for the enzyme of interest. And the transformed host cells are grown to express the fusion gene. The result is-commonly referred to in the art as a "fusion protein"-without limitation.
One related type of recombinant product (enzyme hybrid) is described by one of the following general formulas: A-CBD-MR-X-B A-X-MR-CBD-B Is an amino acid sequence containing at least the cellulose binding domain (CBD) itself; the MR (intermediate region; connecting region)
It may be a linking group consisting of about 100 amino acid residues, especially 2 to 40 amino acid residues, for example 2 to 15 amino acid residues. The MR may in principle be a non-amino acid linker instead (see below). X is an amino acid sequence containing the above-described catalytic (enzymatic) activity sequence of the amino acid residue of the polypeptide encoded by the DNA sequence encoding the transferase enzyme of interest. Parts A and B are independently optional. When present, portion A or B constitutes a terminal extension of the CBD or X portion and usually contains one or more amino acid residues.

Thus, it will be clear from the above that, in particular, the CBD in the enzyme hybrid of the type in question is located at the C-terminus, N-terminus or inside of the enzyme hybrid. Similarly, the X portion in an enzyme hybrid of the type in question is located at the N-terminus, C-terminus or inside the enzyme hybrid.

In the context of the present invention, an enzyme hybrid of interest includes, for example, two or more CBDs directly linked to each other or a spacer or linker sequence (typically consisting of a sequence of amino acid residues of appropriate length) There are enzyme hybrids with two or more CBDs, separated from each other by: The two CBDs in an enzyme hybrid of the type in question may be separated from one another, for example by an -MR-X- moiety, as described above. One or more cellulose binding domains may be linked to the N-terminal and / or C-terminal portion of the cellulase core region. Any part of the CBD can be selected, modified, trimmed, etc.

Preferably, care is taken in the construction of enzyme hybrids of the type in question with regard to stability against proteolysis. Two- and multi-domain proteins are particularly susceptible to proteolytic cleavage of the linker region connecting the domains. Proteases that cause such cleavage include, for example, subtilisins, which are well known to exhibit broad substrate specificity (see, for example, Gron et al., Biochemistry , 31 (
1992), pp. 6011-6018; Teplyakov et al., Protein Engineering , 5 (1992), pp. 413-
420). Glycosylation of linker residues in eukaryotes is one natural way to prevent proteolysis. Another is to use amino acids that are less preferred by peripheral proteases. The length of the linker also plays a role related to accessibility by the protease. Which “solution” is best depends on the environment in which the enzyme hybrid should function. When constructing new enzyme hybrid molecules, attention is preferably paid to linker stability.

Plasmids Methods for producing plasmids capable of expressing a fusion protein having an amino acid sequence derived from a polypeptide fragment of two or more polypeptides are well known in the art (eg, WO
90/00609 and WO 95/16782). The expression cassette may be introduced into a replication system for episomal maintenance in a suitable cellular host, or may be provided without a replication system and integrate it into the host genome. The DNA may be introduced into a host according to known techniques such as transformation, microinjection and the like.

[0048] Once the fusion gene has been introduced into a suitable host, the host is propagated to express the fusion gene. Usually, it is further desirable to add a signal sequence that allows secretion of the fusion gene. Typical examples of useful genes are: 1) signal sequence-(propeptide)-carbohydrate binding domain-linker-
The enzyme sequence of interest, or 2) the signal sequence- (propeptide) -enzyme sequence of interest-linker-carbohydrate binding domain, wherein the propeptide sequence usually comprises 5 to 100, for example 5 to 25, amino acid residues. Contains. The recombinant product may be glycosylated or non-glycosylated.

Cellulose Binding Domain (CBD) In this context, the term “amino acid sequence containing CBD, cellulose binding domain or CBD” is meant to indicate an amino acid sequence that can bind cellulase to a cellulose substrate (eg, P .Kraulis et al., Determination of the
three-dimensional structure of the C terminal domain of cellobiohydrolas
e I from Trichoderma reesei.A study using nuclear magnetic resonance and
hybrid distance geometry-dynamically simulated annealing (Trichoderma r
Determination of the three-dimensional structure of the C-terminal domain of cellobiohydrolase I from eesei. Nuclear magnetic resonance and hybrid distance geometry-studies using dynamic simulated annealing). As described in Biochemistry, 28: 7241-7257, 1989).
The classification and properties of the cellulose binding domain are described in P. Tomme et al., The symposium “E.
nzymatic degradation of insoluble polysaccharides ”(ACS Symposium Series 618, edited by JNSaddler and MHPenner, ACS
, 1995).

Cellulose binding (and other carbohydrate binding) domains are typically composed of a catalytic domain containing an active site for substrate hydrolysis and a carbohydrate binding domain for binding to the carbohydrate substrate in question, especially hydrolysis In an enzyme (hydrolase), a polypeptide amino acid sequence present as an endogenous part of a large polypeptide or protein consisting of two or more polypeptide amino acid sequence regions.
Such enzymes include two or more catalytic domains and one or two or three carbohydrate binding domains, which may further include one or more polypeptide amino acid sequence regions linking the carbohydrate binding domain to the catalytic domain; The latter type of region is commonly referred to as a "linker."

Examples of hydrolases having a cellulose binding domain are cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. "Cellulose binding domain" refers to algae such as the red alga Porphyra purpu
rea in the form of a non-hydrolysable polysaccharide-binding protein [P. Tomme et al.
., Cellulose-binding domains-Classification and Properties in Enzymatic Degradation of Insoluble Carbohydrates , John N. Saddler and Michael H.
Penner (Eds.), ACS Symposium Series, No. 618 (1996)]. However,(
Most of the known CBDs (classified and referred to by P. Tomme et al. (Supra) as "cellulose binding domains") are derived from cellulases and xylanases.

In this context, the term “cellulose binding domain” is referred to in the latter document (P. To
mme et al., supra). P. Tomme et al. Classify more than 120 “cellulose binding domains” into 10 families (IX), which may have different functions or roles with respect to the mechanism of substrate binding. However, it is anticipated that new family examples and additional families will appear in the future.

In proteins / polypeptides in which CBD is present (eg, enzymes, typically hydrolases such as cellulases), the CBD is at the N and C termini or is internal. The portion of the polypeptide or protein (eg, hydrolase) that makes up the CBD itself typically consists of about 30 or more and less than about 250 amino acid residues. For example, the CBD listed and classified in Family I by P. Tomme et al (supra) consists of 33-37 amino acid residues, the one listed and classified in Family IIa consists of 95-108 amino acid residues, One listed and classified in VI consists of 85-92 amino acid residues, whereas one CBD listed and classified in Family VII (derived from cellulase from Clostridium thermocellum) consists of 240 amino acid residues. Therefore, the molecular weight of the amino acid sequence constituting CBD itself is typically in the range of about 4 to about 40 kD, usually about 35 kD or less.

The cellulose binding domain is described in H. Stalbrand et al., Applied and Environmental
Microbiology, Mar. 1995, pp. 1090-1097; E. Brun et al., (1995) Eur. J. Biochem.
231, pp. 142-148; JBCoutinho et al., (1992) Molecular Microbiology, 6 (9), p.
It can be made by recombinant techniques as described on pages 1243-1252.

Several genetic engineering approaches can be used, for example, to isolate the cellulose binding domain of cellulase. In one method, a portion of the gene is removed using restriction enzymes, and the remaining gene-vector fragment is then fused in frame to obtain a mutant gene encoding a protein truncated for a particular gene fragment.
In another method, Ba131 is used to systematically delete nucleotides outside the 5 'and 3' ends of DNA or inside restriction gaps in genes.
With the use of exonucleases such as These gene deficiency methods result in a mutant gene encoding a truncated gene molecule whose expression product binds to a substrate (eg,
Cellulose binding) ability is evaluated. Suitable substrates for assessing binding capacity include cellulosic materials such as Avicel ^™ and cotton fiber. Other substances include CBD, such as terminal CB, from the rest of the polypeptide chain of the protein in question.
There is the use of selective or specific proteases that can cleave D.

As already indicated (above), once the nucleotide sequence encoding the substrate-binding (carbohydrate-binding) region has been identified as cDNA or chromosomal DNA, it is the DNA encoding the enzyme or enzyme-active amino acid sequence of interest. It is manipulated in various ways to fuse it to the sequence. DN encoding a carbohydrate binding amino acid sequence
The A fragment and the DNA sequence encoding the enzyme or enzymatically active amino acid sequence of interest are then ligated with or without a linker. Then, the obtained ligated DNA
Is manipulated in a variety of ways to effect expression. Preferred microbial expression hosts include certain Aspergillus species (eg, A.niger or A.oryzae), Bacillus species, and Es
There are organisms like cherichia coli or Saccharomyces cerevisiae.

A preferred CBD for the purposes of the present invention is CBD C from Trichoderma reesei.
BHII, CBD from Cellulomonas fimi CenC, CenA and Cex, T
CBD CBHI from richoderma reesei, CBD Cellulozome from Clostridium cellulovorans, CBD E3 from Thermonospora fusca, Clostridium s
tecorarium (NCIMB11754) CBD dimer from XynA, Bacillus agaradheren
s (NCIMB40482), and / or CBD family 45 from Humicola insolens. More preferred CB for the purpose of the present invention
D is CBD CenC from Cellulomonas fimi, Clostridium cellulovorans
CBD from Cellulozome and / or Novo Nordisk A / S under the trade name “Carezy
CBD from the fungus Humicola insolens cellulase sold under "me". C
arezyme has a molecular weight of about 43 kDa and exhibits cellulolytic activity.
ola insolens A family 45 endoglucanase derived from DSM1800.

The term [0058] consolidated area "linker", "connecting area" or "intermediate region -MR" is, CBD
Adjacent to the amino acid sequence of the transferase enzyme. When present, this ligation can be performed chemically or by recombinant techniques.

Examples of recombinant techniques that describe the expression of enzymes with different origins of CBD include:
S. Karita et al., (1996) Journal of Fermentation and Bioengineering, Vol. 81
, No. 6, pp. 553-556. A preferred connecting region is an amino acid connecting region (peptide), some examples of which are described in N, R. Gilkes et al., Microbiol. Rev. 55, 1991, pp.
.303-315. The connecting region is from 1 to about 100 amino acid residues, especially from 2 to
It consists of 40 amino acid residues, for example 2 to 15 amino acid residues. As described above,
It is preferable to use amino acids that are less preferred by peripheral proteases. Suitable amino acid linking regions are Humicola insolens family 45 cellulase linker, Klebs
NifA gene of iella pneumoniae-CiP linker, E. coli OmpA gene-
CiP linker, E3 cellulase Thermonospora fusca linker and CenA
Cellulase linkers, preferably Humicola insolens family 45 cellulase linkers and E3 cellulase Thermonospora fusca linker.

Non-amino acid / protein compounds referred to as “non-amino acids” can also be used to link catalytically active amino acid sequences to CBD: 1) Suitable non-amino acid linking regions are described in Shearwater polymers, Inc., January 1996.
Polyethylene glycol derivatives described in catalogs such as nucleophilic PEG, carboxyl PEG, electrophilic activated PEG, sulfhydryl selective PEG, heterofunctional PEG, biotin PEG, vinyl derivatives, PEG silane and PEG phospholipid. In particular, suitable non-amino acid linking regions include heterofunctional PEG, Shearw
(X-PEG-Y) polymers from ater, such as PEG (NPC) 2, PEG-
(NH2) 2, t-BOC-NH-PEG-NH2, t-BOC-NH-PEG
-CO2NHS, OH-PEG-NH-tBOC, FMOC-NH-PEG-C
O2NHS or PEG (NPC) ₂ , MW3400 from Sigma, glutardialdehyde in water 50% solution from Aldrich, disuccinimidyl suberate (DSS) from Sigma, γ-maleimidobutyric acid N-hydroxysuccinimide ester from Sigma (GMBS), 1-ethyl-3- (3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) from Sigma and dimethylsuberimidate hydrochloride (DMS) from Sigma. 2) Other suitable non-amino acid linking regions are 1-ethyl-3- (3-dimethylaminopropyl) carbodiimide, N-ethyl-5-phenylisoxazolium-3-
Sulfonate, 1-cyclohexyl-3- (2-morpholinoethyl) carbodidomet-p-toluenesulfonate, N-ethoxycarbonyl-2-ethoxy-1
, 2-dihydroquinoline or glutaraldehyde. 3) Crosslinkers described under the heading "Crosslinking reagents" in the Pierce Company's 1999/2000 Pierce Products Catalog: SMPH, SMCC, LC-SM
Also suitable are CC compounds, preferably Sulfo-KMUS compounds. Preferred chemical linking regions are PEG (NPC) 2, (NH2) from Shearwater
2-PEG, t-BOC-NH-PEG-NH2, MAL-PEG-NHS, V
S-PEG-NHS polymer and / or Sulfo-KMUS compound from Pierce.

Detergent Components The laundry detergent and / or fabric care compositions of the present invention include at least one additional detergent and / or fabric care component. The exact nature of these additional components, and their level of incorporation, will depend on the physical form of the composition and the nature of the cleaning operation in which it is used.

The laundry detergent and / or fabric care composition of the present invention preferably comprises a surfactant selected from nonionic and / or anionic and / or cationic and / or mixtures thereof, other detergent enzymes , Bleaching agents, dye transfer inhibiting polymers, dispersants and / or detergent components selected from smectite clays.

The laundry detergent and / or fabric care compositions according to the present invention include liquids, pastes,
There are gel, bar soap, tablet, spray, foam, powder or granule form. Granular compositions may be in "compact" form, and liquid compositions may be in "concentrated" form.

The compositions of the present invention include, for example, hand and machine laundry detergent compositions, such as laundry liquor-added compositions and compositions suitable for soaking and / or pretreating soiled fabrics, rinsing liquor-added fabric softeners. It may be formulated as a composition. Before or after treatment of the fabric,
There are gel, spray and liquid fabric care compositions. Rinse cycles in the presence or absence of a softener are also contemplated.

When formulated as a composition suitable for use in a machine washing method, the composition of the present invention preferably comprises both a surfactant and a builder compound, and preferably an organic polymeric compound, a bleach, It further contains one or more detergent components selected from enzymes, foam inhibitors, dispersants, lime soap dispersants, soil suspending and redeposition inhibitors, and corrosion inhibitors. Laundry compositions can also contain softening agents as additional detergent components.

The composition of the present invention can also be used as a detergent additive product in solid or liquid form. Such additive products are to reinforce or enhance the performance of conventional detergent compositions,
It can be added at any stage of the cleaning process. If necessary, the density of the laundry detergent composition may be 400 for the composition measured at 20 ° C.
To 1200 g / L, preferably 600 to 950 g / L.

The “compact” form of the composition is best reflected in terms of density and composition in terms of the amount of inorganic filler salt; inorganic filler salts are a conventional component of detergent compositions in powder form; In some detergent compositions, the filler salt is present in a substantial amount, typically one part of the total composition.
It is present at 7-35% by weight. In a compact composition, the filler salt is one part of the total composition.
Not more than 5% by weight, preferably not more than 10% of the composition, most preferably not more than 5%
It is present in an amount not exceeding%. The inorganic filler salts as meant in the present composition are selected from the alkali and alkaline earth metal salts of sulfates and chlorides. A preferred filler salt is sodium sulfate.

The liquid detergent composition according to the invention may be in “concentrated form”, in which case the liquid detergent composition according to the invention contains a small amount of water compared to conventional liquid detergents. Typically, the water content of the concentrated liquid detergent is preferably less than 40% by weight of the detergent composition, more preferably less than 30%, and most preferably less than 20%.

Surfactant System Preferably, the laundry detergent and / or fabric care composition according to the present invention comprises a surfactant wherein the surfactant can be selected from nonionic and / or anionic and / or cationic surfactants. Contains the system usually.

In the presence of an anionic surfactant, the modified transferase and at least 5% of anionic surfactant, especially alkyl sulfate, alkyl ethoxy sulfate, and linear alkylene sulfonate and / or at least 2%
In combination with nonionic and / or cationic surfactants of the alkyl ethoxylate type provide improved tensile strength, improved anti-wrinkle, anti-shrinkage and anti-pilling properties to fabrics, renewal or It has been surprisingly found that it recovers and provides improved static control, fabric softness, color appearance and fabric abrasion resistance properties and effects. Furthermore, an improved cleaning effect is also achieved with the above combination.

[0071] Surfactants are typically present at a level of 0.1 to 60% by weight. More preferred formulation levels are 1-3 of the laundry detergent and / or fabric care compositions according to the invention.
It is 5% by weight, most preferably 1 to 30% by weight.

[0072] The surfactant is preferably formulated to be compatible with the enzyme components present in the composition. In liquid or gel compositions, the surfactant may be formulated to promote the stability of the enzyme in these compositions or to not degrade it at least.
Most preferred.

Polyethylene, polypropylene and polybutylene oxide condensates of alkylphenols are suitable for use as the nonionic surfactant of the surfactant system of the present invention, with polyethylene oxide condensates being preferred. These compounds include condensation products of alkyl phenols with alkyl phenols having an alkyl group of from about 6 to about 14, preferably from about 8 to about 14, carbon atoms in a straight or branched configuration. In a preferred embodiment, the ethylene oxide is present in an amount corresponding to about 2 to about 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 GAF Cor
There are Igepal ^™ CO-630 sold by poration, all Triton ^™ X-45, X-114, X-100 and X-102 sold by Rohm & Haas Company. These surfactants are commonly referred to as alkylphenol alkoxylates (eg, alkylphenol ethoxylates).

The condensation products of primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl chain of the aliphatic alcohol is straight or branched, primary or secondary, and usually has about 8 to about 22 carbon atoms. About 8 to about 20 carbon atoms
And more preferably an alcohol having an alkyl group of about 10 to about 18 carbon atoms;
Condensation products with from about 2 to about 10 moles of ethylene oxide per mole of alcohol are preferred. About 2 to about 7 moles, most preferably 2 to 5 moles, of ethylene oxide are present in the above condensation product per mole of alcohol. Examples of commercially available nonionic surfactants of this type include both Union Carbide Corporation
Tergitol ^™ 15-S-9 (condensation product of C ₁₁ -C ₁₅ linear alcohol and 9 moles of ethylene oxide) and Tergitol ^™ 24-L-6 NMW (C ₁₂ -C ₁₄ primary alcohol and ethylene oxide 6 Condensation product of narrow molecular weight distribution with mol); Shel
l Chemical Company Neodol sold by ^TM 45-9 _(C 14 _{-C 15} condensation product of linear alcohol with 9 moles ethylene _{^{oxide), Neodol TM 23-3 (C 12}} -C 1 3 linear alcohols with ethylene oxide 3 Condensation product with 2.0 mol), Neodol ^TM 45-7
(Condensation product of C ₁₄ -C ₁₅ linear alcohol and 7 mol of ethylene oxide), Ne
odol ^TM 45-5 _(C 14 _{-C 15} linear alcohol with condensation product of 5 moles of ethylene oxide); The Procter & Gamble Company, sold by _{^{Kyro TM EOB (C 1 3 -C}} 15 alcohol with 9 moles ethylene oxide and there are Genapol sold by Hoechst LA O3O or O50 (C ₁₂ -C ₁₄ alcohols with ethylene oxide 3 or 5 moles and condensation products of); condensation products of). HLB in these products
Is preferably from 8 to 11, and most preferably from 8 to 10.

The nonionic surfactants of the surfactant system of the present invention include hydrophobic groups having about 6 to about 30 carbon atoms, preferably about 10 to about 16 carbon atoms, and about 1.3 to about 10 carbon atoms. ,
Llenado published January 21, 1986, having a polysaccharide having preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units, such as the hydrophilic group of a polyglycoside. Also useful are the alkyl polysaccharides disclosed in US Pat. No. 4,565,647. Reducing sugars having 5 or 6 carbon atoms can also be used, for example, glucose, galactose and galactosyl moieties can be used in place of the glucosyl moiety (optionally a hydrophobic group is attached at the 2, 3, 4 position, etc. Give glucose or galactose instead of galactoside). For example, an intersugar linkage may be present between one position of the additional sugar unit and positions 2, 3, 4, and / or 6 of the preceding sugar unit.

Preferred alkyl polyglycosides have the formula: R ² O (C _n H _2n O) _t (glycosyl) _{x where} R ² is alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl and (Alkyl groups have about 10 to about 18, preferably about 12 to about 14 carbon atoms); n is 2 or 3, preferably 2; t is 0 to about 10, preferably 0; x is about 1
. 3 to about 10, preferably about 1.3 to about 3, most preferably about 1.3 to about 2.7.
It is. Glycosyl is preferably derived from glucose. To make these compounds, an alcohol or alkyl polyethoxy alcohol is first formed and then reacted with glucose or a source of glucose to form glucoside (1).
Bond). Additional glycosyl units may also be linked between their 1-position and the preceding glycosyl unit at positions 2, 3, 4, and / or 6, preferably predominantly at position 2.

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 nonionic surfactant system of the present invention. The hydrophobic portion of these compounds is preferably about 1500
It has a molecular weight of ~ 1800 and is water-insoluble. The addition of a polyoxyethylene moiety to this hydrophobic moiety tends to increase the overall water solubility of the molecule, and the liquidity of the product is such that the polyoxyethylene content is up to about 50% of the total weight of the condensation product. Again, this corresponds to condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain commercial Plurafac ^™ LF404 and Pluronic ^™ surfactants, sold by BASF.

As the nonionic surfactant of the nonionic surfactant system of the present invention, a product obtained from the reaction of propylene oxide with ethylenediamine and a condensation product of ethylene oxide are also suitable for use. The hydrophobic portion of these products consists of the reaction product of ethylenediamine and excess propylene oxide, usually from about 2500 to about 300
It has a molecular weight of 0. The hydrophobic moiety is condensed with ethylene oxide to an extent that the condensation product contains about 40 to about 80% by weight polyoxyethylene and has a molecular weight of about 5000 to about 11,000. Examples of this type of nonionic surfactant include certain commercially available Tetronic ^™ compounds sold by BASF.

The nonionic surfactants of the surfactant system of the present invention include polyethylene oxide condensates of alkylphenols, primary and secondary aliphatic alcohols and about 1 to about 25
Condensation products with moles of ethylene oxide, alkyl polysaccharides, and mixtures thereof are preferred for use. _C 8 _{-C 14} alkyl phenol ethoxylates having from 3 to 15 ethoxy groups, _C 8 _{-C 18} alcohol ethoxylates having from 2 to 10 ethoxy groups (preferably _{C 10} average), and mixtures thereof are most preferred.

Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula:

Embedded image Or the formula ^{R 1} is H, or ^{R 1} is C _1-4 hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl or a mixture thereof, ^{R 2} is C _5-31 hydrocarbyl, Z is A polyhydroxyhydrocarbyl having a linear hydrocarbyl chain and at least three hydroxyls directly attached to the chain, or an alkoxylated derivative thereof. Preferably, R ¹ is methyl, R ² is a linear C _11-15 alkyl or C _16-18 alkyl or alkenyl chain, such as coconut alkyl, or mixtures thereof, and Z is glucose,
It is derived from reducing sugars such as fructose, maltose and lactose.

Suitable anionic surfactants used are described in “The Journal of the American O.
il Chemists Society ", 52 (1975 ), C 8 -C 20 carboxylic acids which are sulfonated with gaseous SO ₃ according Pp.323-329 (i.e., fatty acids), including straight-chain esters of, linear alkylbenzene sulfonates, alkyl Ester sulfonate surfactants Suitable starting materials include natural fatty substances such as those derived from tallow, palm oil and the like.

Particularly preferred alkyl ester sulfonate surfactants for laundry applications include:
There are alkyl ester sulfonate surfactants of the following structural formula:

Embedded image Wherein R ³ is C ₈ -C ₂₀ hydrocarbyl, preferably alkyl, or a combination thereof, R ⁴ is C ₁ -C ₆ hydrocarbyl, preferably alkyl, or a combination thereof, and M is an alkyl ester sulfonate. Is a cation that forms a water-soluble salt with the cation. Suitable salt-forming cations include metals such as sodium, potassium and lithium, substituted or unsubstituted ammonium cations, for example, monoethanolamine, diethanolamine and triethanolamine. Preferably, R ³ is C ₁₀ -C ₁₆ alkyl and R ⁴ is methyl, ethyl or isopropyl. Methyl ester sulfonates where R ³ is C ₁₀ -C ₁₆ alkyl are particularly preferred.

Other suitable anionic surfactants include those of the formula ROSO₃With a water-soluble salt or acid of M
There are certain alkyl sulphate surfactants, where R is preferably C₁₀-C ₂₄ Hydrocarbyl, preferably C₁₀-C₂₀Alkyl with alkyl moiety
Or hydroxyalkyl, more preferably C₁₂-C₁₈Alkyl or hydrid
M is H or a cation, such as an alkali metal cation (
Eg sodium, potassium, lithium), ammonium or substituted ammonium
(Eg, methyl-, dimethyl- and trimethyl-ammonium cations,
And like tetramethylammonium and dimethylpiperidinium cations
Quaternary ammonium cations and ethylamine, diethylamine, triethyl
Quaternary ammonium cations derived from alkylamines such as
And mixtures thereof). Typically, C₁₂-C₁₆Alkyl chains are low
Low washing temperature (for example, below about 50 ° C.)₁₆-C₁₈Alkyl chains are high
A low cleaning temperature (eg, about 50 ° C. or higher) is preferred.

[0084] Other anionic surfactants useful for cleaning purposes can also be included in the laundry detergent and / or fabric care compositions of the present invention. These include salts of soaps (including, for example, sodium, potassium, ammonium and substituted ammonium salts such as mono, di and triethanolamine salts), C ₈ -C ₂₂ primary or secondary alkane sulfonates, C ₈ -C _24. olefin sulfonates, for example the United Kingdom, as described in patent specification No. 1,082,179, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, C ₈ -
C ₂₄ (including within 10 moles ethylene oxide) alkyl polyglycol ether sulfates, alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphate, isethionates such as the acyl isethionates , N- acyl taurates, alkyl succinate cinnamate and sulfosuccinates, monoesters (especially saturated and unsaturated C ₁₂ -C ₁₈ monoesters) sulfosuccinates and sulfosuccinate diesters (especially saturated and unsaturated C ₆ -C ₁₂ diesters), acyl sarcosinates, alkyl polysaccharides such as sulfates of alkyl polyglucosides Rufeto (nonionic non sulfate compound are described below), branched primary alkyl sulfates, and the formula _{RO (CH 2 CH 2 O)} k -CH 2 COO - M + (R is an _C 8 _{-C 22} alkyl , K is an integer from 1 to 10 and M is a soluble salt-forming cation). Resin acids and hydrogenated resin acids, such as rosins, hydrogenated rosins, resin acids and hydrogenated resin acids, which are present in or derived from tall oil, are also suitable.

Another example is “Surface Active Agents and Detergents” (Vol. I and II, Schwar
tz, Perry and Berch). Various such surfactants include 19
US Pat. No. 3,929,678 to Laughlin et al., Issued Dec. 30, 75, also commonly discloses at column 23, line 58 to column 29, line 23 (herein incorporated by reference). Incorporated).

As included herein, the laundry detergent compositions of the present invention typically contain from about 1 to about 40% by weight, preferably from about 3 to about 20%, of such an anionic surfactant. I have.

Highly preferred anionic surfactants include alkylalkoxylated sulfate surfactants that are water-soluble salts or acids of the formula RO (A) _m SO ₃ M, where R is an unsubstituted C ₁₀ − C ₂₄ alkyl or _C 10 _{-C 24} hydroxyalkyl group having an alkyl moiety, preferably a _C 12 _{-C 20} alkyl or hydroxyalkyl, more preferably _C 12 _{-C 18} alkyl or hydroxyalkyl, a is an ethoxy or propoxy unit And m is greater than zero, typically from about 0.5 to about 6, more preferably from about 0.5 to about 3, and M is H or a cation, such as a metal cation (eg, sodium, potassium, lithium , Calcium, magnesium, etc.), ammonium or substituted ammonium cations .
Alkyl ethoxylated sulfates and alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations are derived from methyl, dimethyl, trimethyl-ammonium cations, and quaternary ammonium cations such as tetramethylammonium and dimethylpiperidinium cations, and alkylamines such as ethylamine, diethylamine, triethylamine. And mixtures thereof. An exemplary surfactant is C _12-
C ₁₈ alkyl polyethoxylate (1.0) sulfate (C ₁₂ -C ₁₈ E
(1.0) M), C ₁₂ -C ₁₈ alkyl polyethoxylate (2.25) sulfate (C ₁₂ -C ₁₈ E (2.25) M), C ₁₂ -C ₁₈ alkyl polyethoxylate (3. 0) sulfate _{(C 12 -C 18 E (3.0} ) M) , and _C 12 _{-C 18} alkyl polyethoxylate (4.0) sulfate _{(C 12} -
C ₁₈ E (4.0) M), where M is conveniently selected from sodium and potassium.

The laundry detergent and / or fabric care compositions of the present invention can be used with cationic, amphoteric, zwitterionic and semipolar surfactants, as well as nonionic and / or anionic surfactants other than those already described herein. Agents may also be included.

[0089] Cationic wash suitable for use in the laundry detergents and / or fabric care compositions of the present invention.
A clean surfactant has one long-chain hydrocarbyl group. like this
Examples of cationic surfactants include ammonium surfactants, such as alkyl tris.
There are methyl ammonium halides, and surfactants having the formula:²(OR³)_y] [R⁴(OR³)_y]₂R⁵N⁺X⁻ R in the above formula²Is an alkyl having about 8 to about 18 carbon atoms in the alkyl chain or
An alkylbenzyl group; each R³Is -CH₂CH₂-, -CH₂CH (CH₃ )-, -CH₂CH (CH₂OH)-, -CH₂CH₂CH₂-And their
Selected from the group consisting of mixtures; each R⁴Is C₁-C₄Alkyl, C₁-C₄Hi
Droxyalkyl, two R⁴A benzyl ring structure formed by linking groups, -C
H₂CHOH-CHOHCOR⁶CHOHCH₂OH (R⁶Is less than about 1000
A hexose or hexose polymer having a molecular weight), and y is 0.
If not selected from the group consisting of hydrogen; R⁵Is R⁴Is the same as R ² + R⁵Is an alkyl chain having no more than about 18 carbon atoms; each y is from 0 to about
10, the sum of the y values is from 0 to about 15; X is any suitable anio
It is.

A quaternary ammonium surfactant suitable for the present invention has the following formula (I):

Embedded image Formula I wherein R ₁ is a short chain alkyl (C ₆ -C ₁₀ ) or an alkylamidoalkyl of formula (II):

Embedded image Wherein R ₂ is H or C ₁ -C ₃ alkyl; wherein x is 0-4, preferably 0-2, most preferably Wherein R ₃ , R ₄ and R ₅ are the same or different and are a short-chain alkyl (C ₁ -C ₃ ) or an alkoxylated alkyl of the following formula III:

Embedded image Formula III (where R ⁶ is C ₁ -C ₄ and z is 1 or 2) wherein X ⁻ is a counter ion, preferably a halide such as chloride or methyl sulfate.

Preferred quaternary ammonium surfactants are those of the formula wherein R ₁ is C ₈ , C ₁₀ or a mixture thereof, x = 0, R ₃ , R ₄ ＣＨCH ₃ and R ₅ ＣＨCH ₂ CH ₂ OH. As defined in I.

Highly preferred cationic surfactants are water-soluble quaternary ammonium compounds useful in the present compositions having the formula: R ₁ R ₂ R ₃ R ₄ N ⁺ X ⁻ (i) Wherein R ₁ is C ₈ -C ₁₆ alkyl, and each of R ₂ , R ₃ and R ₄ is independently C ₁ -C ₄ alkyl, C ₁ -C ₄ hydroxyalkyl, benzyl and-
A _{(C 2 H 40) x H} (x has a value of 2 to 5), X is an anion.
No more than one of R ₂ , R ₃ or R ₄ must be benzyl. The preferred alkyl chain length for R ₁ is C ₁₂ -C ₁₅ , especially where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat, or synthetically derived by olefin build-up or oxo alcohol synthesis. Is done. Preferred groups for R ₂ , R ₃ and R ₄ are methyl and hydroxyethyl groups, and the anion X is selected from halide, methosulfate, acetate and phosphate ions.

Examples of quaternary ammonium compounds of the formula (i) suitable for use herein are: coconut trimethylammonium chloride or bromide coconut methyldihydroxyethylammonium chloride or bromide decyltriethylammonium chloride decyldimethylhydroxyethylammonium chloride or bromide C _12-15 dimethyl hydroxyethyl ammonium chloride or bromide coconut dimethyl hydroxyethyl ammonium chloride or bromide myristyl trimethyl ammonium methyl sulphate lauryl dimethyl benzyl ammonium chloride or bromide lauryl dimethyl (ethenoxy) ₄ ammonium chloride or bromide choline esters (R ₁ is CH _{2 -CH 2 -O-C (= O} ) A C _{12-14 alkyl, R 2, R 3, R} 4 is methyl, the compound of formula (i)) compounds of dialkyl imidazoline (Formula (i))

Other cationic surfactants useful herein are Cambre US Pat. No. 4,228,044, issued Oct. 14, 1980 and European Patent Application EP000,20.2
24.

Typical cationic fabric softening components include water-insoluble quaternary ammonium fabric softening activators or their corresponding amine precursors, with dilong chain alkyl ammonium chloride or methyl sulfate being the most commonly used. I have. Among these, preferred cationic softeners include: 1) ditallow dimethyl ammonium chloride (DTDMAC) 2) dihydrogenated tallow dimethyl ammonium chloride 3) dihydrogenated tallow dimethyl ammonium methyl sulfate 4) distearyl dimethyl ammonium Chloride 5) Dioleyldimethylammonium chloride 6) Dipalmitylhydroxyethylmethylammonium chloride 7) Stearylbenzyldimethylammonium chloride 8) Tallow trimethylammonium chloride 9) Hydrogenated tallow trimethylammonium chloride 10) _C12-14 alkyl hydroxyethyldimethylammonium chloride 11) C _12-18 alkyl dihydroxyethyl methyl ammonium chloride 12) di (stearoyl oxyethyl Dimethylammonium chloride (DSOEDMAC) 13) di (tallow oxyethyl) dimethyl ammonium chloride 14) ditallow imidazolinium methylsulfate 15) 1- (2-tallow-ylamide ethyl) -2-tallow-yl imidazolinium methylsulfate

[0096] Biodegradable quaternary ammonium compounds have been provided as an alternative to the traditionally used dilong chain alkyl ammonium chloride and methyl sulfate. Such a quaternary ammonium compound has a long-chain alkyl (alkenyl) group in which a functional group such as a carboxy group is interposed. The above substances and the fabric softening compositions containing them are EP-A-0,040,562 and EP-A-0,
It has been disclosed in numerous documents such as 239,910.

The quaternary ammonium compound and its amine precursor are represented by the following formula (I) or (II)
)have:

Embedded image The formula Q is -O-C (O) -, - C (O) -O -, - O-C (O) -O-, -NR 4 -C (O) -, - C (O) - NR ⁴ - is selected from; ^{R 1} is _{(CH 2)} is n ^{-Q-T 2} or ^{T 3;} is ^{R 2} is _{(CH 2)} m ^{-Q-T 4} or ^{T 5} or ^{R 3,;} R ³ is C ₁ -C ₄ alkyl, C ₁ -C ₄ hydroxyalkyl or H; R ⁴ is H, C ₁ -C ₄ alkyl or C ₁ -C ₄ hydroxyalkyl; T ¹ , T ² , T ³ , T ⁴ , T ⁵ are independently C ₁₁ -C ₂₂ alkyl or alkenyl; n and m are integers from 1 to 4; and X ⁻ is a softener compatible anion. Non-limiting examples of softener compatible anions include chloride or methyl sulfate.

The alkyl or alkenyl chains T ¹ , T ² , T ³ , T ⁴ , T ⁵ are at least 11
And preferably at least 16 carbon atoms.
The chain may be straight or branched. Tallow is a convenient and inexpensive source of long-chain alkyl and alkenyl materials. Compounds in which T ¹ , T ² , T ³ , T ⁴ , T ⁵ represent a mixture of long chain substances typical of tallow are particularly preferred.

Specific examples of quaternary ammonium compounds suitable for use in the present aqueous fabric softening composition include: 1) N, N-di (tallowyloxyethyl) -N, N-dimethylammonium chloride 2) N, N-di (tallowyloxyethyl) -N-methyl, N- (2-hydroxyethyl) ammonium methyl sulfate 3) N, N-di (2-tallowyloxy-2-oxoethyl) -N, N-dimethylammonium Chloride 4) N, N-di (2-tallowyloxyethylcarbonyloxyethyl) -N, N-dimethylammonium chloride 5) N- (2-tallowyloxy-2-ethyl) -N- (2-tallowyl) Oxy-2-oxoethyl) -N, N-dimethylammonium chloride 6) N, N, N-tri (tallowyloxyethyl) -N-methyl Ammonium chloride 7) N- (2-Tallowyloxy-2-oxoethyl) -N- (tallowyl-N, N-dimethylammonium chloride) 8) 1,2-Ditaloyloxy-3-trimethylammoniopropane chloride and There are mixtures of the above substances.

As contained herein, the laundry detergent and / or fabric care compositions of the present invention typically comprise from 0.2 to about 25% by weight, preferably from about 1 to about 8% of such a cationic. Contains a surfactant.

Conventional Detergent Enzymes Laundry detergents and / or fabric care compositions can further include, in addition to the modified transferase enzyme, one or more enzymes that exert cleaning performance, fabric care and / or disinfecting effects. .

The combination of the modified transferases with detergent enzymes-especially proteases, cellulases, lipases and / or amylases-imparts improved tensile strength, improved anti-wrinkle, anti-shrinkage, anti-pilling properties to fabrics, innovation It has been surprisingly found that it provides or better recovery and better static control, fabric flexibility, color appearance and fabric wear resistance. In addition, an improved cleaning effect is also obtained with the above combination.

The above enzymes include cellulase, hemicellulase, peroxidase, protease, glucoamylase, amylase, xylanase, lipase, phospholipase, esterase, cutinase, pectinase, keratanase, reductase,
There are enzymes selected from oxidase, phenol oxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, malanase, β-glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase or mixtures thereof. A preferred combination is a laundry detergent and / or fabric care composition having a cocktail of common enzymes such as proteases, amylases, lipases, cutinases and / or cellulases combined with one or more plant cell wall degrading enzymes. .

Cellulases that can be used in the present invention include both bacterial and fungal cellulases.
Preferably, they have an optimum pH of 5-12 and 50 CEVU (Cellulose Viscosity).
Unit) / mg or more. Suitable cellulases are disclosed in US Pat. Nos. 4,435,307, J61078384 and WO 96/02653 to Barbesgoard et al.
Fungal cellulases each produced from trichum are disclosed. EP739
982 describes a cellulase isolated from a novel Bacillus species. Suitable cellulases are GB-A-2,075,028, GB-A-2,095,275, D
Also disclosed in E-OS-2,247,832 and WO 95/26398. Examples of such cellulases are strains of Humicola insolens (Humicola grisea var.
thermoidea), especially cellulases produced by Humicola strain DSM1800.

Other suitable cellulases have a molecular weight of about 50 kDa, an isoelectric point of 5.5,
Humicola insolens-derived cellulase containing 415 amino acids; a ~ 43 kD endoglucanase derived from Humicola insolens, DSM1800, which exhibits cellulase activity; a preferred endoglucanase component is PCT patent application WO9.
It has the amino acid sequence disclosed in 1/17243. Trichoderma long described in WO94 / 21801 by Genencor, published September 29, 1994.
EGIII cellulases from ibrachiatum are also suitable cellulases. Particularly suitable cellulases are those having a color care effect. Examples of such cellulases are described in European Patent Application 91202879.2, filed November 6, 1991.
(Novo). Carezyme and Celluzyme (Novo Nord
isk A / S) is particularly useful. WO 91/17244 and WO 91/2180
See also 1. Other cellulases suitable for fabric care and / or cleaning properties include:
WO96 / 34092, WO96 / 17994 and WO95 / 24471.

The cellulase described above may be used in laundry detergent and / or fabric care compositions at 0.0001.
At a pure enzyme level of ２2% by weight, it is usually incorporated into laundry detergents and / or fabric care compositions.

The peroxidase enzyme is a source of oxygen such as percarbonate, perborate,
Used in combination with phenolic substrates as persulfate, hydrogen peroxide, and the like, and as a bleach-enhancing molecule. They are used for "solution bleaching", i.e. to prevent dyes or pigments that have fallen off the substrate during the washing operation from migrating to other substrates in the washing liquor. Peroxidase enzymes are known in the art and include, for example, haloperoxidases such as horseradish peroxidase, ligninase, chloro and bromoperoxidase. Peroxidase-containing detergent compositions are described, for example, in PCT International Applications WO 89/099813, WO 89/09.
813 and European Patent Application EP 9120 filed on November 6, 1991
EP 96870013 filed on Feb. 28, 1996 and on Feb. 28, 1996.
. 8 is disclosed. Laccase enzymes are also suitable.

[0108] Enhancers are usually included at levels of 0.1 to 5% by weight of the total composition. Preferred enhancers are the substituted phenothiazines and phenoxazines 10-phenothiazinepropionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-methylphenoxazine (WO94 / 12621), and substituted syringates (
C3-C5 substituted alkyl siline gates) and phenols. Sodium percarbonate or perborate is the preferred source of hydrogen peroxide. The peroxidase is present in the laundry detergent and / or fabric care composition at 0.00
It is usually formulated in laundry detergents and / or fabric care compositions at a pure enzyme level of from 1 to 2% by weight.

Other Preferreds That Can Be Included in the Laundry Detergent and / or Fabric Care Compositions of the Invention
Another enzyme is lipase. Lipase enzymes suitable for detergents include British Patent 1,3.
Such as Pseudomonas stutzeri ATCC 19.154 disclosed in US Pat.
Some are produced by microorganisms of the genus Pseudomonas. Suitable lipases include
Pseudomonas fluorescen showed positive immune cross-reactivity with lipase antibody
t Some are produced by IAM1057. This lipase is trade name Lipase P
 Commercially available as “Amano” from Amano Pharmaceutical Co. Ltd. in Nagoya, Japan
And will be referred to as "Amano-P" hereinafter. Other suitable commercial lipases include Amano-CES,
Chromobacter viscosum, for example Chromobacter vi from Toyo Brewing Co., Ltd.
Lipase from scosum var. lipolyticum NRRLB 3673; U.S. Biochemical of USA
 Chromobacter viscosum lipase from Corp. and Disoiynth Co. of the Netherlands; P
There is a lipase from seudomonas gladioli. A particularly suitable lipase is M1 Lipase ^R And Lipomax^R(Gist-Brocades) and Lipolase^RAnd Lipolase Ultra^R(
Lipases such as Novo), which, when used in combination with the compositions of the present invention,
Was found to be effective. Novo Nordisk EP258068, WO92 / 0
5249 and WO 95/22615, Unilever WO 94/03578, WO
Lipolytic enzymes described in 95/35381 and WO 96/00292 are also suitable
It is.

Also suitable is a special type of lipase, a cutinase [EC 3.1.1.50], which is considered a lipase that does not require surface activity. The addition of cutinase to the detergent composition can be performed, for example, by adding W
OA-88 / 09367 (Genencor), WO90 / 09446 (Plant Geneti
c System), WO 94/14963 and WO 94/14964 (Unilever). Lipases and / or cutinases are typically incorporated into laundry detergents and / or fabric care compositions at a pure enzyme level of 0.0001-2% by weight of the laundry detergent and / or fabric care composition.

Suitable proteases are subtilisins (subtilisins BPN and BPN ') obtained from certain strains of B. subtilis and B. licheniformis. One suitable protease is obtained from the Bacillus strain and has a maximum activity in the pH range from 8 to 12,
Developed by Novo Industries A / S in Denmark and sold as ESPERASE ^R , hereinafter referred to as "Novo". The production of this and similar enzymes is from Novo G
B1, 243, 784. Other suitable proteases include Novo's
ALCALASE ^R, DURAZYM ^R and SAVINASE ^R, as well as the Gist-Brocades MAXATASE ^R,
MAXACAL ^R, is PROPERASE ^R and Maxapem ^R (protein engineered Maxacal). Proteolytic enzymes include modified bacterial serine proteases, such as 1987 Apr.
EP-A-87 / 303761.8, filed on 28/28 (especially pages 17, 24 and 98), hereinafter referred to as "Protease B" and hereinafter referred to as "Protease A Venegas European Patent Application No. 19, published October 29, 1986, for modified bacterial serine proteases designated "
No. 9,404 is described. A variant of the alkaline serine protease from Bacillus , wherein lysine is replaced by arginine at position 27, tyrosine is replaced by valine at position 104, serine is replaced by asparagine at position 123, and alanine is replaced by threonine at position 274. What is referred to as Protease C "is suitable. Protease C was obtained on May 16, 1991.
It is described in EP 90915958: 4, corresponding to WO 91/06637 published on the date. In particular, genetically modified variants of protease C are also included here.

A preferred protease, referred to as “Protease D”, is a carbonyl hydrolase variant having an amino acid sequence that is not found in nature, and is described in WO 95/10591.
Ghosh et al., US Ser. No. 08/3, filed Oct. 13, 1994.
According to the numbering of Bacillus amyloliquefaciens subtilisin as described in the patent application entitled "Bleaching Compositions Containing Protease Enzymes" at 22,677, preferably +99, +101, +103, +104, +107, +123.
, +27, +105, +109, +126, +128, +135, +156, +
166, +195, +197, +204, +206, +210, +216, +2
+7 in combination with one or more amino acid residue positions corresponding to those selected from the group consisting of 17, +218, +222, +260, +265 and / or +274.
At the position corresponding to position 6, it is derived from a precursor carbonyl hydrolase by using different amino acids instead of multiple amino acid residues in the carbonyl hydrolase. The following residues: +33, +62, +67, +76, +100, +
101, +103, +104, +107, +128, +129, +130, +1
32, +135, +156, +158, +164, +166, +167, +17
WO95 / 10591, having an amino acid sequence derived from the substitution of a plurality of amino acid residues replaced on the precursor enzyme corresponding to position +210 with one or more of 0, +209, +215, +217, +218 and +222. The carbonyl hydrolase variants of the proteases described are also suitable, but the numbered positions correspond to natural subtilisins from Bacillus amyloliquefaciens or to the corresponding amino acid residues of other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin (1997). Co-pending patent application USSN 60 / 048,550 filed June 4, 2016).

[0113] Polysubstituted protease variants are also preferred proteases. These protease variants include Bacillus amyloliquefaciens subtilisin 1,3,4,8,9,1
0, 12, 13, 16, 17, 18, 19, 20, 21, 22, 24, 27, 3
3, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 7
2, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 1,
01, 102, 104, 106, 107, 109, 111, 114, 116, 1
17, 119, 121, 123, 126, 128, 130, 131, 133, 1
34, 137, 140, 141, 142, 146, 147, 158, 159, 1
60, 166, 167, 170, 173, 174, 177, 181, 182, 1
83, 184, 185, 188, 192, 194, 198, 203, 204, 2
05, 206, 209, 210, 211, 212, 213, 214, 215, 2
16, 217, 218, 222, 224, 227, 228, 230, 232, 2
36, 237, 238, 240, 242, 243, 244, 245, 246, 2
47, 248, 249, 251, 252, 253, 254, 255, 256, 2
57, 258, 259, 260, 261, 262, 263, 265, 268, 2
Substitution of amino acid residues at positions corresponding to positions 103 of Bacillus amyloliquefaciens subtilisin, with substitution of amino acid residues corresponding to positions 69, 270, 271, 272, 274 and 275, with other natural amino acid residues Bacillus amyloliquefaciens subtilisin 2 when the protease variant has undergone an amino acid residue substitution at positions corresponding to positions 103 and 76.
7, 99, 101, 104, 107, 109, 123, 128, 166, 204
, 206, 210, 216, 217, 218, 222, 260, 265 or 2
There are amino acid residue substitutions at one or more amino acid residue positions other than the amino acid residue position corresponding to position 74; and / or a PCT application filed Oct. 23, 1998, all from The Procter & Gamble Company PCT / US98 / 22
588, Bacillus amyloliquefaciens subtilisin 62, 212, 2 as described in PCT / US98 / 22482 and PCT / US98 / 22486.
Some multi-substituted protease variants have undergone replacement of an amino acid residue with another natural amino acid residue at one or more amino acid residue positions corresponding to positions 30,232, 252 and 257.

[0114] Protease described in patent application EP251446 and WO91 / 06637, WO91 / 02792, protease BLAP ^R described, and WO
Those variants described in 95/23221 are also suitable for the present invention. Novo W
See also the high pH protease from Bacillus sp. NCIMB 40338 described in O93 / 18140A. Enzyme detergents containing proteases, one or more other enzymes and a reversible protease inhibitor are described in Novo WO 92 / 03529A. If desired, proteases with reduced adsorptivity and improved hydrolyzability are available as described in Procter & Gamble, WO 95/07791. Recombinant trypsin-like proteases for detergents suitable here are Novo's W
O94 / 25583. Other suitable proteases are described in Unilever, EP 516200.

The proteolytic enzyme is present in an amount of 0.0001 to 2%, preferably 0.00% by weight of the composition.
Pure enzyme levels of from 0.01 to 0.2%, more preferably 0.005 to 0.1%, are incorporated into the laundry detergent and / or fabric care compositions of the present invention.

Amylases (α and / or β) can be included for removal of carbohydrate-based soils. WO 94/02597 of Novo Nordisk A / S published February 3, 1994 describes a cleaning composition containing a mutant amylase. Novo Nordisk A / S W published April 20, 1995
See also O95 / 10603. Other amylases known for cleaning compositions include both α- and β-amylases. α-amylases are known in the art and are described in US Pat. No. 5,003,257, EP 252,666, WO 91/00003.
53, FR2,676,456, EP285,123, EP525,610, E
P368,341 and British Patent Specification No. 1,296,839 (Novo). Other suitable amylases are WO 94/18314 published August 18, 1994, and Genencor's W published February 22, 1996.
A stabilizing amylase described in O96 / 05295 and an amylase variant with additional modifications to the immediate parent of Novo Nordisk A / S, disclosed in WO 95/10603 published April 95. EP 277216, WO 95/2639
Amylases described in US Pat. No. 7 and WO 96/23873 (all Novo Nordisk) are also suitable.

[0117] Examples of commercial α- amylases products, Purafect of Genencor Ox Am ^R, all Novo N
ordisk A / S Termamyl ^R, commercially available from ^Denmark, Ban ^R, Fungamyl ^R and D
uramyl ^R. WO95 / 26397, the other suitable amylases: as measured by Phadebas ^R alpha-amylase activity assay, temperature and 8 of 25 to 55 ° C.
An α-amylase is described which is characterized by having a specific activity at least 25% higher than the specific activity of Termamyl ^R at pH values in the 10 range. WO96 / 23
873 (Novo Nordisk) are suitable. Other amylolytic enzymes having improved properties in terms of activity levels and a combination of thermostability and high activity levels are described in WO 95/35382.

The amylolytic enzyme is present in an amount of 0.0001 to 2% by weight of the composition, preferably 0.001%.
Pure enzyme levels of 018-0.06%, more preferably 0.00024-0.048%, are incorporated into the laundry detergent and / or fabric care compositions of the present invention.

[0119] The enzymes may be of any suitable origin, such as plant, animal, bacterial, fungal and yeast sources. The origin may also be mesophilic or extremophilic (cryophilic, eutrophic, thermophilic, barophilic, alkaline, acidophilic, halophilic, etc.). Purified or unpurified forms of these enzymes may also be used. At present, it is customary to modify wild-type enzymes by protein / gene engineering techniques to maximize performance efficacy with the cleaning compositions of the present invention. For example, variants are designed to increase the compatibility of the enzyme with the common components of such compositions. On the other hand, the optimal pH of the enzyme variant,
Variants may be designed such that bleed or chelant stability, catalytic activity, etc. are tailored to a particular cleaning application.

In particular, attention should be paid to amino acids that are susceptible to oxidation in terms of bleach stability and surface charge in terms of surfactant compatibility. The isoelectric point of such enzymes may be modified by substitution of some charged amino acids, for example, increasing the isoelectric point helps to improve compatibility with anionic surfactants. Enzyme stability can be further enhanced, for example, by forming additional salt bridges and reinforcing calcium binding sites to increase the stability of the chelants. Special care must be taken to cellulases so that most cellulases have distinct binding domains (CBD). The properties of such enzymes can be altered by modifying these domains.

The enzyme may comprise from 0.0001 to 2% by weight of the laundry detergent and / or fabric care composition.
At a pure enzyme level in laundry detergents and / or fabric care compositions. The enzymes can be added as separate single components (eg, globules, granules, stabilizing liquids containing one enzyme) or as a mixture of two or more enzymes (eg, co-granules).

Another suitable detergent ingredient that can be added is an enzymatic oxidation scavenger, which comprises 1
Co-pending European Patent Application No. 92870018, filed Jan. 31, 992.
No. 6 is described in the specification. An example of such an enzymatic oxidation scavenger is ethoxylated tetraethylene polyamine.

The various enzyme substances and means for their incorporation into synthetic detergent compositions are also described in Genencor I.
WO 9307263A and WO 9307260A from nternational, WO from Novo
89908694A and McCarty et al., US Pat. No. 3,553, January 5, 1971.
139. The enzyme was purchased from Place et al., US Pat.
U.S. Pat. No. 4,507,219 to Hughes, 101,457 and March 26, 1985.
However, it is further disclosed. Enzymatic substances useful in liquid detergent formulations and their incorporation into such formulations are described in Hora et al., US Pat.
868. Enzymes useful in detergents can be stabilized by various techniques. Enzyme stabilization technology is described in US Pat. No. 3,600, Gedge et al.
, 319, EP 199,405 and EP of Venegas dated October 29, 1986.
200,586. Enzyme stabilization systems, for example, US3
519,570. Useful Bacillus sp. AC13 to provide proteases, xylanases and cellulases are described in Novo WO9401532A.

Bleaching Agents The laundry detergent and / or fabric care compositions of the present invention can include bleaching agents in addition to the modified transferase.

The combination of a modified transferase and a bleach results in improved whiteness,
Provides improved tensile strength, improved anti-wrinkle, anti-shrinkage, anti-pilling properties to fabrics, refreshes or restores, as well as improved static control, fabric flexibility, color appearance and fabric wear resistance and effectiveness And, in particular, improved fabric feel. In addition, an improved cleaning effect is also obtained with the above combination.

Bleaching agents include hydrogen peroxide, PB1, PB4, and percarbonate having a particle size of 400-800 microns. These bleach components can include one or more oxygen bleaches and, depending on the bleach selected, one or more bleach activators. When present, the oxygen bleaching compound is typically present at a level of about 1 to about 25%. The bleach component used herein can be any bleach useful in detergent compositions, including oxygen bleaches and others known in the art. Bleaches suitable for the present invention are activated or deactivated bleaches.

[0127] One category of oxygen bleaches that can be used is polycarboxylic acid bleaches and salts thereof. Suitable examples of this class of agents include magnesium monoperoxyphthalate hexahydrate, magnesium salt of m-chloroperbenzoic acid, 4-nonylamino-4
-Oxoperoxybutyric acid and diperoxidedecanedioic acid. Such bleaching agents are disclosed in U.S. Pat. No. 4,483,781, U.S. Pat. No. 740,446, European Patent Application 0,133,354 and U.S. Pat.
Highly preferred bleaches include 6 as described in US Pat. No. 4,634,551.
There is also -nonylamino-6-oxoperoxycaproic acid.

Another category of bleaches that can be used is halogen bleaches. Examples of hypohalous acid bleaches include, for example, trichloroisocyanuric acid, sodium and potassium dichloroisocyanurates, N-chloro and N-bromoalkanesulfonamides. Such substances are usually added at 0.5 to 10% by weight, preferably 1 to 5% by weight of the final product.

Hydrogen peroxide releasing agents can be perhydrolyzed to form peracids as active bleaching species, resulting in improved bleaching effects, such as tetraacetylethylenediamine (TAED), nonanoyloxybenzenesulfonate ( NOBS, US
4,412,934), 3,5-trimethylhexanoloxybenzenesulfonate (described in ISONOBS, EP120,591), pentaacetylglucose (PAG) or phenolsulfonate ester of N-nonanoyl-6-aminocaproic acid (NACA- OBS, described in WO 94/28106). Co-pending European Patent Application No. 91
Acylated citrate esters such as those disclosed in 870207.7 are also suitable activators.

Useful bleaching agents, including bleach activators and peroxygen bleaching compounds, and peroxy acids, for use in laundry detergent and / or fabric care compositions according to the present invention, are our co-pending agents. Application USSN 08/136
626, PCT / US95 / 07823, WO95 / 27772, WO95 / 2
7773, WO 95/27774 and WO 95/27775.

[0131] Hydrogen peroxide may also be present at the beginning or during the washing and / or rinsing process by adding an enzyme system capable of generating hydrogen peroxide (ie, the enzyme and its substrate). Such an enzyme system is described in EP-A-Oct.
It is disclosed in patent application 91202655.6.

The metal-containing catalysts used in the bleach compositions include cobalt-containing catalysts, such as pentaamine cobalt (III) acetate, and manganese-containing catalysts, such as EPA549271,
EPA 549272, EPA 458 397, US 5,246,621, EPA 4
58398, US 5,194,416 and US 5,114,611. Bleach compositions comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent are described in patent application 94870206.3.

[0133] Bleaches other than oxygen bleaches are known in the art and may be utilized herein. One type of non-oxygen bleach of particular interest is a light activated bleach such as sulfonated zinc and / or aluminum phthalocyanine. These substances can adhere to the substrate during the cleaning process. Light irradiation in the presence of oxygen, such as hanging and drying clothes under sunlight, activates the sulfonated zinc phthalocyanine, thereby bleaching the substrate. A preferred zinc phthalocyanine and light activated bleaching process is described in US Pat. No. 4,033,718. Typically,
Laundry detergent and / or fabric care compositions contain from about 0.025 to about 1.25% by weight of the sulfonated zinc phthalocyanine.

Dye Inhibition The laundry detergent and / or fabric care compositions of the present invention are preferably used to transfer dye from a fabric with dissolved and suspended dye to another encountered during a fabric washing operation with a colored fabric. Compounds for inhibiting dyeing can also be included. The combination of the modified transferase and the dye transfer inhibitor imparts improved tensile strength, improved anti-wrinkle, anti-shrinkage, anti-pilling properties to the fabric, refreshes or restores,
It has been surprisingly found to provide improved static suppression, fabric flexibility, color appearance and fabric wear resistance and effects. In addition, an improved cleaning effect is also obtained with the above combination.

Polymer Transfer Inhibitors Laundry detergents and / or fabric care compositions according to the present invention comprise from 0.001 to 10% by weight of polymer, preferably from 0.01 to 2%, more preferably from 0.05 to 1%. It also contains a dye transfer inhibitor. The above-mentioned polymeric transfer dye inhibitors are commonly incorporated into laundry detergents and / or fabric care compositions to prevent the transfer of dye from the colored fabric onto the washed fabric. These polymers have the ability to complex with or adsorb free dye washed off from the colored fabric before the dye has a chance to adhere to other objects in the wash liquor. Particularly suitable polymeric dye transfer inhibitors are polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidone and polyvinylimidazole, or mixtures thereof. The addition of such a polymer also enhances the performance of the enzyme according to the invention.

A) Polyamine N-Oxide Polymers Suitable for use with the polyamine N-oxide polymers comprise units having the following structural formula:

Embedded image In the above formula, P is a polymerizable unit, to which an R—N—O group can be bound, or the R—N—O group forms part of the polymerizable unit, or a combination of both A is NC (= O), C (= O) O, C = O, -O-, -S-, -N-;
x is 0 or 1; R is an aliphatic, ethoxylated aliphatic, aromatic, heterocyclic, alicyclic group or a combination thereof, to which the nitrogen of the NO group can be attached, or The nitrogen of the NO group is part of these groups.

The N—O group can be represented by the following general structure:

Embedded image Wherein R1, R2 and R3 are an aliphatic group, an aromatic, a heterocyclic, an alicyclic group or a combination thereof, wherein x or / and y or / and z is 0 or 1, where N The nitrogen of the -O group is attached, or the nitrogen of the NO group forms part of these groups.

The NO group may be part of the polymerizable unit (P), attached to the polymer backbone, or a combination of both. Suitable polyamine N-oxides in which the NO group forms part of the polymerizable unit include those polyamine N-oxides in which R is selected from aliphatic, aromatic, cycloaliphatic or heterocyclic groups. is there. One class of polyamine N-oxides comprises a group of polyamine N-oxides in which the nitrogen of the NO group forms part of the R group. Preferred polyamine N
An oxide is where R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof. Another class of polyamine N-oxides consists of a group of polyamine N-oxides in which the nitrogen of the NO group is attached to the R group.

[0139] Other suitable polyamine N-oxides are polyamine oxides in which the NO groups are attached to polymerizable units. A preferred class of these polyamine N-oxides is the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group and the nitrogen of the NO functional group is part of the above R group. Polyamine N-oxide. Examples of these classes are polyamine oxides, where R is a heterocyclic compound such as pyridine, pyrrole, imidazole and derivatives thereof. Another preferred class of polyamine N-oxides is the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group and the nitrogen of the NO functionality is attached to the R group. ). Examples of these classes are polyamine oxides, where the R groups are aromatic, such as phenyl.

Any polymer backbone may be used as long as the amine oxide polymer formed is water soluble and has dye transfer inhibiting properties. Examples of suitable polymer backbones include
Polyvinyl, polyalkylene, polyester, polyether, polyamide, polyimide, polyacrylate and mixtures thereof.

The amine N-oxide polymers of the present invention typically comprise 10: 1 to 1: 1000
It has a ratio of amine to amine N-oxide of 000. However, the amount of amine oxide groups present in the polyamine oxide polymer can be varied by suitable copolymerization or by moderate N-oxidation. Preferably, the ratio of amine to amine N-oxide is 2: 3 to 1: 1,000,000, more preferably 1: 4 to 1: 1,000,000, and most preferably 1: 7 to 1: 100,000.
0. The polymers of the present invention actually include random or block copolymers in which one monomer type is an amine N-oxide and the other monomer type is or is not an amine N-oxide. The amine oxide units of the polyamine N-oxide have a pKa <10, preferably a pKa <7, more preferably a pKa <6. Polyamine oxides can be obtained at almost any degree of polymerization. The degree of polymerization is not critical as long as the material has the desired water solubility and dye suspending power. Typically, the average molecular weight is between 500 and 1,000,000, preferably 1000
~ 50,000, more preferably 2000 to 30,000, most preferably 30
It is in the range of 00 to 20,000.

B) Copolymer of N-vinylpyrrolidone and N-vinylimidazole The N-vinylimidazole N-vinylpyrrolidone polymer used in the present invention has an average molecular weight of 5000 to 1,000,000, preferably 5000 to 200,000. Having a range. Highly preferred polymers for use in laundry detergents and / or fabric care compositions according to the present invention are those selected from N-vinylimidazole N-vinylpyrrolidone copolymers, wherein the polymer is 5000-50,000, more preferably It has an average molecular weight range of 8,000 to 30,000, most preferably 10,000 to 20,000. The average molecular weight range is from Barth HGand Mays JW, Chem
It was examined by light scattering as described in ical Analysis, Vol. 113, “Modern Methods of Polymer Characterization”. Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have an average molecular weight range of 5,000 to 50,000, more preferably 8,000 to 30,000, and most preferably 10,000 to 20,000.

N-vinylimidazole N-vinylpyrrolidone copolymers, characterized by having the above average molecular weight range, exhibit excellent dye transfer inhibiting properties while maintaining the efficacy of laundry detergent and / or fabric care compositions formulated therewith. Does not adversely affect cleaning performance. The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention comprises:
0.2, more preferably 0.8: 0.3, most preferably 0.6: 0.4 N-
It has a molar ratio of vinylimidazole to N-vinylpyrrolidone.

C) Polyvinylpyrrolidone In the laundry detergent and / or fabric care compositions of the present invention, from about 2500 to about 400
000, preferably from about 5000 to about 200,000, more preferably about 500
Polyvinyl pyrrolidone ("PVP") having an average molecular weight of from 0 to about 50,000, most preferably from about 5000 to about 15,000, may also be utilized. Suitable polyvinylpyrrolidones are product names PVP K-15 (viscosity molecular weight of 10,000), PV
PK-30 (average molecular weight of 40,000), PVP K-60 (160,00
0 and an average molecular weight of PVP K-90 (average molecular weight of 360,000) from ISP Corporation, New York, NY and Montreal, Canada. Other suitable polyvinylpyrrolidones commercially available from BASF Cooperation include Sokalan HP165 and Sokalan HP12; polyvinylpyrrolidone known to the detergent industry (see, for example, EP-A-262,897 and EP-A-256,696). There is.

D) Polyvinyloxazolidone In the laundry detergents and / or fabric care compositions of the present invention, polyvinyloxazolidone may also be utilized as a polymeric dye transfer inhibitor. The above polyvinyl oxazolidone is used in an amount of about 2500 to about 400,000, preferably about 5000 to about 200,000.
0, more preferably from about 5000 to about 50,000, and most preferably from about 5000 to about 50,000.
It has an average molecular weight of about 15,000.

E) Polyvinylimidazole In the laundry detergents and / or fabric care compositions of the present invention, polyvinylimidazole may also be utilized as a polymeric dye transfer inhibitor. The polyvinyl imidazole described above can be used in an amount of about 2500 to about 400,000, preferably about 5000 to about 200,000.
More preferably from about 5000 to about 50,000, and most preferably from about 5000 to about 1
It has an average molecular weight of 5,000.

F) Crosslinked Polymers Crosslinked polymers are polymers in which the backbone is linked to some extent, these links may be of chemical or physical nature, with the possibility that the active groups may be on the backbone or It may be on the side chain, and the crosslinked polymer can be found in Journal of Polymer Science, volum
e 22, pages 1035-1039. In one embodiment, the crosslinked polymer is made to form a three-dimensional rigid structure and can trap dye in the pores formed by the three-dimensional structure. In another aspect, the crosslinked polymer captures the dye by swelling. Such crosslinked polymers are described in co-pending patent application 94870213.9.

Dispersant The laundry detergent and / or fabric care composition of the present invention may further contain a dispersant. The combination of the modified transferase and dispersant imparts improved tensile strength, improved anti-wrinkle, anti-shrinkage, anti-pilling properties to the fabric, refreshes or restores, as well as improved static control, fabric flexibility, It has been surprisingly found to provide color appearance and fabric abrasion resistance properties and effects. In addition, an improved cleaning effect is also obtained with the above combination.

Suitable water-soluble organic salts are homo- or copolymeric acids, or salts thereof, wherein the polycarboxylic acids have at least two carboxyl groups separated from each other by no more than 2 carbon atoms. This type of polymer is disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates of MW 2000-5000, and their copolymers with maleic anhydride, such copolymers having a molecular weight of 1000-100,000. In particular, copolymers of acrylates and methyl acrylates, such as 480N, having a molecular weight of 4000 may be incorporated into the laundry detergent and / or fabric care compositions of the present invention at a level of 0.5-20% by weight of the composition. it can.

The compositions of the present invention may contain a lime soap peptizer compound, which has a lime soap dispersing power (LSDP) of 8 or less, preferably 7 or less, most preferably 6 or less. Is preferred. The lime soap peptizer compound is preferably present at a level of 0-20% by weight.

A numerical measure of the effectiveness of a lime soap peptizer is the lime soap dispersive power (LSD).
P), HCBorghetty and CA Bergman, J. Am. Oil. Chem. Soc., Volum
e 27, pages 88-90 (1950) Measured using a lime soap dispersion test as described in the article. This lime soap dispersion test method is widely used by those skilled in the art,
For example, the following review literature: WNLinfield, Surfactant Science Series, Volume 7,
p.3; WNLinfield, Tenside Surf.det., volume 27, pages 159-163 (1990); MK
Nagarajan, WFMasler, Cosmetics and Toiletries, volume 104, pages 71-73 (19
89). LSDP is 333 ppm CaCo ₃ (Ca: Mg
= 3: 2) Percent by weight of dispersant to sodium oleate required to disperse the lime soap precipitate formed by 0.025 g of sodium oleate in 30 ml of water of equivalent hardness.

Surfactants that have good lime soap peptizer capabilities include certain amine oxides, betaines, sulfobetaines, alkyl ethoxy sulfates and ethoxylated alcohols. Exemplary surfactants having an LSDP of 8 or less for use according to the present invention include C ₁₆ -C ₁₈ dimethylamine oxide, C ₁₂ -C ₁₈ alkyl ethoxy sulfates having an average degree of ethoxylation of 1 to 5, especially ethoxylation degree 3 C ₁₂ -C ₁₅ alkyl ethoxy sulfate surfactants (LSDP = 4)
, And from BASF GmbH are respectively sold under the trade names Lutensol A012 and Lutensol A030, average degree of ethoxylation of 12 (LSDP = 6) or 30 _{C 14} -
There is a C ₁₅ ethoxylated alcohol.

[0153] Polymer lime soap peptizers suitable for use herein are described in Cosmetics and To
MKNagarajan, WFMasl found in iletries, volume 104, pages 71-73 (1989)
er. 4- (N-octanoyl-6-aminohexanoyl) benzenesulfonate,
4- (N-nonanoyl-6-aminohexanoyl) benzenesulfonate, 4-
Hydrophobic bleach, such as (N-decanoyl-6-aminohexanoyl) benzenesulfonate and mixtures thereof; Nonanoyloxybenzenesulfonate in combination with a hydrophilic / hydrophobic bleach formulation can also be used as a lime soap peptizer compound .

Color Care and Fabric Care Effects Technologies that exert a type of color care effect can also be included. Examples of these technologies are metal catalysts for color maintenance. Such metal catalysts are described in co-pending European Patent Application No. 92870181.2. Dye fixing agent, polyolefin dispersant for preventing wrinkles and improving water absorption, fragrance,
Amino-functional polymers for color care treatment and perfume retention are another example of color care / fabric care technology and are described in co-pending patent application No. 96870140.9 filed on November 7, 1996. Have been.

[0155] Fabric softeners can also be incorporated into laundry detergents and / or fabric care compositions according to the present invention. These agents may be inorganic or organic in type. The inorganic softener is GB-
A-1,400,898 and exemplified by the smectite clay disclosed in US Pat. No. 5,019,292. Organic fabric softeners include GB-A1, 514, 27
Water-insoluble tertiary amines as disclosed in US Pat.
Mono-C ₁₂ -C ₁₄ quaternary ammonium salts disclosed in EP-B-0,026,527 and EP-B-0,026,528 and combinations thereof, and EP-B
-Dilong chain amides as disclosed in US Pat. Other useful organic components of the fabric softening system include EP-A-0,299,575 and 0,313,1.
There are high molecular weight polyethylene oxide materials as disclosed at 46.

Preferably, the laundry detergent and / or fabric care composition of the present invention comprises a smectite clay in addition to the modified transferase enzyme. The combination of the modified transferase and the smectite clay provides improved tensile strength, improved anti-wrinkle, anti-shrinkage, anti-pilling properties to the fabric, refreshes or restores, as well as improved static control, fabric flexibility, It has been surprisingly found to provide color appearance and fabric abrasion resistance properties and effects. In addition, an improved cleaning effect is also obtained with the above combination.

The level of smectite clay is usually 2 to 20% by weight, more preferably 5 to 15%.
%, The substance being added as a dry mix component to the rest of the formulation. Organic fabric softeners, such as water-insoluble tertiary amines or di-long chain amide materials, may be used in aqueous solutions.
5 to 5% by weight, usually 1 to 3% by weight, high molecular weight polyethylene oxide substance and water-soluble cationic substance 0.1 to 2% by weight, usually 0.15 to 1%
. Added at the 5% level. These substances are usually added to the spray-dried portion of the composition, but in some cases, they may be added as dry mix particles or sprayed as a molten liquid onto other solid components of the composition. Is convenient.

Other Surfactants Ampholytic surfactants are also suitable for use in the laundry detergent and / or fabric care compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines, wherein the aliphatic group is linear or It may be branched. One of the aliphatic substituents has at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms;
At least one has an anionic water-soluble group, such as a carboxy, sulfonic acid, or sulfate group. For examples of amphoteric surfactants, see Laughlin et al., US Pat. No. 3,929,678, issued Dec. 30, 1975, column 19, lines 18-35. When included herein, the laundry detergent and / or fabric care compositions of the present invention typically contain from 0.2 to about 15% by weight, preferably from about 1 to about 10%, of such amphoteric surfactants. Including.

[0159] Zwitterionic surfactants are also suitable for use in laundry detergents and / or fabric care compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. . For examples of zwitterionic surfactants, see Laughlin et al., U.S. Pat.
See column 19, line 38 to column 22, line 48 of S Patent 3,929,678. As contained herein, the laundry detergent and / or fabric care compositions of the present invention typically comprise from 0.2 to about 15%, preferably from about 1 to about 10%, of such a dipolar surfactant. including.

Semipolar nonionic surfactants comprise two alkyl moieties selected from the group consisting of one alkyl moiety of about 10 to about 18 carbon atoms, an alkyl group of about 1 to about 3 carbon atoms, and a hydroxyalkyl group. Water-soluble amine oxide; about 10 to about 1 carbon atoms
Water-soluble phosphine oxide having one alkyl moiety of eight, two moieties selected from the group consisting of an alkyl group of about 1 to about 3 carbon atoms and a hydroxyalkyl group; one alkyl of about 10 to about 18 carbon atoms Particular categories of nonionic surfactants, including water-soluble sulfoxides having a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of about 1 to about 3 carbon atoms.

Semi-polar nonionic detergent surfactants include amine oxide surfactants having the formula:

Embedded image Wherein R ³ is an alkyl, hydroxyalkyl, alkylphenyl group having about 8 to about 22 carbon atoms or a mixture thereof; R ⁴ is an alkylene, hydroxyalkylene group having about 2 to about 3 carbon atoms or Mixtures thereof;
x is 0 to about 3; each R ⁵ is an alkyl or hydroxyalkyl group having about 1 to about 3 carbon atoms, or a polyethylene oxide group having about 1 to about 3 ethylene oxide groups. The R ⁵ groups may be linked together, for example, via an oxygen or nitrogen atom to form a ring structure. Among these amine oxide surfactants are, in particular, C ₁₀ -C ₁₈ alkyldimethylamine oxide and C ₈ -C ₁₂ alkoxyethyldihydroxyethylamine oxide. When included herein, the cleaning compositions of the present invention typically comprise from 0.2 to about 15% by weight, preferably from about 1 to about 10%, of such a semi-polar nonionic surfactant.

[0162] The laundry detergent and / or fabric care compositions of the present invention may further comprise a cosurfactant selected from the group of primary or tertiary amines. Primary amines suitable for use herein include amines according to the formula R ₁ NH ₂ , where R ₁ is a C ₆ -C ₁₂ , preferably C ₆ -C ₁₀ alkyl chain, or R ₄ X (C
H ₂₎ is _n, X is -O -, - C (O) NH- or a -NH-, _{R 4} is a _C 6 _{-C 12} alkyl chains, n represents 1-5, preferably 3 is there. The R ₁ alkyl chain may be straight or branched and may have up to 12 and preferably less than 5 ethylene oxide moieties. Preferred amines according to the above formula are n-alkylamines. Amines suitable for use herein are selected from 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary amines include C ₈ -C ₁₀ oxypropylamine, octyloxypropylamine, 2-ethylhexyloxypropylamine, laurylamidopropylamine and amidopropylamine.

Tertiary amines suitable for use herein include tertiary amines having the formula R ₁ R ₂ R ₃ N, wherein R ₁ and R ₂ are a C ₁ -C ₈ alkyl chain or

Embedded image And R ₃ is a C ₆ -C ₁₂ , preferably a C ₆ -C ₁₀ alkyl chain, or R ₃ is R ₄ X (CH ₂ ) _n (X is —O—, —C (O) NH -Or -NH-
Wherein R ₄ is C ₄ -C ₁₂ and n is 1-5, preferably 2-3. R ₅ is H or C ₁ -C ₂ alkyl, and x is 1-6. R ₃ and R ₄ may be linear or branched, and the R ₃ alkyl chain may have up to 12, preferably less than 5, ethylene oxide moieties.

Preferred tertiary amines are those in which R ₁ is a C ₆ -C ₁₂ alkyl chain and R ₂ and R ₃ are C ₁ -C ₃ alkyl or

Embedded image (Wherein R ₅ is H or CH ₃ and x = 1 to 2), and is R ₁ R ₂ R ₃ N. Amidoamines of the following formula are also preferred:

Embedded image In the above formula, R ₁ is C ₆ -C ₁₂ alkyl, n is 2 to 4, preferably n is 3, and R ₂ and R ₃ are C ₁ -C ₄ .

Most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, C _8-10 oxypropylamine, N-
Coco-1,3-diaminopropane, coconut alkyldimethylamine, lauryldimethylamine, laurylbis (hydroxyethyl) amine, cocobis (hydroxyethyl) amine, 2 mol propoxylated laurylamine, 2 mol propoxylated octylamine, laurylamide dimethylamine, there is C _8-10 dimethylamine and C ₁₀ amidopropyl dimethylamine. The most preferred amines for use in the composition are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Particularly desirable are:
n-dodecyldimethylamine, bishydroxyethyl coconut alkylamine,
7-ethoxylated oleylamine, laurylamidopropylamine and cocoamidopropylamine.

Builder System The laundry detergent and / or fabric care composition according to the present invention may further comprise a builder system. Aluminosilicate materials, silicates, polycarboxylates, alkyl or alkenyl succinic acids, and fatty acids, materials such as ethylenediaminetetraacetic acid, diethylenetriaminepentamethyleneacetic acid, sequestering agents such as aminopolyphosphonates, especially ethylenediaminetetramethylenephosphonic acid and diethylenetriamine Any conventional builder system is suitable for use herein, including pentamethylenephosphonic acid. A phosphate builder may also be used here.

Suitable builders include inorganic ion exchange materials, usually inorganic hydrated aluminosilicate materials, and more specifically hydrated synthetic zeolites, such as hydrated zeolites A, X
, B, HS or MAP. Another suitable inorganic builder material is a laminated silicate, such as SKS-6 (
Hoechst). SKS-6 is a crystal laminated silicate made of sodium silicate (Na ₂ Si ₂ O ₅ ).

Suitable polycarboxylates having one carboxy group include lactic acid, glycolic acid and their ether derivatives as disclosed in Belgian patents 831,368, 821,369 and 821,370. Polycarboxylates having two carboxy groups include succinic acid, malonic acid, (ethylenedioxy)
Water-soluble salts of diacetate, maleic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid and the ethers described in DE-A 2,446,686, 2,446,687 and US Pat. No. 3,935,257 Carboxylates and the sulfinylcarboxylates described in Belgian Patent 840,623. Polycarboxylates having three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconates, and British Patent 1,379,241.
Carboxymethyl oxysuccinate, Dutch application 720587
3, and oxypolycarboxylate materials such as 2-oxa-1,1,3-propanetricarboxylate described in British Patent 1,387,447. is there.

The polycarboxylates having four carboxy groups are described in GB 1,261
Oxydisuccinate, 1,1,2,2-ethanetetracarboxylate, 1,1,3,3-propanetetracarboxylate and 1,1
There is 1,2,3-propanetetracarboxylate. Polycarboxylates with sulfo substituents include the sulfosuccinate derivatives disclosed in British Patents 1,398,421, 1,398,422 and US Pat. No. 3,936,448, and in British Patent 1,082,179. Among the sulfonated pyrolytic citrates described, polycarboxylates having a phosphon substituent are known from British Patent 1,439,000.
Are disclosed.

Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,
Cis, cis-tetracarboxylate, cyclopentadienidepentacarboxylate, 2,3,4,5-tetrahydrofuran-cis, cis, cis-tetracarboxylate, 2,5-tetrahydrofuran-cis-dicarboxylate, 2,
2,5,5-tetrahydrofuran-tetracarboxylate, 1,2,3,4
There are 5,6-hexane-hexacarboxylate and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include melitic acid, pyromellitic acid, and the phthalic acid derivatives disclosed in British Patent 1,425,343. Among the above preferred polycarboxylates are hydroxycarboxylates having up to 3 carboxy groups per molecule, more particularly citrates.

Preferred builder systems for use in the present compositions include water-insoluble aluminosilicate builders or laminated silicates (SKS-6), such as zeolite A, and a water-soluble carboxylate chelating agent, such as citric acid. There is a mixture. Preferred builder systems include a mixture of a water-insoluble aluminosilicate builder such as zeolite A and a water-soluble carboxylate chelating agent such as citric acid. Preferred builder systems for use in the liquid laundry detergent and / or fabric care compositions of the present invention are soaps and polycarboxylates.

Other builder substances which can form part of the builder system in use in the granular composition include inorganic substances such as carbonates, bicarbonates, alkali metal silicates, and organic phosphonates.
There are organic substances such as aminopolyalkylene phosphonates and aminopolycarboxylates. Other suitable water-soluble organic salts are homo- or copolymeric acids or salts thereof, wherein the polycarboxylic acid has at least two carboxyl groups separated from each other by no more than 2 carbon atoms. This type of polymer is GB-A-1,596
, 756. Examples of such salts are polyacrylates with a MW of 2000 to 5000 and copolymers thereof with maleic anhydride, such copolymers having a molecular weight of 20,000 to 70,000, in particular of about 40,000. ing.

The cleaning builder salt is usually present in an amount from 5 to 80%, preferably from 10 to 70%, most usually from 30 to 60% by weight of the composition.

Chelating Agents The laundry detergent and / or fabric care compositions of the present invention may also optionally include one or more iron and / or manganese chelating agents. Such chelators can be selected from the group consisting of aminocarboxylates, aminophosphonates, polyfunctionally substituted aromatic chelators and mixtures thereof, all as described below. Without being bound by theory, it is believed that the effects of these materials are due in part to their exceptional ability to remove iron and manganese ions from the wash liquor by the formation of soluble chelates.

Aminocarboxylates useful as optional chelating agents include ethylenediaminetetraacetic acid, N-hydroxyethylethylenediaminetriacetic acid, nitrilotriacetic acid,
There are ethylene diamine tetrapropionic acid, triethylene tetraamine hexaacetic acid, diethylene triamine pentaacetic acid and ethanol diglycine, their alkali metal, ammonium and substituted ammonium salts, and mixtures thereof. Aminophosphonates are also suitable for use as chelating agents in the compositions of the present invention when at least low levels of total phosphorus are tolerated in laundry detergent and / or fabric care compositions, including ethylenediamines such as DEQUEST There is tetrakis (methylene phosphonate). Preferably, these aminophosphonates do not contain alkyl or alkenyl groups of about 7 or more carbon atoms. Polyfunctionally substituted aromatic chelators are also useful in the present compositions. May 2, 1974
See Connor et al., U.S. Pat. A preferred compound of this type is a dihydroxydisulfobenzene, such as 1,2-dihydroxy-3,5-disulfobenzene, in the acid form.

Preferred biodegradable chelators for use herein are Hartma, Nov. 3, 1987.
n and ethylenediaminedisuccinic acid ("EDDS") as described in Perkins US Patent 4,704,233, especially the [S, S] isomer. The composition may also contain a water-soluble methylglycine diacetate (MGDA) salt (or acid form) as a cobuilder useful as an insoluble builder, such as zeolites, laminated silicates, and the like, or as a chelant.

[0177] If utilized, these chelating agents are usually from about 0.1 to about 15% by weight of the laundry detergent and / or fabric care compositions. More preferably, if utilized, the chelating agent will be from about 0.1 to about 3.0% by weight of such a composition.

[0178] Another optional component foam control agents, silicone and silica - a foam control agent which is exemplified by silicone mixture. Silicones are typically represented by alkylated polysiloxane materials, and silica is commonly used in finely divided form, exemplified by silica airgels, xerogels and various types of hydrophobic silica. These materials can be formulated as particles, and the suds suppressor is advantageously formulated to be released in a water-soluble or water-dispersible, substantially non-surfactant, detergent-impermeable carrier. . Alternatively, the foam control agent may be applied by dissolving or dispersing in a liquid carrier and spraying on one or more other components.

Preferred silicone suds suppressors are described in US Pat. No. 3,933,67 to Bartollota et al.
2 is disclosed. Another particularly useful suds suppressor is a self-emulsifying silicone suds suppressor, which is a German patent application DTOS 2,6 published April 28, 1977.
46, 126. An example of such a compound is DC-544, commercially available from Dow Corning, which is a siloxane-glycol copolymer. A particularly preferred suds suppressor is a suds suppressor system consisting of a mixture of silicone oil and a 2-alkyl-alkanol. A suitable 2-alkyl-alkanol is 2-butyloctanol, sold under the trade name Isofol 12R. Such a suds suppressor system is described in co-pending European Patent Application N 92870174.7, filed November 10, 1992. Particularly preferred silicone suds suppressors are described in co-pending European Patent Application N 92022
649.8. The compositions may comprise silicone / silica mixture in combination with a molten nonporous silica such as Aerosil ^R.

[0180] The above-mentioned foam suppressing agent is used in an amount of 0.001 to 2% by weight, preferably 0.02% by weight of the composition.
Usually used at a level of 1 to 1% by weight.

Preservatives The laundry detergent and / or fabric care compositions may also optionally include one or more preservatives. The function of the preservative is to keep organisms / microorganisms from propagating and growing in the laundry detergent and / or fabric care composition and the fabric treated with the composition. In the absence of such preservatives, organisms / microorganisms can grow on fabrics treated with the present laundry detergents and / or fabric care compositions because significant amounts of carbohydrate / sugar remain in the fabric after treatment. This is because they may remain. The disinfection of the fabric can be carried out with the composition according to the invention containing antimicrobial substances, for example antibacterial halogenated compounds, quaternary compounds and phenolic compounds. Preservatives suitable for use with the present invention include, but are not limited to:

It is preferred to use broad spectrum preservatives, such as those that are effective on both bacteria (both Gram-positive and Gram-negative) and fungi. Limited spectrum preservative,
For example, a single group of microorganisms, such as those that are effective only for fungi, are complementary and / or
Alternatively, it can be used in combination with a broad spectrum preservative or other limited spectrum preservative that has complementary activity. Mixtures of broad spectrum preservatives can also be used. In some cases (eg, Gram negative) where a particular group of microbial contaminants is of concern, aminocarboxylate chelators may also be used as enhancers, alone or with other preservatives. These chelators, including, for example, ethylenediaminetetraacetic acid (EDTA), hydroxyethylenediaminetriacetic acid, diethylenetriaminepentaacetic acid, other aminocarboxylate chelators, mixtures thereof, and salts thereof, and mixtures thereof, are gram-negative bacteria, especially It can increase the preservative efficacy against Pseudomonas species. Antimicrobial preservatives useful in the present invention include biocidal compounds, ie, substances that kill microorganisms,
Alternatively, there are biostatic compounds, ie, substances that inhibit and / or regulate the growth of microorganisms.

(1) Organic Sulfur Compound A preferable water-soluble preservative for use in the present invention is an organic sulfur compound. Some non-limiting examples of organosulfur compounds suitable for use in the present invention are:

(A) 3-isothiazolone compounds Preferred preservatives are antimicrobial organic preservatives containing 3-isothiazolone groups having the formula:

Embedded image Wherein Y is an unsubstituted alkyl, alkenyl or alkynyl group of about 1 to about 18 carbon atoms, about 3 to about 6 carbon rings and an unsubstituted or substituted cycloalkyl group of up to 12 carbon atoms, An unsubstituted or substituted aralkyl group, or an unsubstituted or substituted aryl group of up to about 10 carbon atoms; R ¹ is hydrogen, halogen or a (C ₁ -C ₄ ) alkyl group; and R ² is hydrogen, halogen Or a (C ₁ -C ₄ ) alkyl group. Preferably, when Y is methyl or ethyl, R ¹ and R ² must not both be hydrogen. Also suitable are the salts of these compounds formed by reacting the compounds with acids such as hydrochloric acid, nitric acid, sulfuric acid and the like.

This class of compounds is disclosed in US Pat. No. 4,265,899 to Lewis et al., Issued May 5, 1981, which is incorporated herein by reference. Examples of the above compounds are 5-chloro-2-methyl-4-isothiazolin-3-one,
-N-butyl-3-isothiazolone, 2-benzyl-3-isothiazolone, 2-
Phenyl-3-isothiazolone, 2-methyl-4,5-dichloroisothiazolone, 5-chloro-2-methyl-3-isothiazolone, 2-methyl-4-isothiazolin-3-one and mixtures thereof. A preferred preservative is 5-chloro-2
Water-soluble mixture of -methyl-4-isothiazolin-3-one and 2-methyl-4-isothiazolin-3-one, more preferably about 77% of 5-chloro-2-methyl-4-isothiazolin-3-one and about 23% 2-methyl-4-isothiazolin-3-one mixture, trade name Kathon ^R CG by Rohm and Haas Company
Is a broad spectrum preservative commercially available as a 1.5% aqueous solution. When Kathon ^R is used as a preservative in the present invention, it can be used in an amount of about 0.00
0.01 to about 0.01% by weight, preferably about 0.0002 to about 0.005%, more preferably about 0.0003 to about 0.003%, and most preferably about 0.0004 to about 0.002%. Present at the level.

[0186] Other isothiazolines, commercially available under the trade name Proxel ^R product on commercially available 1,2-benzisothiazolin-3-one, and trade name Promexal ^R 2-
There is methyl-4,5-trimethylene-4-isothiazolin-3-one. Proxel
And Promexal are both commercially available from Zeneca. They are stable over a wide pH range (ie, 4-12). Neither contains active halogens and is not a formaldehyde releasing preservative. Both Proxel and Promexal have about 0.5% of the composition used.
Typical gram-negative and Effective against positive bacteria, fungi and yeast.

(B) Sodium pyrithione Another preferred organic sulfur preservative is sodium pyrithione, which has a water solubility of about 50%. When sodium pyrithione is used as a preservative in the present invention, it is typically from about 0.0001 to about 0.01% by weight of the use composition, preferably from about 0.0002 to about 0.005%, more preferably Present at a level of about 0.0003 to about 0.003%. Mixtures of the preferred organic sulfur compounds can also be used as preservatives in the present invention.

(2) Halogenated Compound A preferable preservative for use in the present invention is a halogenated compound. Some non-limiting examples of halogenated compounds suitable for use in the present invention are the following: Henkel is commercially available as trade name Bronidox L ^R from 5-bromo-5-nitro-1,3-dioxane. Bronidox ^LR has a solubility of about 0.46% in water. When Bronidox is used as a preservative in the present invention, it typically comprises from about 0.0005 to about 0.02% by weight of the use composition, preferably from about 0.001 to about 0.02%.
Present at 1% level.

2-Bromo-2-nitropropane-1,3-diol, commercially available from Inolex under the trade name Bronopol ^R , can be used as a preservative in the present invention. Bronopol has a solubility in water of about 25%. When Bronopol is used as a preservative in the present invention,
It typically comprises about 0.002 to about 0.1% by weight of the use composition, preferably about 0 to about 0.1%.
. It is present at a level of from 005 to about 0.05%.

1,1′-hexamethylenebis [5, commonly known as chlorhexidine
-(P-chlorophenyl) biguanide], and salts thereof, such as salts with acetic acid and gluconic acid, can be used as preservatives in the present invention. Digluconate is about 70 in water
%, And the diacetate has a solubility in water of about 1.8%. When chlorhexidine is used as a preservative in the present invention, it is typically from about 0.0001 to about 0.04% by weight of the use composition, preferably from about 0.0005 to about 0.5%.
Present at 01% level.

[0191] 1,1,1-- having a water solubility of about 0.8%, commonly known as chlorobutanol
Typical effective levels of trichloro-2-methylpropan-2-ol; chlorobutanol are from about 0.1 to about 0.5% by weight of the use composition.

4,4 '-(trimethylenedioxy) bis (3-bromobenzamidine) diisethionate or dibromopropamidine having a water solubility of about 50%; when dibromopropamidine is used as a preservative in the present invention, it is typically Typically, it is present at a level of from about 0.0001 to about 0.05%, preferably from about 0.0005 to about 0.01% by weight of the use composition. Mixtures of the preferred halogenated compounds can also be used as preservatives in the present invention.

(3) Cyclic Organic Nitrogen Compound A preferred water-soluble preservative for use in the present invention is a cyclic organic nitrogen compound. Some non-limiting examples of cyclic organic nitrogen compounds suitable for use in the present invention are as follows: (a) Imidazolidinedione Compounds Preferred preservatives for use in the present invention are imidazolidione compounds. Some non-limiting examples of imidazolidinedione compounds suitable for use in the present invention are the following: for example, is commercially available as Glydant ^R from Lonza, was commonly known as dimethyloldimethylhydantoin, or DMDM hydantoin 1,3 -Screw(
(Hydroxymethyl) -5,5-dimethyl-2,4-imidazolidinedione. DM
DM hydantoin has a water solubility of more than 50% in water and is mainly effective against bacteria. When DMDM hydantoin is used, it is preferably used in combination with a broad spectrum preservative such as Kathon CG ^R or formaldehyde. A preferred mixture is commercially available from Lonza under the trade name Glydant Plus ^R , about 95:
5 DMDM hydantoin versus 3-butyl-2-iodopropynyl carbamate mixture. When Glydant Plus ^R is used as a preservative in the present invention, it is typically present at a level of from about 0.005 to about 0.2% by weight of the use composition.

N- [1,3-bis (hydroxymethyl) -2,5-dioxo, commonly known as diazolidinyl urea, commercially available under the trade name Germall II ^R from Sutton Laboratories, Inc. (Sutton) -4-imidazolidinyl] -N, N'-bis (
(Hydroxymethyl) urea can also be used as a preservative in the present invention. When Germall II ^R is used as a preservative in the present invention, it typically comprises from about 0.01 to about 0.01% of the use composition.
It is present at a level of about 0.1% by weight. For example, under the trade name Abiol from 3V-Sigma ^R, Unicide from Induchem U-13 ^R, (Sutto
n) it is commercially available as Germall 115 ^R from, N, which is commonly known as imidazolidinyl urea, N "- methylenebis [N '- [1- (hydroxymethyl) -2
, 5-Dioxo-4-imidazolidinyl] urea] can be used as a preservative in the present invention. When imidazolidinyl urea is used as a preservative, it is typically present at a level of from about 0.05 to about 0.2% by weight of the use composition. Mixtures of the preferred imidazolidinedione compounds can also be used as preservatives in the present invention.

(B) Polymethoxy Bicyclic Oxazolidine Another preferred water-soluble cyclic organic nitrogen preservative is a polymethoxy bicyclic oxazolidine having the general formula:

Embedded image (Where n has a value of about 0 to about 5) and is available from Huls America under the trade name Nu
It is commercially available as osept ^{R C.} When Nuosept ^{R C} is used as a preservative,
It is typically present at a level of from about 0.005 to about 0.1% by weight of the use composition. Mixtures of the preferred cyclic organic nitrogen compounds can also be used as preservatives in the present invention.

(4) Low-Molecular-Weight Aldehyde (a) Formaldehyde A preferred preservative for use in the present invention is formaldehyde. Formaldehyde is a broad spectrum preservative and is commonly marketed as formalin, a 37% aqueous solution of formaldehyde. When formaldehyde is used as a preservative in the present invention, typical levels are from about 0.003 to about 0.2% by weight of the use composition
, Preferably about 0.008 to about 0.1%, more preferably about 0.01 to about 0.0%.
5%.

(B) Glutaraldehyde A preferable preservative for use in the present invention is glutaraldehyde. Glutaraldehyde is a water-soluble, broad spectrum preservative, commonly marketed as a 25-50% solution in water. When glutaraldehyde is used as a preservative in the present invention, it is typically present at a level of from about 0.005 to about 0.1% by weight of the use composition, preferably from about 0.01 to about 0.05%. I do.

(5) Quaternary Compounds Preservatives preferred for use in the present invention are cationic and / or quaternary compounds. Such compounds include polyaminopropyl biguanides, also known as polyhexamethylene biguanides having the general formula: HCl.NH ₂ — (CH ₂ ) ₃ -[— (CH ₂ ) ₃ —NH—C (= NH) -NH
-C (= NH.HCl) -NH- (CH ₂ ) _3- ] _x- (CH ₂ ) ₃ -NH-C
(= NH) -NH.CN polyaminopropyl biguanide is available from ICI Americas, Inc. under the trade name Cosmocil
CQ ^R or Brooks, Inc., Commercially available as a 20% aqueous solution under the trade name Mikrokill ^R from a water-soluble broad spectrum preservative. For example, 1- (3-
Chlorallyl) -3,5,7-triaza-1-azoniaadamantanchloride is an effective quaternary ammonium preservative, which is readily soluble in water, however, it has a tendency to discolor (yellowing) And therefore not highly desirable. Mixtures of the preferred quaternary ammonium compounds can also be used as preservatives in the present invention. When quaternary ammonium compounds are used as preservatives in the present invention, they will typically contain from about 0.005 to about 0.2% by weight of the use composition, preferably from about 0.01 to about 0.2%.
Present at a level of about 0.1%.

(6) Dehydroacetic acid A preferred preservative for use in the present invention is dehydroacetic acid. Dehydroacetic acid is a broad spectrum preservative, preferably in the form of a sodium or potassium salt, so that it is water soluble. This preservative acts as a biostatic preservative rather than a biocidal preservative. When dehydroacetic acid is used as a preservative, it typically comprises from about 0.005 to about 0.2% by weight of the use composition, preferably from about 0.008 to about 0.2%.
It is used at a level of about 0.1%, more preferably about 0.01 to about 0.05%.

(7) Phenyl and phenolic compounds Some non-limiting examples of phenyl and phenolic compounds suitable for use in the present invention are as follows: Commonly known as propamidine isethionate with a water solubility of about 16%. 4,
4'-diamidino-α, ω-diphenoxypropane diisethionate; 4,4'-diamidino-α, ω-diphenoxyhexane diisethionate commonly known as hexamidine isethionate. Typical effective levels of these salts are from about 0.0002 to about 0.05% by weight of the use composition. Other examples are benzyl alcohol with a water solubility of about 4%, 2-phenylethanol with a water solubility of about 2%, and 2-phenoxyethanol with a water solubility of about 2.67%, the typical effectiveness of these phenyl and phenoxy alcohols. Levels are from about 0.1 to about 0.5% by weight of the use composition.

(8) Mixtures thereof

It is preferred that volatile low molecular weight monohydric alcohols such as ethanol and / or isopropanol are not intentionally added or essentially not added to the compositions of the present invention because of their volatile nature. This is because the volatile organic compound is involved in both the flammability problem and the environmental pollution problem. Due to the addition of small amounts of low molecular weight monohydric alcohols to such things as stabilizers for perfume and preservatives,
If present in the compositions of the present invention, it is preferred that the level of monohydric alcohol be less than about 5% by weight, preferably less than about 3%, and more preferably less than about 1%.

(9) Mixtures thereof The preservatives of the present invention can be used in mixtures to control a wide range of microorganisms. The bacteriostatic effect is achieved by adjusting the composition pH to an acidic pH, for example, less than about pH 4, preferably less than about pH 3, or a basic pH, for example, about 10 or more, preferably about 11 or more,
Sometimes obtained with aqueous compositions.

(10 ) Preferred preservatives Preferably, the preservatives used in the composition of the present invention include isothiazolones, bronopol, hydantoins, oxazolidines, glutaraldehyde, isethionates, quats (benzalkoniums) and Selected from the group consisting of mixtures thereof.

Other ingredients such as soil suspending agents, soil release agents, optical brighteners, abrasives, bactericides, haze inhibitors, coloring agents and / or encapsulated or unencapsulated fragrances can also be used. A particularly suitable encapsulating material is a water-soluble capsule consisting of a matrix of a polysaccharide and a polyhydroxy compound as described in GB 1,464,616. Other suitable water-soluble encapsulating materials include dextrins derived from non-gelatinized starch esters of substituted dicarboxylic acids, as described in US Pat. No. 3,455,838. These acid ester dextrins are preferably made from starches such as waxy maize, waxy sorghum, sago, tapioca and potato. A suitable example of the encapsulating material is N-Lok from National Starch.
The N-Lok encapsulant consists of modified maize starch and glucose. Starch is modified by adding a monofunctional substituent such as octenyl succinic anhydride.

Suitable anti-redeposition and soil suspending agents herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or copolymer polycarboxylic acids or salts thereof. Polymers of this type include polyacrylates and maleic anhydride-acrylic acid copolymers already described as builders, and maleic anhydride and ethylene,
There are copolymers with methyl vinyl ether or methacrylic acid, with maleic anhydride accounting for at least 20 mol% of the copolymer. These materials are generally used at levels of 0.5 to 10%, more preferably 0.75 to 8%, most preferably 1 to 6% by weight of the composition.

Preferred optical brighteners are anionic in nature, examples of which are 4,4'-bis (2
-Diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate disodium, 4,4'-bis (2-morpholino-4-anilino-s-triazin-6-ylamino ) Stilbene-2,2'-
Disodium disulfonate, disodium 4,4'-bis (2,4-dianilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate,
', 4 "-bis (2,4-dianilino-s-triazin-6-ylamino) stilbene-2-sulfonic acid monosodium salt, 4,4'-bis [2-anilino-4- (
N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylamino] stilbene-2,2'-disulfonate disodium, 4,4'-bis (4
-Phenyl-2,1,3-triazol-2-yl) stilbene-2,2'-disulfonate, 4,4'-bis [2-anilino-4- (1-methyl-
2-hydroxyethylamino) -s-triazin-6-ylamino] stilbene-2,2'-disulfonate disodium salt, 2-stilbyl-4 "-(naphtho-1
', 2', 4,5) -1,2,3-Triazole-2 "-sodium sulfonate and 4,4'-bis (2-sulfostyryl) biphenyl. Highly preferred brighteners are Certain brighteners from pending European patent application 952020943.8.

Other useful polymeric substances are polyethylene glycols, especially molecular weights between 1000 and 1
0000, more specifically 2000-8000, most preferably about 4000. These are used at a level of from 0.20 to 5% by weight, more preferably from 0.25 to 2.5%. These polymers, and the previously described homo or copolymer polycarboxylate salts, provide whiteness maintenance, fabric ash adhesion (fabric ash).
deposition) and in the presence of transition metal impurities to improve cleaning performance on soil, proteins and oxidizing soils.

The soil release agents useful in the compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid and ethylene glycol and / or propylene glycol units in various configurations. Examples of such polymers are described in commonly assigned U.S. Pat. Nos. 4,116,885 and 4,711,730 and European Patent Application 0,2.
72,033. A particularly preferred polymer according to EP-A-0,272,033 has the formula: (CH ₃ (PEG) ₄₃ ) _0.75 (POH) _0.25 [(T-PO) _2.8 (T-PEG) _0.4 ] T (POH) _0.25 ((PEG) ₄₃ CH ₃ ) _{0.75 wherein} PEG is — (OC ₂ H ₄ ) O—, PO is (OC ₃ H ₆ O), and T is (pcOC ₆ H ₄ CO). .

Modified polyesters are also very useful as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1,2-propanediol, with the end groups being mainly sulfobenzoate, and secondarily ethylene glycol and / or Or it consists of a monoester of propanediol. The purpose is to obtain a polymer capped at both ends by sulfobenzoate groups, in the present context most of the copolymers being "mainly" end-capped with sulfobenzoate groups. However, some copolymers are not completely capped, so their end groups may consist of monoesters of ethylene glycol and / or propane-1,2-diol,
"Secondary" consists of such species. The polyester selected here is about 46% by weight dimethyl terephthalic acid, about 1%.
6% by weight of propane-1,2-diol, about 10% by weight of ethylene glycol,
It contains about 13% by weight dimethylsulfobenzoic acid and about 15% by weight sulfoisophthalic acid and has a molecular weight of about 3000. Polyesters and their methods of manufacture are described in detail in EPA 311,342.

It is well known in the art that free chlorine in tap water rapidly inactivates enzymes contained in laundry detergents and / or fabric care compositions. Thus, when a chlorine scavenger such as perborate, ammonium sulfate, sodium sulfite or polyethyleneimine is used in a formulation at a level of 0.1% or more by weight of the total composition, an improved through-the-wash of detergent enzymes ( throuth the wash) provides stability. Compositions containing chlorine scavengers are described in European Patent Application 928700188.6, filed January 31, 1992.

[0212] Alkoxylated polycarboxylates, such as those made from polyacrylates, are useful herein to provide additional fat removal performance. Such materials are described in WO 91/08281 and PCT9, which are incorporated herein by reference.
0/01815 on page 4 et seq. Chemically, these substances are 7-
Consists of a polyacrylate with one ethoxy side chain for every eight acrylate units. Side chain of the formula _- consists _{(CH 2 CH 2 O) m} (CH 2) n CH 3, wherein m
Is 2-3 and n is 6-12. The side chains are esterified to the polyacrylate “backbone” to form a “comb” polymer type structure. Molecular weights vary, but typically range from about 2000 to about 50,000. Such alkoxylated polycarboxylates comprise from about 0.05% to about 10% by weight of the composition.
It is.

Cleaning Methods The laundry detergent and / or fabric care compositions of the present invention include dipping methods, pre-treatment methods, methods involving a rinsing step in which another rinse aid composition may be added, and post-treatment methods. May be used in essentially any cleaning, cleaning and / or fabric care method. An example of a pretreatment comprises treating the fabric with a pretreatment composition containing a transferase and / or a corresponding enzyme substrate. This step may be performed earlier in a washing machine or bowl, or the pretreatment composition may be sprayed onto the fabric. Optionally, the pretreated fabric is dried and then washed / treated with a conventional laundry detergent and / or fabric care composition (containing neither the transferase nor the substrate of the present invention). Examples of post-treatments consist of washing / treating the fabric with a conventional laundry detergent and / or fabric care composition (containing neither the transferase nor the substrate of the present invention). Optionally, the fabric is dried. The fabric is then treated with a post-treatment composition containing the transferase and / or the corresponding enzyme substrate. The transferase and / or the corresponding enzyme substrate may be incorporated into the rinse composition used at the end of the wash cycle. In other examples, the enzyme and substrate are contained in different compositions and / or are added at different steps. For example, pre- or post-treatment compositions exclusively contain the transferase enzyme and / or the corresponding enzyme substrate, and conventional laundry detergent and / or fabric care compositions exclusively contain the corresponding enzyme substrate or transferase enzyme. . The process described herein consists in contacting the fabric with the washing liquid in a conventional manner,
This is illustrated below. The process of the present invention is conveniently performed during the cleaning process. The cleaning method is preferably 5 to 95 ° C, particularly 10 to 60 ° C.
Performed at ° C. The pH of the treatment solution is preferably 7-12.

The following examples are meant to illustrate the compositions of the present invention and do not necessarily limit or limit the scope of the present invention. In laundry detergent and / or fabric care compositions, enzyme levels are expressed as pure enzyme by weight of total composition, and unless otherwise noted, detergent components are expressed by weight of total composition. The abbreviated component designations have the following meanings: LAS: Sodium linear C _11-13 alkyl benzene sulfonate TAS: Sodium tallow alkyl sulfate CxyAS: Sodium C _1x -C _1Y alkyl sulfate CxySAS: Sodium C _1X -C _1Y secondary (2,3) alkyl sulfates CxyEz: mean z moles of ethylene oxide condensed with C _1X -C _1Y primarily for linear primary alcohol CxyEzS: C _1X -C _1Y sodium was condensed with an average z moles of ethylene oxide Alkyl sulfate QAS: R ₂ N ⁺ (CH ₃ ) ₂ (C ₂ H ₄ OH) (R ₂ = C ₁₂ -C ₁₄ ) QAS 1: R ₂ N ⁺ (CH ₃ ) ₂ (C ₂ H ₄ OH) (R ₂ = C ₈ -C ₁₁ ) APA: C _8-10 amidopropyldimethylamine Soap: 80 / of tallow and coconut fatty acids 20 mixing sodium linear alkyl carboxylate derived from compounds STS: Sodium toluene sulphonate CFAA: C ₁₂ -C ₁₄ alkyl N- methyl glucamide TFAA: C ₁₆ -C ₁₈ alkyl N- methyl glucamide TPKFA: C ₁₂ -C ₁₄ Topped whole cut fatty acid DEQA: di (tallowoxyethyl) dimethylammonium chloride DEQA (2): di (soft tallowyloxyethyl) hydroxyethylmethyl ammonium methyl sulfate DTDMAMS: ditallow dimethyl ammonium methyl sulfate SDASA: 1: 2 ratio of stearyl dimethyl amine: triple-Puresudo (triple Pressed accompanied by) stearate silicate: amorphous sodium silicate (SiO _2: Na ₂ O ratio = 1.6-3.2) Seolla Preparative A: formula _{Na 12 (AlO 2 SiO 2)} 12 · 27H 2 O of hydrated sodium aluminosilicate (wt displayed on a dry basis) Na-SKS-6 having a main particle size of 0.1~10μm Range: wherein δ -Layered silicate citrate of Na ₂ Si ₂ O ₅ : trisodium citrate dihydrate having a particle size distribution of 425 to 850 μm and having an activity of 86.4% citric acid: anhydrous citric acid borate: sodium borate carbonate : Anhydrous sodium carbonate bicarbonate having a particle size of 200 to 900 μm: anhydrous sodium hydrogen carbonate having a particle size distribution of 400 to 1200 μm sulfate: anhydrous sodium sulfate magnesium: anhydrous magnesium sulfate STPP: sodium tripolyphosphate TSPP: tetrasodium pyrophosphate MA / AA : Random copolymer of 4: 1 acrylate / maleate average molecular weight About 70,000-80,000 MA / AA 1: 6: 4 acrylate / maleate random copolymer Average molecular weight about 10,000 AA: sodium polyacrylate polymer with average molecular weight of 4500 PB1: empirical formula of NaBO ₂ .H ₂ O ₂ anhydrous sodium perborate monohydrate PB4: empirical formula _{NaBO 2 · 3H 2 O · H} 2 O 2 of sodium perborate tetrahydrate percarbonate: over anhydrous empirical formula _{2Na 2 CO 3 · 3H 2 O} 2 Sodium carbonate TAED: Tetraacetylethylenediamine NOBS: Nonanoyloxybenzenesulfonate in sodium salt form NACA-OBS: (6-nonamidocaproyl) oxybenzenesulfonate DTPA: Diethylenetriaminepentaacetic acid HEDP: 1,1-hydroxyethanediphosphonic acid DETPMP: Monsanto Diethyltriaminepenta (methylene) phosphonate sold under the trade name Dequest 2060 EDDS: (S, S) isomer of ethylenediamine-N, N'-disuccinic acid in its sodium salt form Light activated bleach: in dextrin soluble polymer Sulfonated Zinc Phthalocyanine Encapsulated in Light-Activated Bleach 1: Sulfonated Aluminophthalocyanine Protease Encapsulated in Dextrin Soluble Polymer Protease: Proteolytic enzyme sold under the trade names Savinase, Alcalase, and Durazym from Novo Nordisk A / S; Gist-Brocades sold by Maxacal, Maxapem; and patent WO91 / 06637 and / or WO95 / 10591 and / or protease-amylase described in EP251446: sold under the trade name Purafact Ox Am ^R from Genencor WO94 / 8314, WO96 / amylolytic enzymes is described in the 05295; all Novo Nordisk A / S Termamyl commercially available from ^R, Fungamyl ^R and Duramyl ^R; and lipase those described in WO95 / 26397: from Novo Nordisk A / S Lipoase, a lipolytic enzyme sold under the trade name Lipolase Ultra, and a Lipomax CBD-transferase by Gist-Brocades: sold under the trade name Cellulose Binding Domain from Sigma, into a CBD Cellulozome from Clostridium cellulovorans, Sigma PEG (NPC) ₂ MW3400 from Sigma; Transferase EC 2.4.1.5 sold by Sigma under the trade name dextransucrase; Transferase sold by Novo Nordisk A / S under the trade name Transglutaminase -Transfers sold under the trade name Toruzyme from Ze EC 2.3.2.13 and / or Novo Nordisk A / S EC 2.4.1.19; and / or sold by Sigma under the trade name dextransucrase linked to the cellulolytic enzyme CBD sold by Novo Nordisk A / S under the trade name Carezyme via the Humicola insolens family 45 cellulase linker Transferase EC 2.4.1.5 substrate: Maltose, such as Maltose M5885 and / or starch, such as Sigma, sold by Sigma; YES2760, sold by Sigma; amino acids, di / tri / polypeptides and / or proteins and / or cyclodextrins (Α, β, γ) and / or sucrose cellulase: Cellulolytic enzyme sold by Novo Nordisk A / S under the trade names Carezyme, Celluzyme and / or Endolase CMC: Sodium carboxymethylcellulose PVP: Polyvinyl of average molecular weight 60,000 Polymer PVNO: average molecular weight 50,000 polyvinylpyridine-N-oxide PVPVI: a copolymer of vinylimidazole and vinylpyrrolidone with an average molecular weight of 20,000 Brightener 1: Brightener 2,4'-bis (2-sulfostyryl) biphenyl disodium brightener 2: Disodium 4,4'-bis (4-anilino-6-morpholino-1,3,5-triazin-2-yl) stilbene-2,2'-disulfonate Silicone defoamer: 10: 1 to 100: 1 A polydimethylsiloxane foam modifier blended with a siloxaneoxyalkylene copolymer as a dispersant at a ratio of foam modifier to dispersant of the following: Foaming inhibitor: granular, 12% silicone / silica, 18% stearyl alcohol, 70% % Starch opacifier: sold by BASF Aktiengesellschaft under the trade name Lytron 621 Water based monostyrene latex mixture SRP1: anionic end-capped polyester SRP2: diethoxylated poly (1,2-propylene terephthalate) short block polymer QEA: bis _{[(C 2 H 5 O) (} C 2 H 4 O) n ] (CH ₃ ) -N ⁺ -C ₆ H ₁₂ -N ⁺ -(CH ₃ ) bis [(C ₂ H ₅ O) (C ₂ H ₄ O)] _n (n = 20-30) PEI: average of 1800 Polyethyleneimine having a molecular weight and an average degree of ethoxylation of 7 ethyleneoxy residues per nitrogen SCS: Sodium cumene sulfonate HMWPEO: High molecular weight polyethylene oxide PEGx: Polyethylene glycol having a molecular weight x PEO: Polyethylene oxide having an average molecular weight of 5000 TEMPAE: Tetraethylene penta Amine ethoxylate

Example 1 The following high density laundry detergent composition was prepared in accordance with the present invention: I II III IV V VI
LAS 8.0 8.0 8.0 2.0 6.0 6.0 TAS-0.5-0.5 1.0 0.1 C46 (S) AS 2.0 2.5----C25AS---7.0 4.5 5.5 C68AS 2.0 5.0 7.0---C25E5--3.4 10.0 4.6 4.6 C25E7 3.4 3.4 1.0 ---C25E3S---2.0 5.0 4.5 QAS-0.8----QAS1---0.8 0.5 1.0 Zeolite A 18.1 18.0 14.1 18.1 20.0 18.1 Citric acid---2.5-2.5 Carbonate 13.0 13.0 27.0 10.0 10.0 13.0 Na- SKS-6---10.0-10.0 Silicate 1.4 1.4 3.0 0.3 0.5 0.3 Citrate-1.0-3.0--Sulfate 26.1 26.1 26.1 6.0--Mg sulfate 0.3--0.2-0.2 MA / AA 0.3 0.3 0.3 4.0 1.0 1.0 CMC 0.2 0.2 0.2 0.2 0.4 0.4 PB4 9.0 9.0 5.0---Percarbonate----18.0 18.0 TAED 1.5 0.4 1.5-3.9 4.2 NACA-OBS-2.0 1.0---DETPMP 0.25 0.25 0.25 0.25--SRP1---0.2-0.2 EDDS -0.25 0.4-0.5 0.5 CFAA-1.0-2.0-- EDP 0.3 0.3 0.3 0.3 0.4 0.4 QEA---0.2-0.5 CBD-transferase 1.0 0.1 0.05 0.02 0.1 0.5 Substrate 0.1-5.0-10.0 15.0 Protease 0.009 0.009 0.01 0.04 0.05 0.03 Amylase 0.002 0.002 0.002 0.006 0.008 0.008 Cellulase 0.0007--0.0007 0.0007 0.0007
Lipase 0.006--0.01 0.01 0.01 Light activated bleach (ppm) 15 15 15-20 20 PVNO / PVPVI---0.1--Brightener 1 0.09 0.09 0.09-0.09 0.09 Fragrance 0.3 0.3 0.3 0.4 0.4 0.4 Silicone defoamer 0.5 0.5 0.5-0.3 0.3 Density g / L 850 850 850 850 850 850 850 Others Up to 100%

Example 2 The following granular laundry detergent compositions particularly useful under European machine wash conditions were prepared according to the present invention: I II III IV V VI
LAS 5.5 7.5 5.0 5.0 6.0 7.0 TAS 1.25 1.9-0.8 0.4 0.3 C24AS / C25AS-2.2 5.0 5.0 5.0 2.2 C25E3S-0.8 1.0 1.5 3.0 1.0 C45E7 3.25----3.0 TFAA--2.0---C25E5-5.5--- -QAS 0.8-----QAS1-0.7 1.0 0.5 1.0 0.7 STPP 19.7-----Zeolite A-19.5 25.0 19.5 20.0 17.0 NaSKS-6 / citric acid (79:21)-10.6-10.6--Na-SKS -6--9.0-10.0 10.0 Carbonate 6.1 21.4 9.0 10.0 10.0 18.0 Bicarbonate-2.0 7.0 5.0-2.0 Silicate 6.8--0.3 0.5-Citrate--4.0 4.0--Sulfate 39.8--5.0-12.0 Mg sulfate-- 0.1 0.2 0.2-MA / AA 0.5 1.6 3.0 4.0 1.0 1.0 CMC 0.2 0.4 1.0 1.0 0.4 0.4 PB4 5.0 12.7----Percarbonate----18.0 15.0 TAED 0.5 3.1--5.0-NACA-OBS 1.0 3.5--- 2.5 DETPMP 0.25 0.2 0.3 0.4-0.2 HEDP-0.3-0.3 0.3 0.3 QEA--1.0 1.0 1.0-CBD-transferase 0.02 1.5 0.1 0.5 0.0008 0.02 substrate-0.1 5.0 10.0 12.0 0.1 protease 0.009 0.03 0.03 0.05 0.05 0.02 lipase 0.003 0.003 0.006 0.006 0.006 0.004 cellulase 0.0006 0.0006 0.0005 0.0005 0.0007 0.0007
Amylase 0.002 0.002 0.006 0.006 0.01 0.003 PVNO / PVPVI--0.2 0.2--PVP 0.9 1.3---0.9 SRP1--0.2 0.2 0.2-Light activated bleach (ppm) 15 27--20 20 Light activated bleach (1) (ppm) 15-----Brightener 1 0.08 0.2--0.09 0.15 Brightener 2-0.04----Fragrance 0.3 0.5 0.4 0.3 0.4 0.3 Silicone defoamer 0.5 2.4 0.3 0.5 0.3 2.0 Density g / L 750 750 750 750 750 750 Others up to 100%

Example 3 The following detergent compositions which are particularly useful under European machine wash conditions were prepared according to the present invention: I II III IV
Blown Powder: LAS 6.0 5.0 11.0 6.0 TAS 2.0--2.0 Zeolite A 24.0--20.0 STPP-27.0 24.0-Sulfate 4 6.0 6.0 13.0-MA / AA 1.0 4.0 6.0 2.0 silicate 1.0 7.0 3.0 3.0 3.0 CMC 1.0 1.0 0.5 0.6 Brightener 1 0.2 0.2 0.2 0.2 Silicone defoamer 1.0 1.0 1.0 0.3 DETPMP 0.4 0.4 0.2 0.4 Spray-on: Brightening 0.02 --- 0.02 C45E7 --- 5.0 C45E2 2.5 2.5 2.0-C45E3 2.6 2.5 2.0-Fragrance 0.5 0.3 0.5 0.0. 2 Silicone defoamer 0.3 0.3 0.3-Dry additive: QEA---1.0 EDD 0.3---Sulfate 2.0 3.0 5.0 10.0 Carbonate 6.0 13.0 15.0 14.0 Citric acid 2.5--2.0 QAS1 0.5--0 5.5 Na-SKS-6 10.0----Percarbonate 18.5----PB4-18.0 10.0 21.5 TAED 2.0 2.0-2.0 NACA-OBS 3.0 2 0.0 4.0-CBD-transferase 0.005 1.0 0.1 0.2 Substrate-0.1 10.0 10.0 Protease 0.03 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 0.004 Amylase 0.003 0.003 0.003 0.006 Brightener 1 0.05--0.05
Others up to 100%

Example 4 The following granular detergent composition was prepared according to the present invention: I II III IV V VI
Blown powder: LAS 23.0 8.0 7.0 9.0 7.0 7.0 TAS----1.0-C45AS 6.0 6.0 5.0 8.0--C45AES-1.0 1.0 1.0--C45E35----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 / AA1 7.0-------AA-3.0 3.0 2.0 3.0 3.0 Sulfate 5.0 6.3 14.3 11.0 15.0 19.3 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 Brightener 2 0.3 0.2 0.3-0.1 0.3 Spray on: C45E7-2.0--2.0 2.0 C25E9 3.0------C23E9--1.5 2.0-2.0 Fragrance 0.3 0.3 0.3 2.0 0.3 0.3 Aggregate : 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 Carbonate-4.0 4.0 5.0-4.0 PEG4000-0.5 0.5--0.5 Others (water, etc.)-2.0 2.0 2.0-2.0 Dry additives: QAS-----1.0-Citric acid-----2.0-PB4-----12.0 1.0 PB1 4.0 1.0 3.0 2.0---Percarbonate---- -2.0 10.0 Carbonate-5.3 1.8-4.0 4.0 NOBS 4.0-6.0--0.6 Methylcellulose 0.2------Na-SKS-6 8.0------STS--2.0-1.0-Cumenesulfonic acid-1.0--- -2.0 CBD-transferase 0.025 0.8 0.5 0.01 0.025 0.8 Substrate-0.1 10.0 5.0 0.02-Protease 0.02 0.02 0.02 0.01 0.02 0.02 Lipase 0.004-0.004-0.004 0.008 Amylase 0.003-0.002-0.003-Cellulase 0.0005 0.0005 0.0005 0.0007 0.0005 0.0005 PVPVI--- -0.5 0.1 PVP-----0.5-PVNO--0.5 0.3--QEA------1.0-SRP1 0.2 0.5 0.3-0.2-Silicone Foams 0.2 0.4 0.2 0.4 0.1 - sulfate Mg - - 0.2 - 0.2 - to other 100%

Example 5 The following bleach-free detergent compositions which are particularly useful for washing colored garments were prepared according to the present invention: I II III Blown powder: Zeolite A 15.0 15.0-Sulfate-5.0-LAS 3 3.0 3.0-DETPMP 0.4 0.5-CMC 0.4 0.4-MA / AA 4.0 4.0-Aggregate: C45AS--11.0 LAS 6.0 5.0-TAS 3.0 2.0-Silicate 4.0 4.0-Zeolite A 10.0 15.0 13.0 CMC--0.5 MA / AA--2.0 Carbonate 9.0 7.0 7.0. 0 Spray-on: Fragrance 0.3 0.3 0.5 C45E7 4.0 4.0 4.0 C25E3 2.0 2.0 2.0 Dry additive: MA / AA--3.0 Na-SKS- 6--12.0 citrate 0.0-8.0 Bicarbonate 7.0 3.0 5.0 Carbonate 8.0 5.0 7.0 PVPVI / PVNO 0.5 0.5 0.5 CBD-transferase 0.001 1. 0 0.01 Substrate 0.1-5.0 Protease 0.03 0.02 0.05 Lipase 0.008 0.008 0.008 Amylase 0.01 0.01 0.01 0.01 Cellulase 0.001 0.0010 0.001 Silicone antifoaming agent 5.0 5.0 5.0 Sulfate-9.0-Density (g / L) 700 700 700 700 Others up to 100%

[0220] Example 6 The following detergent composition was prepared in accordance with the present invention: I II III IV Base granule Zeolite A 30.0 22.0 24.0 10.0 sulfate 10.0 5.0 10.0 7.0 MA / AA 3.0 - - - AA - 1.6 2.0 - MA / AA1 -12.0-6.0 LAS 14.0 10.0 9.0 20.0 C45AS 8.0 7.0 9.0 7.0 C45AES-1.0 1.0-Silicate-1.0 0.5 10.0 Soap-2.0--Brightener 1 0.2 0.2 0.2 0.2 Carbonate 6.0 9.0 10.0 10.0 PEG4000-1.0 1.5-DTPA- 0.4--Spray-on: C25E9---5.0 C45E7 1.0 1.0--C23E9-1.0 2.5-Fragrance 0.2 0.3 0.3-Dry additive: Carbonate 5.0 10.0 18.0 8.0 PVPVI / PVNO 0.5-0.3-CBD-transferase 1.0 0.01 0.5 0.1 Substrate 0.1-10.0 10.0 Protease 0.03 0.03 0.03 0.02 Lipase 0.008--0.008 Amylase 0.002--0.002 Cellulase 0.0002 0.0005 0 .0005 0.0002 NOBS-4.0-4.5 PB1 1.0 5.0 1.5 6.0 Sulfate 4.0 5.0-5.0 SRP1-0.4--Foaming inhibitor-0.5 0.5-Others up to 100%

Example 7 The following granular detergent composition was prepared in accordance with the present invention: I II III Blown powder: Zeolite A 20.0-15.0 STPP-20.0-Sulfate-5.0 Carbonate-5 1.0 TAS--1.0 LAS 6.0 6.0 6.0 C68AS 2.0 2.0-Silicate 3.0 8.0-MA / AA 4.0 2.0 2.0 CMC 0.6 0.6 0.2 Brightener 1 0.2 0.2 0.1 DETPMP 0.4 0.4 0.1 STS --- 1.0 Spray-on: C45E7 5.0 5.0 4.0 Silicone Foaming agent 0.3 0.3 0.1 Fragrance 0.2 0.2 0.3 Dry additive: QEA--1.0 Carbonate 14.0 9.0 10.0 10.0 PB1 1.5 2.0- PB4 18.5 13.0 13.0 TAED 2.0 2.0 2.0 QAS--1.0 Light-activated bleach 15 ppm 15 ppm 15 ppm Na-SKS-6--3.0 CBD-transferase 0.001 1.0 0.01 Substrate--5.0 Protease 0.03 0.03 0.007 Lipase 0.004 0.004 0.004 Amylase 0.006 0.006 0.003 Cellulase 0.0002 0.0002 0.0005 Sulfate 10.0 20.0 5.0 Density (g / L) 700 700 700 Others up to 100%

Example 8 The following detergent composition was prepared in accordance with the present invention: I II III Blown Powder: Zeolite A 15.0 15.0 15.0 Sulfate-5.0-LAS 3.0 3.0 QAS-1.5 1.5 DETPMP 0.4 0.2 0.4 EDDS-0.4 0.2 CMC 0.4 0.4 0.4 MA / AA 4.0 2.0 2.0 Aggregate : LAS 5.0 5.0 5.0 TAS 2.0 2.0 1.0 silicate 3.0 3.0 4.0 Zeolite A 8.0 8.0 8.0 Carbonate 8.0 8.0 4.0 Spray-on: Perfume 0.3 0.3 0.3 C45E7 2.0 2.0 2.0 C25E3 2.0 --- Dry additive: Citrate 5.0-2.0 Bicarbonate --3. 0-carbonate 8.0 15.0 10.0 TAED 6.0 2.0 5.0 PB1 14.0 7.0 10.0 PEO--0.2 Bentonite clay--10.0 CBD-transferase 0.025 0.5 0.1 Substrate 0.01-12.0 Protease 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 Cellulase 0.001 0.001 0.001 Amylase 0.01 0.01 0.01 Silicone Defoamer 5.0 5.0 5.0 Sulfate -3.0-Density (g / L) 850 850 850 Others Up to 100%

Example 9 The following detergent composition was prepared in accordance with the present invention: I II III IV
LAS 18.0 14.0 24.0 20.0 QAS 0.7 1.0-0.7 TFAA-1.0--C23E56.5--1.0-C45E7-1.0--C45E3S 0 2.5 1.0-STPP 32.0 18.0 30.0 22.0 Silicate 9.0 5.0 9.0 8.0 Carbonate 11.0 7.5 10.0 5.0 Bicarbonate Salt-7.5--PB1 3.0 1.0--PB4-1.0--NOBS 2.0 1.0--DETPMP-1.0--DTPA 0.5-0.2 0.3 SRP1 0.3 0.2-0.1 MA / AA 1.0 1.5 2.0 2.0 0.5 CMC 0.8 0.4 0.4 0.2 PEI-0.4-Sulfate 20.0 10.0 20.0 30.0 Mg sulfate 0.2-0.4 0.9 CBD- Lance Feller Ze 0.001 0.5 0.01 0.5 Substrate - 0.05 5.0 10.0 Protease 0.03 0.03 0.02 0.02
Amylase 0.008 0.007-0.004 Lipase 0.004-0.002-Cellulase 0.0003--0.0001
Light activated bleach 30ppm 20ppm -10ppm
Perfume 0.3 0.3 0.1 0.2 Brightener 1/2 0.05 0.02 0.08 0.1 Others Up to 100%

Example 10 The following liquid detergent formulations were prepared according to the present invention (levels are given in parts / weight; enzymes are indicated as pure enzyme): I II III IV V
LAS 11.5 8.8-3.9-C25E2.5S-3.0 18.0-16.0 C45E2.25S 11.5 3.0-15.7-C23E9-2.7 1.8. 0 1.0 C23E7 3.2-----CFAA--5.2-3.1 TPKFA 1.6-2.0 0.5 2.0 2.0 Citric acid (50%) 6.5 1.2 2. 5 4.4 2.5 Ca formate 0.1 0.06 0.1 --- Na formate 0.5 0.06 0.1 0.05 0.05
SCS 4.0 1.0 3.0 1.2-borate 0.6-3.0 2.0 2.9 Na hydroxide 5.8 2.0 3.5 3.7 2.7 2.7 ethanol 1.75 1.0 3.6 4.2 2.9 1,2-propanediol 3.3 2.0 8.0 7.9 5.3 Monoethanolamine 3.0 1.5 1.3 2.5 2.5. 8 TEPAE 1.6-1.3 1.2 1.2 CBD-transferase 0.001 0.01 1.0 0.05 0.5 Substrate 0.1-0.01-10.0 Protease 0.03 0.01 0.03 0.02 0.02
Lipase--0.002--Amylase----0.002-Cellulase--0.0002 0.0005 0.0001 SRP1 0.2-0.1--DTPA--0.3--PVNO--0.3-0.2 Brightener 1 0.2 0.07 0.1 --- Silicone defoamer 0.04 0.02 0.1 0.1 0.1 Water and other up to 100%

Example 11 The following liquid detergent formulation was prepared according to the present invention (levels are given in parts / weight; enzymes are indicated as pure enzyme): I II III IV
LAS 10.0 13.0 9.0-C25AS 4.0 1.0 2.0 10.0 10.0 C25E3S 1.0--3.0 C25E7 6.0 8.0 13.0 2.5 TFAA---- 4.5 APA-1.4--TPKFA 2.0-13.0 7.0 Citric acid 2.0 3.0 1.0 1.5 Dodecenyl / tetra 12.0 10.0--Decenyl succinic acid Rapeseed fatty acid 4.0 2.0 1.0-ethanol 4.0 4.0 7.0 2.0 1,2-propanediol 4.0 4.0 2.0 7.0 monoethanolamine---5.0 Triethanolamine--8.0-TEPAE 0.5-0.5 0.2 DETPMP 1.0 1.0 0.5 1.0 CBD-transferase 0.01 0.01 0.01 0.001 Substrate 5.0 -5.0 0.1 protection Aase 0.02 0.02 0.01 0.008 Lipase-0.002-0.002 Amylase 0.004 0.004 0.01 0.008 Cellulase---0.002 SRP2 0.3-0.3 0.1 Boric acid 0.1 0.2 1.0 2.0 Ca chloride -0.02-0.01
Brightener 1-0.4--Foaming inhibitor 0.1 0.3-0.1 Opacifier 0.5 0.4-0.3 NaOH (up to right pH) 8.0 8.07 6.6 7.7 Water and other up to 100%

Example 12 The following liquid detergent composition was prepared according to the present invention (levels are given in parts / weight; enzymes are indicated as pure enzyme): I II III IV
LAS 25.0---C25AS-13.0 18.0 15.0 C25E3S-2.0 2.0 4.0 C25E7--4.0 4.0 TFAA-6.0 8.0 APA 3.0 1.0 2.0-TPKFA-15.0 11.0 11.0 Citric acid 1.0 1.0 1.0 1.0 Dodecenyl / tetra 15.0----decenyl succinic acid Rapeseed fatty acid 1. 0-3.5-ethanol 7.0 2.0 3.0 2.0 1,2-propanediol 6.0 8.0 10.0 13.0 Monoethanolamine--9.0 9.0 TEMPAE- -0.4 0.3 DETPMP 2.0 1.2 1.0-CBD-transferase 0.01 1.0 0.05 0.5 Substrate 5.0 0.01-10.0 Protease 0.080. 02 0.01 0. 02
Lipase--0.003 0.003 Amylase 0.004 0.01 0.01 0.01 0.01
Cellulase--0.004 0.003 SRP2--0.2 0.1 Boric acid 1.0 1.5 2.5 2.5 Bentonite clay 4.0 4.0--Brightener 1 0.1 0.2 0. 3-Foaming inhibitor 0.4---Opaque agent 0.8 0.7--NaOH (up to right pH) 8.0 7.5 8.0 8.2 Water and other up to 100%

Example 13 The following liquid detergent composition was prepared according to the present invention (levels are given in parts / weight; enzymes are indicated as pure enzyme): I II LAS 27.6 18.9 C45AS 13.8 5.9 C13E8 3.0 3.1 Oleic acid 3.4 2.5 Citric acid 5.4 5.4 Na hydroxide 0.4 3.6 Ca formate 0.2 0.1 Na-0 formate 5.5 Ethanol 7.0-Monoethanolamine 16.5 8.0 1,2-Propanediol 5.9 5.5 Xylenesulfonic acid-2.4 TEMPE 1.5 0.8 Protease 0.05 0.02 CBD -Transferase 0.05 0.5 substrate-10.0 PEG-0.7 brightener 2 0.4 0.1 fragrance 0.5 0.3 water and other up to 100%

[0228] Example 14 The following granular fabric detergent compositions which exhibit the capacity "softening by washing" was prepared in accordance with the present invention: I II C45AS - 10.0 LAS 7.6 - C68AS 1.3 - C45E7 4.0 -C25E3-5.0 Cocoalkyldimethylhydroxyethyl 1.4 1.0 Ammonium chloride citrate 5.0 3.0 Na-SKS-6-11.0 Zeolite A 15.0 15.0 MA / AA 4.04 0.0 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 CBD-transferase 0.001 0.01 Substrate -5.0 Protease 0.02 0.01 Lipase 0.02 0.01 Amylase 0.03 .005 Cellulase 0.001 - Silicate 3.0 5.0 Carbonate 10.0 10.0 suds suppressor 1.0 4.0 CMC 0.2 0.1 to other 100%

Example 15 The following rinse fluid added fabric softener composition was prepared in accordance with the present invention: DEQA (2) 20.0 CBD-transferase 0.5 substrate 0.1 cellulase 0.001 HCl 0.03 antifoam 0.01 Blue pigment 25ppm CaCl ₂ 0.20 Preservative 0.05 Fragrance 0.90 Water and others Up to 100%

Example 16 The following fabric softener and dryer-added fabric conditioner composition was prepared in accordance with the present invention: I II III IV V
DEQA 2.6 19.0---DEQA (2)----51.8 DTMAMS---26.0-SDASA--70.0 42.0 40.2 Stearic acid with IV = 0 0.3----Neodol 45-13--13.0--Hydrochloric acid 0.02 0.02 ---Ethanol--1.0--CBD-transferase 0.001 0.5 0.01 0.1 0.001 Substrate-0.1 5.0 5.0 1.0 Fragrance 1.0 1.0 0.75 1.0 1.5 Glycoperse S-20----15.4 Glycerol monostearate---26.0-Digeranyl succine --0.38--Silicone defoamer 0.01 0.01---Electrolyte-0.1---Clay---3.0-Preservative 0.05 0.05---Dye 10ppm 25ppm 0.01--Water and other 100% 100%---

Example 17 The following solid laundry detergent composition was prepared in accordance with the present invention (levels are given in parts / weight; enzymes are expressed as pure enzyme): I II III IV V VI VII VIII LAS --19.0 15.0 21.0 6.75 8.8-C28AS 30.0 13.5----15.75 11.2 22.5
Na laurate 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 15.0 10.0
Carbonate 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---DETPMP-0.7 0.6-0.6 0.7 0.7 0.7
CMC-1.0 1.0 1.0 1.0--1.0
Talc--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 0.5 0.4
SRP1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3
CBD-transferase 0.001 0.05 0.5 0.01 0.001 0.05 0.5 0.01
Substrate 0.1 5.0 8.0 5.0-0.1 2.0 5.0
Amylase--0.01---0.002-Protease-0.004-0.003 0.003--0.003
Lipase-0.002-0.002-----Cellulase-.0003--.0003 .0002--
PEO -0.2 -0.2 0.3--0.3
Fragrance 1.0 0.5 0.3 0.2 0.4--0.4
Mg sulfate--3.0 3.0 3.0----
Brightener 0.15 0.1 0.15-----0.1
Light activated bleach (ppm)-15.0 15.0 15.0 15.0--15.0

Example 18 The following pre- or post-treatment compositions were prepared according to the present invention: I II III IV V VI
DEQA (2)--20.0-20.0 20.0 CBD-transferase 0.8 0.05 0.05 0.005 0.05 0.15 Substrate-10.0 10.0 1.0 0.1 5.0 Cellulase--0.001-0.001 0.001
HCl--0.03-0.03 0.03 Antifoam--0.01-0.01 0.01 Blue dye 25ppm 25ppm 25ppm 25ppm 25ppm 25ppm
CaCl ₂ - - 0.20 - 0.12 0.20 Preservatives 0.05 0.05 0.05 0.05 0.05 0.05 0.90 0.90 0.90 0.90 0.90 0.90 water / other 100% perfume

──────────────────────────────────────────────────続 き Continuation of front page (81) Designated country EP (AT, BE, CH, CY, DE, DK, ES, FI, FR, GB, GR, IE, IT, LU, MC, NL, PT, SE ), OA (BF, BJ, CF, CG, CI, CM, GA, GN, GW, ML, MR, NE, SN, TD, TG), AP (GH, GM, KE, LS, MW, SD, SL, SZ, UG, ZW), EA (AM, AZ, BY, KG, KZ, MD, RU, TJ, TM), AE, AL, AM, AT, AU, AZ, BA, BB, BG, BR , BY, CA, CH, CN, CU, CZ, DE, DK, EE, ES, FI, GB, GD, GE, GH, GM, HR, HU, ID, IL, IN, IS , JP, KE, KG, KP, KR, KZ, LC, LK, LR, LS, LT, LU, LV, MD, MG, MK, MN, MW, MX, NO, NZ, PL, PT, RO, RU, SD, SE, SG, SI, SK, SL, TJ, TM, TR, TT, UA, UG, US, UZ, VN, YU, ZA, ZW (71) Applicant ONE PROCTER & GANBLE PLAZA, (72) Inventor Marie, Villarani, Barnabas, Ohio, USA, West, Chester, Sawgrass, Drive, 5777 (72) Inventor Michael, Stamford, Showwell, Ohio, Cincinnati, Finney , Trail, 810 (72) Inventor Stanton, Rain, Boyer Rica Ohio, Fairfield, Fall, River, Court, 12 (72) Inventor Andre, Christian, Convents Ohio, Cincinnati, Humphrey, Rhodes, USA, 9696 F-term (reference) 4B024 AA20 BA10 CA01 DA05 DA11 DA12 EA04 GA11 GA19 4B050 CC02 CC08 DD02 DD03 DD04 DD11 DD13 GG06 JJ03 KK05 KK14 LL04 4H003 AB14 AB19 AB27 AB31 AC05 AC08 AE06 BA10 BA12 BA20 DA01 EA12 EA15 EA16 EA20 EA27 EA28 EB08 EB12 EB21 EB19 EB19 EB19 FA22 FA47 4L031 BA39 DA20

Claims (31)

[Claims] 1. A modified enzyme comprising a catalytically active amino acid sequence of transferase linked to an amino acid sequence containing a cellulose binding domain. 2. The modified enzyme according to claim 1, wherein the catalytically active amino acid sequence is derived from a transferase selected from a glycosyltransferase (EC2.4) or a mutant glycosyltransferase. 3. Glycosyltransferase is transglucosidase (EC 2.4.1.24).
3. A cyclomaltodextrin glucanotransferase (EC 2.4.1.19), endoxyloglucan transferase, glucan sucrase, alternan sucrase (EC 2.4.1.140) and / or a mixture thereof. 3. The modifying enzyme according to item 1. 4. The modified enzyme according to claim 3, wherein the glucan sucrase is dextransucrase (EC 2.4.1.5). 5. The modified enzyme according to claim 1, wherein the catalytically active amino acid sequence is derived from an acyltransferase (EC2.3). 6. The acyltransferase is an aminoacyltransferase (EC2.3.2).
The modification enzyme according to claim 6, which is preferably transglutaminase (EC 2.3.2.13). 7. The method according to claim 7, wherein the catalytically active amino acid sequence is xyloglucan endotransglycosylase (X
The modified enzyme according to claim 1, wherein the modified enzyme is derived from a transferase selected from ET), endoxyloglucan transferase (EXGT) and / or a mixture thereof. 8. The modified enzyme according to claim 1, which has at least 50% of the maximum activity at 10 to 50 ° C. 9. The modified enzyme according to claim 1, which is alkaline. 10. The cellulose binding domain is a CBD CenC, C from Cellulomonas fimi.
enA, Cex, CBD CBHI, Clostridium ce from Trichoderma reesei
CBD from Cellulozome from C. llulovorans, CBD E from Thermonospora fusca
3. CBD dimer from Clostridium stecorarium XynA, Bacillus agara
dherens, CBD family 45 from Humicola insolens and / or
Or the modification enzyme according to any one of claims 1 to 9, which is selected from the group consisting of a mixture thereof. 11. The cellulosic binding domain comprises a CBD family 45 from Humicola insolens.
CenC and / or Clostridium cellu from Cellulomonas fimi
11. The modified enzyme according to claim 10, wherein the modified enzyme is selected from the group consisting of CBD Cellulozome from lovorans. 12. The modified enzyme according to claim 1, further comprising a connecting region between the catalytically active amino acid sequence of the transferase enzyme and the amino acid sequence containing the cellulose binding domain. 13. The modifying enzyme according to claim 12, wherein the connecting region is an amino acid connecting region. 14. The connecting region is a non-amino acid connecting region, preferably PEG (NPC) 2, (NH2).
The modified enzyme according to claim 12, which is a polymer selected from 2-PEG, t-BOC-NH-PEG-NH2, MAL-PEG-NHS and / or VS-PEG-NHS polymer. 15. A laundry detergent and / or fabric care composition comprising a laundry detergent and / or a fabric care component and the modified enzyme according to any one of claims 1 to 14. 16. The composition according to claim 1, wherein the modifying enzyme is present in an amount of 0.0001 to 10% by weight of the composition, preferably 0.0005 to 5%.
A laundry detergent and / or fabric care composition according to claim 15, wherein the laundry detergent composition is present at a level of pure modified enzyme of from 0.001 to 1%. 17. The laundry detergent and / or fabric care composition according to claim 15, further comprising an enzyme substrate. 18. The laundry according to claim 17, wherein the substrate is present at a level of from 0.01 to 30% by weight of the total composition, preferably from 0.1 to 20%, more preferably from 1 to 10%. Detergent and / or fabric care composition. 19. The laundry detergent and / or detergent according to claim 17, wherein the substrate is a glycoside dimer, oligomer and / or polymer, preferably selected from starch, xyloglucan, cyclodextrin, sucrose and / or maltose. Or a fabric care composition. 20. The laundry detergent and / or fabric care composition according to claim 17, wherein the substrate is an amino acid, di / tri / poly-peptide and / or protein. 21. The method according to claim 15, further comprising at least 5% by weight of an anionic surfactant, preferably an alkyl sulphate, an alkyl ethoxy sulphate and / or a linear alkylene sulphonate. Laundry detergent and / or fabric care compositions. 22. The laundry detergent and / or fabric care composition according to any one of claims 15 to 21, further comprising at least 2% of an alkyl ethoxylate nonionic surfactant. 23. A cationic surfactant, preferably a cationic surfactant having two long alkyl chain lengths, an anionic surfactant, preferably a protease, cellulase,
A detergent enzyme selected from lipase, amylase and / or mixtures thereof,
23. The method according to any one of claims 15 to 22, further comprising a laundry detergent and / or fabric care ingredient selected from a bleach, a dye transfer inhibitor, a dispersant, a smectite clay and / or a mixture thereof. Laundry detergent and / or fabric care composition. 24. Laundry detergent and / or fabric care composition according to any one of claims 15 to 23, in the form of an additive, pre-treatment, post-treatment, dipping and / or rinsing composition. . 25. Laundry detergent and / or fabric care composition according to any one of claims 15 to 24, which is in spray and / or foam form. 26. The laundry detergent and / or fabric care composition according to any one of claims 15 to 24, which is a granular composition containing up to 15% by weight of the total composition of an inorganic filler salt. 27. A liquid composition according to any one of claims 15 to 24, which is a liquid composition containing less than 40% by weight of the total composition, preferably less than 30%, more preferably less than 20%. Laundry detergent and / or fabric care composition. 28. A method comprising contacting a fabric with a laundry detergent and / or fabric care composition according to any one of claims 15 to 27. 29. The method of claim 28, wherein the fabric is treated with an enzyme substrate. 30. The method according to claim 28 or 29, wherein the fabric has been treated with a laundry and / or fabric care pre-treatment and / or post-treatment composition. 31. A fabric care including imparting tensile strength, anti-wrinkling property, anti-pilling property and anti-shrinkage property to the fabric, and renewing or recovering the fabric, to suppress static electricity, fabric flexibility, color appearance and / or 28. Use of a laundry detergent and / or fabric care composition as claimed in any one of claims 15 to 27 to provide fabric wear resistance and effect.