JP2002534597A - Detergent composition containing an enzyme system - Google Patents

Abstract

  (57) [Summary] The present invention relates to a detergent composition containing a mannanase enzyme, a pectate lyase enzyme, and a xyloglucanase enzyme, and provides excellent stain removal, darkness cleaning properties, and white maintenance properties.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

TECHNICAL FIELD OF THE INVENTION

The present invention relates to detergent compositions containing an enzyme system containing mannanase, xyloglucanase and pectate lyase.

[0002] The performance of a detergent product is determined by a number of factors, including the ability to remove soil and the ability to prevent the re-adhesion of degradants of soil or article soil in the cleaning fluid. Accordingly, detergent compositions have in recent years contained active ingredient combinations that meet certain requirements. In particular, current detergent formulations generally contain surfactants and detergent enzymes that provide cleaning and textile protection performance.

[0003]

[Problems to be solved by the invention]

Removal of spot stains from plants, wood, mold clay, base stains, mud stains, and fruits is the most difficult cleaning task of recent years, especially in the trend to lower wash temperatures. These stains usually contain a complex mixture of fibrous materials based on hydrocarbons and their derivatives: fibers and cell wall components. Plant soils are also associated with amylose, sugar and their derivatives. Food stains are always difficult to efficiently remove from soiled substrates. Highly colored or "dry" stains from fruit and / or vegetable juices are particularly challenging to remove. Particular examples of such stains are orange juice, tomato juice, banana, mango or broccoli stains. In addition, pectin polymers are important components of plant cell walls. Pectin is a heteropolysaccharide whose backbone consists of varying homogalacturonan (smooth regions) and rhamnogalacturonan (hairy regions). The smooth region is a linear polymer of 1,4-linked alpha-D-galacturonic acid. Galacturonic acid residues may be methylesterified to the extent that the carboxyl groups change, usually non-randomly such that the polygalacturonic acid blocks are completely methylesterified. Substrates with pectin-containing stains are generally knitted fabrics, tableware or hard surfaces.

In addition, the everyday “body” found in pillow cases, T-shirts, collars and socks
The complex nature of the soil presents the detergent with a constant and thorough cleaning challenge. Some of these stains are difficult to remove completely due to interaction with the pectin components in the primary cell wall of the cotton fibers that make up the cotton-containing knitted fabric, and residue often accumulates in such woven or knitted fabrics Darken the woven or knitted fabric. In addition, body fluid stains such as blood and menstrual fluid are difficult to remove efficiently from soiled articles, particularly over time. Daily body soils are also found on surfaces of sanitary and kitchenware such as bathtubs, toilet bowls and dishes.

[0005]

[Prior art]

The use of enzymes in detergents is well known in the art. For example, amylase enzymes have long been used in detergent compositions to remove starchy food residues or to remove starchy films from dishes or hard surfaces, and to improve the cleaning performance of starchy soils, as well as soils commonly encountered in laundry. It has been recognized as bringing. Proteinase enzymes have long been recognized in detergent compositions for removing proteinaceous food soils from dishes and hard surfaces, and for cleaning proteinaceous soils as well as those soils commonly encountered in laundry. . In addition, the use of cellulases is also well known in the art. This activity provides the fabric with cleaning, renewal, softening, and, typically, improved hand properties in the fabric construction. It is known to include lipolytic enzymes (eg, lipases) in detergent compositions to improve cleaning performance, for example, to facilitate removal of triglyceride-containing stains and spot stains from knitted fabrics.

[0006] Pectinolytic enzymes, when used in washing and cleaning operations, enhance the cleaning properties of detergent compositions that provide a stain / stain removal effect, particularly for the removal of a wide range of plant and fruit stains. It is known to be an item. Also, the removal of stains from plants, wood, mold clay stains and fruits,
This is the most challenging cleaning task of modern times, especially in the trend to lower cleaning temperatures. Food stains are often difficult to efficiently remove from soiled substrates. Highly colored or "dry" stains from fruit and / or vegetable juices are particularly challenging to remove. As a specific example of such a stain,
There are orange juice, tomato juice, banana, mango or broccoli stains.

A xyloglucan-specific endoglucanase with high xyloglucan-degrading activity may be used to degrade cell wall materials with high xyloglucan content,
For example, it may be used in the wine and fruit industries, and for pectin extraction and hemicellulose removal from textile fibers. Further, it has been recognized that certain such xyloglucan enzymes remove xyloglucan without changing cellulose. The use of such xyloglucan-specific endoglucanases in detergent compositions has recently been discovered, as described in WO 98/50513.

[0008] Another type of enzyme currently used in the detergent industry is mannanase. Mannanase enzymes are known for their hydrolytic properties on mannan-containing stains / soils, such as food and / or cosmetic stains / soils. Food and cosmetic stains / dirt
It is an important part of the stains / soils familiar to consumers and contains additives such as thickeners / stabilizers. In addition, hydrocolloid gums and emulsifiers are commonly used additives.

[0009]

[Means for Solving the Problems]

There is a continuing effort in the detergent industry to formulate detergent compositions that provide excellent cleaning performance. The challenge is mannanase,
Pectate lyase and / or xyloglucanase
This has been achieved by formulating a detergent composition containing a specific enzyme system containing ase).

Surprisingly, when used in combination with the following three specific enzymes: mannanase, pectate lyase and xyloglucanase, the synergistic effect of the mixed enzyme system provides excellent cleaning performance, ie, excellent stain removal. It was found that a darkening cleaning and white maintenance effect were provided. In particular, when the enzyme is used in combination, it can be used in laundry, dishwashing and hard surface cleaning applications, for example,
It has been found that even low wash temperatures and / or low detergent concentrations provide excellent removal performance for important stains.

It has been found that the performance of the detergent compositions of the present invention is enhanced by the addition of selected surfactants, builders, other enzymes and / or bleaching systems.

[0012] Mannanase is found in several species of Bacillus species. For example,
Talbot et al., Appl.Environ.Microbiol., Vol.No. 11, pp.
3505-3510 (1990) describes a β-mannanase with a molecular weight of 162 kDa in dimer form from Bacillus stearothermophilus and an optimum pH of 5.5-5.7.
Mendoza et al. (Mendoza et al.) World J. Micobio. Boitech. Vol. 10, no.5,
pp. 551-555 (1994) has a molecular weight of 38 kDa derived from Bacillus subtilisis and has an optimal p.
A β-mannanase with an H of 5.0 / 55 ° C. and a pl of 4.8 is described. J030
No. 4706 is derived from Bacillus sp. And has a molecular weight of 37 +/- determined by gel filtration.
Disclose a β-mannanase at 3 kDa, with a pH optimum of 8-10 and a pl of 5.3-5.4. J63056289 describes, for example, an alkaline, thermostable β-mannanase that hydrolyzes the β-1,4-D-mannopyranoside linkage of mannan to produce manno: oligo: saccharide. J63036774,
Bacillus producing β-mannanase and β-mannosidase at alkaline pH
It relates to the microorganism FERM P-8856. Purified mannanase from Bacillus amyloliquefacients and its method of preparation useful for bleaching pulp and paper are disclosed in WO 97/11164. WO 91/18974 describes hemicellulases, such as glucanases, xylanases or mannanases, which are active at extreme pH and temperature, and their production. WO94 / 25576 discloses Aspergillus aculeatus CBS1 which is desirable to decompose or modify the cell wall of a plant or a plant, but may be used for various purposes.
An enzyme exhibiting mannanase activity from 01.43 is described. WO 93/24622 discloses a mannanase isolated from Trichoderma reesie for bleaching lignocellulosic pulp.

Pectinolytic enzymes as detergent enzymes are described in EP-A-751990, WO 98 /
06805, WO98 / 06806, WO98 / 06807, WO98 / 068
No. 08 and WO 98/06809. WO95 / 35362 describes,
Disclosed is a cleaning composition for removing stains from vegetables, comprising a pectinase and / or hemicellulase and optionally a plant cell wall degrading enzyme having cellulase activity.

[0014] Xyloglucan-specific endoglucanases have been found in a variety of plants, for example, Fry et al., Biochem. J. (1992), Vol. 282, pp 821-828, Nishitan.
i and Tominaga, The Journal of Biol. Chemistry (1992) .Vol.267, No. 29,
pp.21058-21064, Hayashi et al., Plant Physiol. , (1984), Vol. 75, pp.605-
610, McDougall and Fry, J. Plant Physiol. , (1991), Vol. 137, pp. 332-336
And WO 93/17101. All of these enzymes have transferase activity (Fry
et al., 1992 and Nishitani et al., 1992), and are said to not be classified as true endoglucanases. In addition, xyloglucan-specific endoglucanases in microorganisms are described in WO 94/149.
No. 53. Among them, `` Glucanases with high xyloglucan degrading activity remove hemicellulose from the degradation of cell wall materials with high xyloglucan content, such as in the wine and fruit industries, from pectin extraction, and from textile fibers. It is particularly useful. " Particularly preferred for this last property is the use of these enzymes in the production of knitted textile fibres: "Hemicellulose, such as xyloglucan, can be used to produce cotton, flax and jute before being used as a textile. Must be removed from the natural plant fibers.
Endoglucanases II (ie, xyloglucan-specific enzymes) have the advantage of specifically removing xyloglucan without damaging the cellulose. "In addition, the endoglucanases and analogs thereof of the present invention may be used to treat cellulosic fibers or materials rich in cellulosic fibers. It is used to treat fibers, such as cotton fibers, and is used to smooth fibers.

However, the synergistic combination of mannanase, pectate lyase and xyloglucanase to obtain the excellent cleaning performance of detergent compositions, ie, good stain removal, darkening cleaning and white maintenance, is still never Was not recognized.

The present invention includes a laundry, dishwashing, hard surface cleaning composition containing mannanase, pectate lyase and xyloglucanase, having excellent cleaning performance, ie, excellent stain removal, darkening and white maintenance. The present invention relates to a detergent composition.

DETAILED DESCRIPTION OF THE INVENTION The detergent composition of the present invention contains as essential elements: mannanase, pectate lyase and xyloglucanase. Surprisingly, it has been found that such compositions provide excellent cleaning performance, i.e., good stain removal, dark cleaning and white maintenance performance.

Without wishing to be bound by theory, the combination of all three enzymes, mannanase, pectate lyase, and xyloglucanase, degrade complex hydrocarbon stains / stains compared to each enzyme alone. Is more efficient. Many plant and fruit stains contain intact plant cell wall material consisting of pectin and xyloglucan. In addition, hydrocolloid gums such as guar gum are stabilizers and rheology modifiers commonly used in processed foods. Thus, pectin, xyloglucan and mannan substrates are found in soils / stains of vegetable and / or fruit based foods. The polymeric, branched nature of these matrices allows the stain / dirt components to
It is believed to attract and retain on tableware and / or hard surfaces. Attacking these substrates with a specific mixture of the enzymes results in better overall removal of soils / stains, especially food-based soils and stains, than can be obtained with a single enzyme. In addition, cotton fibers are known to retain part of the primary cell wall. The pectin and xyloglucan present in this residual primary cell wall layer provide a preferred binding site for hydrocolloid gums in many processed foods and personal and beauty care products such as shampoos, body lotions, and makeup. When such materials come into contact with cotton fibers, they are difficult to remove with standard detergents. The enzyme mixture devised in the present invention is such that pectate lyase and xyloglucanase help to remove the primary cell wall component residues of cotton garments, and mannanase degrades the hydrocolloids present in the stain / stain itself. It is recommended to be effective in removing stains.

Mannanase Enzyme The first essential element of the detergent composition of the present invention is the mannanase enzyme.

[0020] Included in the present invention are the following three mannanase-degrading enzymes: EC 3.2.1.2.
5: β-mannosidase, EC 3.2.1.78: endo-1,4-β-mannosidase, among them “mannanase” and EC 3.2.1.100:1,
4-β-mannobiosidase (IUPAC classification-enzyme standard name, IS 1992
BN0-12-227165-3 Academic Press). More preferably, the detergent composition of the present invention comprises β-1,
Contains 4-mannosidase (EC 3.2. 1.78). The term "mannanase" or "galactomannanase" is formally defined in the art and is named mannan endo-1,4-beta mannosidase and has alternative names beta mannanase and endo-1,4-mannanase, Mannan, galactomannan, glucomannan, and 1,4-beta- in galactoglucomannan
1 represents a mannanase enzyme having an action of catalyzing a random hydrolysis reaction of a D-mannosidic bond.

In particular, mannanase (EC 3.2. 1.78) is an enzyme capable of degrading mannan and cleaving the polysaccharide chains containing mannose units, namely mannan, glucomannan, galactomannan and galactomannan. It constitutes a group of polysaccharides that can cleave glycosidic bonds in gluco-mannan. Mannan is β
A polysaccharide having a backbone composed of -1,4-linked mannose;
Glucomannan is a polysaccharide having a somewhat regularly varying β-1,4-linked mannose backbone and glucose; galactomannan and galactoglucomannan are α-1,6-linked galactose side chain branches. And glucomannan.

The degradation of galactomannan and galactoglucomannan is promoted by the total or partial removal of galactose side chain branches. The degradation of acetylated mannan, glucomannan, galactomannan, and galactoglucomannan is facilitated by total or partial deacetylation. Acetyl groups can be removed with alkali or mannan acetyl stearase. Oligomers released from mannanase, or a combination of mannanase and α-galactosidase and / or mannan acetylesterase, may be β-mannosidase and / or β-mannosidase.
It is further degraded by glucosidase, releasing free maltose.

[0023] Mannanase is found in several species of Bacillus species. For example,
Talbot et al. Appl.Environ.Microbiol., Vol. 56 No. 11, p.
p. 3505-3510 (1990) describes a beta-mannanase from Bacillus stearothermophilus in dimeric form, with a molecular weight of 162 kDa and an optimum pH of 5.5-5.7. Mendoza et al., World J. Microbiol. Boitech.
Vol. 10, No. 5, pp. 551-555 (1994) has a molecular weight of 38 k from Bacillus subtilis.
A beta-mannanase with an optimum pH of 5.0 at 55 ° C. and a pl of 4.8 at Da is described. JP-0304706 discloses a beta-mannanase derived from Bacillus sp. Having a molecular weight of 373 kDa, an optimum pH of 8-10 and a pl of 5.3-5.4, as measured by gel filtration. JP-63056289 describes, for example, an alkaline, thermostable beta-mannanase that hydrolyzes the beta-1,4-D-mannopyranozide linkage of mannan to produce manno-oligosaccharides.
JP-63037674 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase at alkaline pH. JP-0
No. 8051975 discloses alkaline beta-mannanase from alkalophilic Bacillus sp. AM-001. Purified mannanase from Bacillus amyloliquefacients and its preparation useful for bleaching pulp and paper is disclosed in WO 97/11164. WO 91/18974 describes hemicellulases such as glucanases, xylanases or mannanases which are active at extreme pH and temperature. WO 94/25576 describes an enzyme exhibiting mannanase activity from Aspergillus aculeatus CBS 101.43 that is useful for decomposing or modifying the cell wall of plants or grasses. WO 93/24622 discloses a mannanase isolated from Trichoderma reseei, which is useful for bleaching lignocellulosic pulp. Hemicellulases capable of degrading mannan-containing semicellulose are described in WO 91/18974, and pure mannanase from Bacillus amyloliquefacients is described in WO 97/1.
No. 1164.

Preferably, the mannanase enzyme is an alkaline mannanase as described below, more preferably a mannanase from a bacterial source. The term "alkaline mannanase enzyme" refers to an enzyme that has at least 10%, preferably at least 25%, more preferably at least 40% of its maximum activity in the pH range 7-12, preferably 7.5-10.5. It is meant to include enzymes having activity.

In particular, the laundry detergent composition of the present invention comprises Bacillus agaradhaerens NICMB 40482 bacteria;
Mannanase from Bacillus subtilis strain 168, gene yght; Bacillus sp.
AAI12 and / or an alkaline mannanase selected from a mannanase from Bacillus sp. AAI12. The most preferred mannanase for inclusion in the detergent composition of the present invention is co-pending Danish patent application PA199801.
No. 340 (PCT International Application / DK / 99/00314, June 10, 1999), a mannanase enzyme from Bacillus sp. 1633.

Alkaline mannanase from Bacillus agaradhaerens NICMB 40482 has been disclosed in co-pending US patent application Ser. No. 09 / 111,256 (international application PCT / DK / 99/0).
No. 0314, June 10, 1999). More specifically, the mannanase comprises: i) a polypeptide produced by Bacillus agaradhaerens NCIMB 40482; or ii) a position corresponding to SEQ ID NO: 2 at positions 32-343 of SEQ ID NO: 2 shown in U.S. Patent Application No. 09 / 111,256. A polypeptide comprising an amino acid sequence; or iii) an analog having at least 70% homology to the polypeptide defined in i) or ii), or substituting one or several amino acids of said peptide,
Those that have been deleted or added, and that are immunologically reactive with the polyclonal antibody obtained against the peptide in a purified form.

(A) a polypeptide encoding a mannanase activity, which is disclosed in US patent application Ser.
A polynucleotide molecule comprising a nucleotide sequence from nucleotide 97 to nucleotide 1029 of SEQ ID NO: 1 set forth in US Pat. No. 11,256; (b) a species similar to (a); (c) US patent application Ser. No. 09 / 111,256. The amino acid sequence from amino acid residue 32 to amino acid residue 343 of SEQ ID NO: 2 shown in SEQ ID NO: 2 and at least 70
(D) a molecule complementary to (a), (b) or (c); and (e) (a), (a) a polynucleotide molecule having a percent homology and encoding a polypeptide having mannanase activity. b) a modified nucleotide sequence of (c) or (d); and a corresponding isolated polypeptide selected from the group consisting of: which has a mannanase activity.

The plasmid pSJ1678 containing a polynucleotide molecule (DNA sequence) encoding mannanase was transformed into an Escherichia coli species,
Escherichia coli was established by the inventor as an international organization of deposit of microorganisms for patent proceedings in accordance with the Budapest Treaty (Deutsche Sammlung von Mikroorganismen und Zellkul
turen GmbH, Mascheroder Weg 1b, D-38124 Braunschweig, Germany,
Deposit No. DSM12180 on May 18, 1998).

[0029] A second more preferred enzyme is mannanase from Bacillus subtilis sp. 168, which is co-pending US patent application Ser. No. 09 / 095,163 (International Application PCT).
/ DK99 / 00314, June 10, 1999). More specifically, the mannanase comprises: i) SED ID No. 1 shown in US patent application Ser. No. 09 / 095,163. D of 5
The one encoded by the coding site of the NA sequence or an analog of said sequence; and / or ii) a polypeptide comprising the amino acid sequence of SED ID NO: 6 set forth in US patent application Ser. No. 09 / 095,163; or iii) analogs of the polypeptide defined in i) or ii) having at least 70% homology, or substituting one or several amino acids of said peptide,
Those that have been deleted or added, and that are immunologically reactive with the polyclonal antibody obtained against the peptide in a purified form.

(A) Encoding a polypeptide having mannanase activity, which is described in US patent application Ser.
A polynucleotide molecule comprising the nucleotide sequence of SEQ ID NO: 5 set forth in U.S. Pat. No. 95,163; (b) a homologous species of (a); (c) a SEQ ID ID set forth in U.S. Ser. A polynucleotide molecule having at least 70% homology to the amino acid sequence of NO: 6 and encoding a polypeptide having mannanase activity; (d) a molecule complementary to (a), (b) or (c); And (e) a modified nucleotide sequence of (a), (b), (c) or (d); and a corresponding isolated polypeptide selected from the group consisting of: which has mannanase activity.

A third more preferred mannanase is disclosed in co-pending Danish patent application no. PA
1998 01340 (International application PCT / DK99 / 00314, June 1999
10). More specifically: i) a polypeptide produced by Bacillus sp. 1633; ii) Danish application no. No. SEQ.
A polypeptide containing the amino acid sequence shown at positions 33-340 of ID-NO: 2; iii) an analog of the polypeptide defined in i) or ii) having at least 65% homology, Wherein one or several amino acids are substituted, deleted or added, or immunologically reactive with a polyclonal antibody obtained against the peptide in a purified form.

(A) encodes a polypeptide having mannanase activity and
. A polynucleotide molecule comprising the nucleotide sequence from nucleotide 317 to nucleotide 1243 of SEQ ID NO: 1 set forth in PA 1998 01340; (b) a homologous species of (a); SEQ ID
NO: a polynucleotide molecule that is at least 65% identical to the amino acid sequence from amino acid residue 33 to amino acid residue 340 of 2 and encodes a polypeptide having mannanase activity; (d) (a), (b) or ( c) a complementary polypeptide selected from the group consisting of: (e) a modified nucleotide sequence of (a), (b), (c) or (d).

The plasmid pBXM3 containing the polynucleotide molecule (DNA sequence) encoding the mannanase of the present invention was transformed into an Escherichia coli species.
The Escherichia coli was established by the inventor as an international organization of deposit of microorganisms for patent proceedings in accordance with the Budapest Treaty (Deutsche Sammlung von Mikroorganismen und Zel
lkulturen GmbH, Mascheroder Weg 1b, D-38124 Braunschweig, Germany, May 29, 1998) with the deposit number DSM12197.

A fourth more preferred mannanase is co-pending Danish patent application no. PA
1998 01341 (International Application PCT / DK99 / 00314, June 10, 1999). More specifically, the mannanase comprises: i) a polypeptide produced by Bacillus sp. AAI 12; ii) Danish application no. The sequence shown in PA 1998 01341
A polypeptide containing the amino acid sequence set forth at positions 25-362 of ID NO: 2; iii) an analog of the polypeptide defined in i) or ii) having at least 65% homology, wherein said polypeptide has One or several amino acids are substituted, deleted or added, or those which are immunologically reactive with a polyclonal antibody obtained against the peptide in a purified form.

(A) encodes a polypeptide having mannanase activity and
. A polynucleotide molecule comprising the nucleotide sequence from nucleotide 225 to nucleotide 1236 of SEQ ID NO: 1 set forth in PA 1998 01341; (b) homologous species of (a); (c) Danish application no. The sequence shown in PA 1998 01341
(D) (a), (b) a polynucleotide molecule having at least 65% homology with the amino acid sequence from amino acid residue 25 to amino acid residue 362 of ID NO: 2 and encoding a polypeptide having mannanase activity; Or (c); and a corresponding isolated polypeptide molecule selected from the group consisting of: (e) a modified nucleotide sequence of (a), (b), (c) or (d); .

The plasmid pBXM1 containing the polynucleotide molecule (DNA sequence) encoding the mannanase of the present invention was transformed into an Escherichia coli species,
The Escherichia coli was established by the inventor as an international organization of deposit of microorganisms for patent proceedings in accordance with the Budapest Treaty (Deutsche Sammlung von Mikroorganismen und Zel
lkulturen GmbH, Mascheroder Weg 1b, D-38124 Braunschweig, Germany, October 7, 1998) with the deposit number DSM12433. Mannanase is added to the detergent composition of the present invention at a concentration of pure enzyme of preferably 0.0001 to 2% by weight of the composition, more preferably 0.0005 to 0.1% by weight, most preferably 0.001 to 0.1%. It contains 0.02% by weight.

Pectate Lyase Enzyme The second essential element of the compositions of the present invention is the pectate lyase enzyme.

The pectate lyase is classified as EC 4.2.2.2 in the enzyme classification provided by the Enzyme Nomenclature, 1992. The enzyme cleaves the α-1,4, glucosidic bond of galacturonic acid in the pectin substrate and produces C4 and C5
And has substantially no other pectolytic activity, ie, 25
It is known to have other pectinolytic enzyme activities of less than 15% by weight, preferably less than 15% by weight, more preferably less than 5% by weight.

Pectate lyases are available from Erwinia, Pseudomonas, Klebsiella and Xanthomonas,
Strepomyces, Penicillium, Baceriodess, Thermomonospora, Fusarium, and As
It has been cloned from different bacterial genera, such as pergillus. Also, B
acillus subtilis (Nasser et al. (1993) FEBS 335: 319-326) and Bacillus sp.YA-
14 (Kim et al (1994) Biosci. Biotech. Biochem. 58: 947-949). Bacillus pumilus (Dave and Vaughn
(1971) J. Bacteriol. 108: 166-174), B. polymyxa (Nagel and Vaughn (1961)
Arch. Biochem. Biophys. 93: 344-352), B. stearothermophilus (Karbassi and
Vaughn (1980) Can.J. Microbiol. 26: 377-384), Bacillus sp. (Hasegawa and
Nagel (1966) J. Food Sci. 31: 838-845) and Bacillus sp.RK9 (Kelly and Fogar
ty (1978) Can. J. Microbiol. 24: 1164-1172, pH range 8
Purification of the pectate lyase with maximum activity at -10 has been reported. WO9
No. 8/45393 discloses a detergent composition containing protopectinase, which has a remarkable detergency against mud stains.

Further, pectate lyases suitable for use in the present invention are described in WO 98/45.
No. 393, when polygalacturonic acid is used as a substrate, protopectinase and EP having an optimum reaction pH of 7.0 or above.
Pectate lyase having the amino acid sequence of SEQ ID NO: 870843, SEQ ID NO: 1, or having one or more of its amino acid sequences deleted, added or substituted.

Preference is given to PCT / DK98 / 00515 (1998)
A pectate lyase enzyme as described in International Application No. WO 99/27084, Nov. 24, 2011): pectate lyase in which the first amino acid sequence consists of seven amino acid residues having the following sequence: Asn Leu Asn Ser Arg Val Pro (NLNSRVP);

The pectate lyase is: i) by Bacillus agaradhaerens, NCIMB 40482 or DSM 8721, or by Baci
a polypeptide produced by a Bacillus species having at least 99% 16S rDNA sequence homology to llus agaradhaerens DSM 8721, or ii) SEQ ID NO: 27 of PCT / DK98 / 00515
A polypeptide comprising the amino acid sequence at position -359, or iii) an analog of the polypeptide defined in i) or ii), having at least 45% homology with said polypeptide; or iv) position 240. Optionally, also by substitution, deletion or addition of one or several amino acids of the peptide, provided that the arginine at position 245 is maintained and the derived polypeptide has at least 42% homology. What was induced,
v) It is immunologically reactive with the polyclonal antibody obtained against the peptide in purified form.

The pectate lyase is: i) according to Bacillus licheniformis, ATCC 14580 or Bacillus licheniformis
Bacillus with at least 99% 16S rDNA sequence homology to ATCC 14580
A polypeptide produced by the species, or ii) 28-34 of SEQ ID NO: 4 of PCT / DK98 / 00515.
A polypeptide containing the amino acid sequence shown at position 1, or iii) an analog of the polypeptide defined in i) or ii), having at least 45% homology with said polypeptide; or iv) Substitution, deletion or deletion of one or several amino acids of the peptide, provided that the arginine at position 233, optionally also at position 238, is maintained and the derived polypeptide has at least 42% homology Those induced by the addition,
v) those that are immunologically reactive with the polyclonal antibody obtained against the peptide in purified form.

The pectate lyase is: i) 16S rD of SEQ ID NO: 14 of PCT / DK98 / 00515
Depending on the Bacillus species having the NA sequence or the S of PCT / DK98 / 00515
A polypeptide produced by a Bacillus species having a 16S rDNA sequence homology greater than 97.3% to the sequence of EQ ID NO: 14; or ii) 181-50 of SEQ ID NO: 6 of PCT / DK98 / 00515
A polypeptide containing the amino acid sequence shown at position 9, or iii) an analog of the polypeptide defined in i), having at least 50% homology with said polypeptide, or iv) position 390; Optionally, also at position 395, provided that arginine is maintained and the derived polypeptides have at least 44% homology,
Those derived by substitution, deletion or addition of one or several amino acids of the peptide; v) those which are immunologically reactive with the polyclonal antibody obtained against the peptide in purified form; is there.

The pectate lyase is: i) a polypeptide produced by Bacillus halodurans species, or ii) PCT / DK98 / 00115, SEQ ID NO: 8, 42-34.
A polypeptide containing the amino acid sequence shown at position 8, or iii) an analog of the polypeptide defined in i) or ii), having at least 45% homology with said polypeptide; or iv) At position 240, optionally, and also at position 245, provided that arginine is maintained and the derived polypeptides have at least 40% homology.
Those derived by substitution, deletion or addition of one or several amino acids of the peptide; v) those which are immunologically reactive with the polyclonal antibody obtained against the peptide in purified form; is there.

The pectate lyase is: i) 16S rD of SEQ ID NO: 13 of PCT / DK98 / 00515
Depending on the Bacillus species having the NA sequence or the S of PCT / DK98 / 00515
A polypeptide produced by a Bacillus species having 16S rDNA sequence homology greater than 98.1% with the sequence of EQ ID NO: 13; or ii) 25-3 of SEQ ID NO: 10 of PCT / DK98 / 005155.
A polypeptide containing the amino acid sequence shown at position 35, or iii) an analog of the polypeptide defined in i), having at least 45% homology with said polypeptide, or iv) position 227; Arginine is optionally maintained at position 232,
Derived by substitution, deletion or addition of one or several amino acids of the peptide, provided that the derived polypeptide has at least 41% homology, v) obtained against the peptide in purified form Is immunologically reactive with the polyclonal antibody obtained.

Similarly, international co-pending application PCT / DK98 / 00514 (November 1998)
Pectate lyase enzymes as described in International Application No. WO 99/27083, published on May 24, which are: i) polypeptides produced by Bacillus licheniformis, ATCC 14580, or ii) SEQ ID No. PCT / DK98 / 00514 28-22 of ID NO: 4
A polypeptide containing the amino acid sequence shown at one position, or iii) an analog of the polypeptide defined in i) or ii), having at least 60% homology with said polypeptide, or iv) Lysines at positions 133 and 155, arginine at position 158 are maintained, and the derived polypeptide is identified in SEQ ID NO: PCT / DK98 / 00514.
: 4. Derived by substitution, deletion or addition of one or several amino acids of the peptide, provided that they have at least 66% homology with positions 60-158 of 4); One that is immunologically reactive with the polyclonal antibody obtained against the peptide;

For the purposes of the present invention, more preferred pectate lyases have optimal activity when the pH is above 7.0, and are preferably Streptomyces fradiae, Streptomyces nitrosporeus, E
rwinia carotovora, Bacillus spheroides, Thermomonospora fusca, Pseudomon
as solanacearum, Bacteroides thetaiotaomicron, Fusarium solani, Xanthomo
nas campestris, Bcillus agaradhaerens and / or Bacillus licheniformis.

For the purposes of the present invention, the most preferred pectate lyase is Bcillus agaradhaeren
s, pectate lyase from NCIMB 40482 or DSM8721.

The pectate lyase is added to the detergent composition of the present invention in a concentration of pure enzyme, preferably 0.0001 to 2% by weight of the composition, more preferably 0.0005 to 0.1% by weight.
, Most preferably 0.001 to 0.02% by weight.

Xyloglucanase Enzyme A third essential element of the present invention is a co-pending international patent application PCT / US98 / 09.
No. 126 (International application by Procter and Gamble on May 5, 1998, WO 98
Xyloglucanase enzyme as described in US Pat.

[0052] was suitable for the present invention, the catalyst metabolic rate K _cat at maximum condition of the enzyme, for xyloglucan than about carboxymethylcellulose, an enzyme that shows a specific endoglucanase activity at least five times higher xyloglucan is there.

As used herein, the term “endoglucanase activity” refers to the ability of an enzyme to hydrolyze the 1,4-β-D-glucoside bond present in any xyloglucan material to cellulose. Endoglucanase activity is determined according to methods known in the art, examples of which are described in WO 94/14953 and below. One unit of endoglucanase activity (eg, CMCU, AVIU, X
GU or BGU) is defined as 1 μmol reducing sugar production / minute from a glucan substrate, and the glucan substrate is, for example, CMC (CMCU), acid swollen Avicell (AV
IU), xyloglucan (XGU), or grain β-glucan (BGU).
The reducing sugar is determined as described in WO 94/14953 and below. The specific activity of the endoglucanase on the substrate is defined as units / mg protein.

Suitable are enzymes exhibiting high activity XGU endoglucanase activity (hereinafter “xyloglucan-specific”), said enzymes comprising: i) consisting of or containing at least one of the following subsequences: Which is encoded by a DNA sequence

Embedded image

Embedded image Or a sequence having homology thereto and encoding a polypeptide specific to xyloglucan having endoglucanase activity.

Ii) immunologically reactive with antibodies raised against highly purified endoglucanases encoded by the DNA sequences defined in i), and Aspergillus
aculeatus, derived from CBS 101.43, specific for xyloglucan.

More specifically, as used herein, the term “xyloglucan-specific” means that the endoglucanase enzyme exhibits the highest endoglucanase activity on the xyloglucan substrate, and that carboxymethylcellulose, cellulose, or other glucans. It preferably has less than 75% activity, more preferably less than 50% activity, and most preferably less than about 20% activity on such other cellulose-containing substrates.

Preferably, the specificity of the endoglucanase for xyloglucan is further determined by the optimal conditions obtained by culturing the enzyme with xyloglucan and the release of reducing sugars on each of the other substrates tested. Relative activity. For example, specificity is determined by xyloglucan versus β-glucan activity (XGU / BG
U), xyloglucan versus carboxymethylcellulose activity (XGU / CMCU)
Or xyloglucan versus acid swollen Avicell activity (XGU / AVIU), which is preferably greater than about 50, such as 75, 90 or 100.

As used herein, the term “origin” refers to not only the endoglucanase produced by CBS101.43, but also the DNA sequence isolated from CBS101.43, which is transformed with the DNA sequence. Refers to endoglucanase produced in a host. As used herein, the term "homologue" refers to a homolog under certain conditions (pre-soaked in 5 × SSC, 5 × SSC solution, 5 × Denhardt solution, 50 μg of denatured sonicated calf thymus). Prehybridized at 50 ° C for 1 hour, then hybridized with 50 μCi 32-P-dCTP for 18 hours at 40 ° C in the same solution to which the labeled probe was added, at 40 ° C for 30 minutes, 2xSSC, 0
. (3 washes in 2% SDS), showing the polypeptide encoded by the DNA hybridizing to the same probe as the DNA encoding the endoglucanase enzyme specific for xyloglucan. More specifically, the term refers to at least 70% homologous DN encoding an endoglucanase specific for xyloglucan as shown above.
It is intended to refer to the A sequence and refers to a sequence that is at least 75%, at least 85%, at least 90%, and even at least 95% homologous to any of the above sequences. The term may refer to nucleotide substitutions that match the codon usage of the host organism into which the DNA structure containing any DNA sequence is introduced, without giving rise to other amino acids in the polypeptide encoded by the sequence, or may vary. Amino acid sequence,
It is intended to include modifications of any of the above DNA sequences where possible, such as nucleotide substitutions resulting in different amino acid sequences, different protein structures that may result in endoglucanase variants of different properties than the native enzyme. Other examples of possible mutations include inserting one or more nucleotides into the sequence, adding one or more nucleotides at the end of the sequence or in the sequence, replacing one or more nucleotides at the end of the sequence or in the sequence. May be deleted.

The xyloglucan-specific endoglucanases useful in the present invention preferably have an XGU / BGU, XGU / CMU and / or XGU / AVIU ratio (as defined above) of 75, 90 or 100. It is larger than 50.

In addition, the xyloglucan-specific endoglucanase preferably has substantially no activity on β-glucan and / or has 100% activity on xyloglucan, At most 25%, such as about 5% or about 5%. In addition, the xyloglucan-specific endoglucanases of the present invention preferably lack substantially the transferase activity found in most plant-derived xyloglucan-specific endoglucanases.

The xyloglucan-specific endoglucanase is obtained from the A. aculeatus strain described in WO / 94/14953. Xyloglucan-specific microbial endoglucanases are also described in WO 94/14953. Although xyloglucan-specific endoglucanases from plants have been described, these enzymes have transferase activity, and therefore, where degradation of large amounts of xyloglucan is desired, xyloglucan-specific endoglucanases derived from microorganisms. Must be considered inferior to. An additional advantage of microbial enzymes is that they are typically produced in larger amounts in microbial hosts than enzymes of other origins.

The xyloglucanase of the present invention can be obtained by cloning a suitable vector from a DNA library of Aspergillus spp., Transforming a suitable yeast host with the vector, and culturing the host cell under suitable conditions Screening the positive clones by expressing the enzyme of interest encoded in the clones of the DNA library and measuring the endoglucanase activity of the enzymes produced in the clones. Can be isolated.

A detailed description of this screening method is given in WO 94/14953. The DNA sequence encoding the enzyme is, for example, Centraalbureau voor Schimmel
Aspergillus aculeatus cd such as CBS 101.43 publicly available from culture
The NA library is isolated by screening, expressing enzymes, expressing β-1,3- and / or between two glucose molecules in a glucose-containing polymer (eg, cellulose, cereal β-glucan or xyloglucan). Or β-1,4-
It can be isolated by selecting a clone capable of hydrolyzing the bond. Suitable DNA sequences may be isolated from the clones by standard methods, for example as described in Example 1 of WO 94/14953. DNA sequences encoding homologous enzymes may be found in other microorganisms, especially Aspergillus species, especially A. aculeatus or A. niger, Tric.
It is derived by similarly screening a cDNA library of a fungal species, such as a hoderma species, in particular, T. harianun, T. reesie, Fusarium species, especially F. oxysporum or Humicola species.

In addition, the DNA encoding the endoglucanase of the present invention can be easily prepared from DNA from any of the aforementioned organisms by a well-known procedure using a 20-mer probe prepared based on the DNA sequence disclosed herein. It is isolated by using such an oligonucleotide probe. For example, suitable oligonucleotide probes include, for example, any of the partial nucleotide sequences a) listed in WO 94/14953.
-P). The DNA sequence is then inserted into a recombinant expression vector. This is any vector that is conveniently subjected to the recombinant DNA procedure, and the choice of vector often depends on the host into which the vector is to be introduced. Thus, the vector is an autonomously replicating vector, ie, exists as an extrachromosomal component, the replication of which is independent of chromosomal replication, eg, a plasmid. Further, when introduced into a host cell, it may be integrated with the host genome and replicated together with the integrated chromosome.

DNA encoding xyloglucan-specific endoglucanase in a vector
The sequence should be operably linked to appropriate promoter and terminator sequences. The promoter can be any DN that exhibits transcriptional activity in the chosen host.
A is derived from a gene encoding a protein homologous or heterologous to the host cell. The procedures used to ligate each of the DNA sequence encoding the endoglucanase, the promoter, and the terminator and insert them into a suitable vector are well known to those skilled in the art (see, for example, Sambrook et al., Mol ecular Cloning. A Laboratory Manual, Cold Sring Harbor, NY 1989).

The host cell transformed with a DNA sequence encoding an enzyme useful in the composition of the invention is preferably a eukaryotic cell, especially a fungal cell such as a yeast or filamentous fungal cell. In particular, the cells belong to the species Aspergillus, most preferably Aspergillus ory
zae or Aspergillus niger. Fungal cells may be transformed by protoplast formation, as known in the art, followed by protoplast transformation followed by cell wall regeneration. The use of Aspergillus as a host microorganism is described in EP 238,0.
No. 23 (Novo Nordisk A / S). The host cell may also be a yeast, for example, a Saccharomyces strain, especially a Saccharomyces cerevisiae.

The medium used to culture the transformed host cells can be any conventional medium suitable for growing the subject host. The expressed xyloglucan-specific endoglucanase is simply secreted into the culture medium, the cells are separated from the medium by centrifugation or filtration, and the protein-like components of the medium are precipitated with a salt such as ammonium sulfate. Performed by chromatography methods such as exchange chromatography and affinity chromatography.

[0068] Purified endoglucanase may be used to immunize animals for the production of antibodies. Antisera to xyloglucan-specific endoglucanases are described in N. Axelsen et al .
: A Manual of Quantitiave Immunoelectrophoresis , Blackwell Scientific Pu
Rabbits (and other rodents) according to the method of blications, 1973, Chapter 23, or A. Johnstone and R. Thorpe, Immunochem istry in Practice , Blackwell Scientific Publications, 1982 (more specifically, pages 27-31). ) Can be obtained by immunization. Purified immunoglobulins can be obtained from antisera, for example, after salt precipitation ((NH ₄ ) ₂ SO ₄ ), followed by dialysis and, for example, DEAE-Seph.
It can be obtained by ion exchange chromatography using adex. Immunochemical characterization of the protein, Outcherlony gel double diffusion analysis (O. Ouchterlony in:. Ha ndbook of Experimental Immunology (DM Weir, Ed), Blackwell Scientific
Publications, 1967, pp. 655-706), cross immunoelectrophoresis (N. Axelse
n et al., supra , Chapters 3 and 4), or rocket immunoelectrophoresis (N. Axelse
n et al ., Chapter 2).

The xyloglucan-specific endoglucanases useful in the compositions of the present invention are produced substantially free of other plant cell wall degrading enzymes. Enzyme preparations useful in the compositions of the present invention are prepared according to methods known in the art and can be in liquid or dry form. For example, the enzyme preparation is granules or microgranules. The enzyme contained in the preparation may be stabilized according to methods known in the art.

Test method: Standard culture: For characterization of the enzymes, cultures are carried out in Eppendorf tubes containing 1 ml of substrate (AZCL-xyloglucan substrate or pure polysaccharide from MegaZyme, Australia). Mix 0.5 mL of the 0.4% AZCL-substrate suspension with 0.5 mL of the optimal pH, 0.1 M citrate / phosphate buffer and add 10 μl of the appropriately diluted enzyme solution. Incubation was performed at 30 ° C. for 15 minutes in an Eppendorf thermomixer (unless otherwise specified) and heat inactivation at 95 ° C. for 20 minutes. Enzyme culture is performed in triplicate. Blanks were immediately inactivated by addition of enzyme. After centrifugation, the absorbance of the supernatant was measured in a 620 nm microtiter plate and blanks were subtracted.

Pure polysaccharides with different enzymatic activities: xyloglucan and beta-glucan from MegaZyme (AZCL-xyloglucan and AZCL-HE cellulose),
CMC (Blanose from Aqualon) and Avicell (microcrystalline cellulose from Merck) were measured. Before use, Avicell was swollen in 85% orthophosphoric acid for 1 hour at room temperature and washed with acetone and water. Producing 0.5% solutions / suspensions of different substrates in 0.1 M acetate buffer (unless otherwise specified) at the optimal pH,
After adding 10 μl of the enzyme solution to 1 ml of the substrate and culturing at 30 ° C. for 15 minutes,
The thermal inactivation as described above is performed. In a microtiter plate, reduce with a PHBAH reagent containing 0.15 g of parahydroxybenzoic hydrazide (Sigma H-9882), 0.50 g of potassium-sodium tartrate (Merck 8087) and up to 10.0 ml of 2% NaOH solution. The sugar is determined by the reaction. Subtract blank results. Glucose is used as a standard.

MegaZyme (enzyme described below: AZCL-EG II on xyloglucan, pure β-
Optimal pH of substrate from EG III on glucan and EG IV on AZCL-β-glucan)
Is measured. 0.5 ml of 0.4% substrate is mixed with 0.5 m of 0.1 M at different pH
Mix with citrate / phosphate buffer and add 10 μl of appropriate diluted enzyme solution. Culture is performed as described above. The enzymes useful in the present invention have an optimum pH even at such a pH that it is desired to match the pH of the composition or cleaning method in which the enzyme is used, preferably the enzymes useful in the present invention have a pH of about It is active at a pH in the range of 6-11, preferably 7-11, more preferably in the range of about 8 to about 10.5. The specificity of different enzymes on different AZCL-substrates is tested as described above at the optimal pH in 0.1 M acetate buffer. The pH stability is determined by allowing the enzyme to stand for 1 hour in a 0.1 M citrate / trisodium phosphate buffer at a different pH before the enzyme is used for culturing AZCL-β-glucan at the optimum pH. The optimal temperature to be measured is determined by culturing the enzyme with the AZCL-β-glucan substrate at the optimal pH for 15 minutes at different temperatures. Temperature stability at 30 ° C with related substrate
Before culturing, the enzyme is measured by diluting the enzyme with water and allowing it to stand at various temperatures for 1 hour.

The K _m and the specific activity were measured at a substrate concentration (S) of 0.025 to 1.5% (hereinafter referred to as xyloglucan for EG II and β-glucan for EG IV), and the reaction rate was determined. (V)
Is measured, S / v is plotted as a function of S, a linear regression analysis is performed, and the slope (= 1)
/ V _max ) and intercept (K _m / V _max ) are determined and K _m and specific activity (= V _max / E) are calculated (where E is the amount of enzyme added). Prepare a 1% solution / suspension of the pure polysaccharide described above for gel filtration chromatography. The appropriate amount of enzyme is added and the culture is run for 0, 1, 2, 4 and 24 hours and heat inactivated. TSK-column with three 25 μl samples (
PW G4000, PW G3000, PW G2500).
. Elute with 4 M acetate buffer at 0.8 ml / min. Elution saccharide is Shimadzu R
The data is measured with an I detector, and the data is compiled by Dionex software. Dextran (from serum) is used as a molecular weight standard.

Substrate Specificity The relative activity, determined as the release of reducing sugars of different enzymes from different polysaccharides, compared to the optimal substrate (100%) is given in WO 94/14953 and reproduced in the table below. .

[0075]

[Table 1]

From these results, the specificities of the different endoglucanases are expressed as follows:

[Table 2]

The results of the substrate specificity determined for the AZCL-substrate are also described in WO 94/14
No. 953, reproduced in the following table:

[Table 3]

From the specificity results, EG II appears to be specific for xyloglucan as defined for use in the compositions of the present invention, as compared to EG III and EG IV, but the other two ene dog glucanases Is not so. EG III is active on all types of substrates, but not the most active on xyloglucan, EG IV is unable to degrade xyloglucan, β
-Very specific for glucan. (There is a slight difference in the results obtained with reducing sugars and AZCL-substrates, because the explanation is that AZCL-substrates are more sensitive than others. In this case, AZCL-HE-cellulose is AZCL- More sensitive than β-glucan.)

The K _m and specific activity of EG II and EG III are given in WO 94/14953. The 1 / V _max and K _m / V _max standard deviations obtained from the linear regression analysis are used to calculate the enzyme intervals as evident from the table below.

[Table 4]

Optimal temperature and temperature / pH stability- EG II and EG III have similar optimal temperatures (optimal activity between 30-60 ° C) and temperature stability (stable up to 60 ° C for 1 hour)
EG III is more stable at alkaline pH than EG II.

Gel filtration chromatograms confirming substrate specificity show that EG II replaces xyloglucan with a known repeating subunit of xyloglucan (Fry, 1989) at about 7-
It shows that it completely decomposes into an oligomer of 9 residues. EG III degrades very small amounts of xyloglucan, and EG IV does not degrade xyloglucan at all. EG III is β
Glucan is decomposed in large quantities into DP3-4 and high molecular oligomers. This is consistent with β-glucan being composed of a row of 3-4β-1,4-linked glucose units interrupted by a single β-1,3-linkage.

The xyloglucanase is present at a pure enzyme concentration of preferably 0.0001 to 2%, more preferably 0.0005 to 0.1%, most preferably 0.001 to 0.02% by weight of the composition. , Contained in the detergent composition of the present invention.

Preferably, the detergent composition of the present invention comprises the three enzymes at a pure enzyme weight ratio of mannanase: pectate lyase: xyloglucanase of 10: 1: 1 to 1: 10: 1.
-1: 1: 10 in a specific ratio. More preferably, the ratio is 5: 1: 1 to 1
: 5: 1 to 1: 1: 5, most preferably a ratio of 1: 1: 1.

[0084] Mannanase, pectate lyase and / or mannanase incorporated in the detergent composition of the present invention.
Alternatively, xyloglucanases also contain, in addition to the enzyme core containing the catalytic domain, a cellulose binding domain (CBD), wherein the cellulose binding domain of the enzyme and the enzyme core (the catalytically active domain) are operably linked. are doing. The cellulose binding domain (CBD) can be present as an integral part of the encoding enzyme, or CBD from other species can be introduced into the enzyme to create a hybrid enzyme. In this sense, the term “cellulose-binding domain” refers to Peter To
mme et al. "Cellulose-Binding Domains: Classification and Properties" in
"Enzymatic Degradatiion of Insoluble Carbohydrates", John N. Saddler an
d Understood as defined by Michael H. Penner (Eds.), ACS Symposium Series, No. 618, 1996. This definition classifies more than 120 cellulose binding domains into 10 families (IX), and CBD is found in various enzymes such as cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. Indicates that CBD is found as a non-hydrolyzable polysaccharide-binding protein in, for example, red alga Porphyra purpurea (see Tomme et al., Op.cit.). However, most CBD is from cellulases and xylanases, and CBD is found at the N and C termini or inside the protein. Enzyme hybrids are known in the art (see, for example, WO 90/00609 and WO 95/16782) and link the host to a DNA sequence encoding a mannanase and / or pectate lyase and / or a xyloglucanase enzyme. D, including or without a ligated version of at least one DNA fragment encoding a cellulose binding domain
It can be prepared by transforming with the NA structure and growing a host that expresses the fusion gene. The enzyme complex is represented by the following formula:

Embedded image Wherein CBD is at least the N-terminal or C-terminal region of the amino acid sequence corresponding to the cellulose binding domain; MR is preferably from about 2 to about 100, more preferably 2 to 40 carbon atoms. In the intermediate region (linking group), a bond or a short linking group; preferably about 2 to about 100 amino acids, more preferably 2 to 4 amino acids
With 0 amino acids; X is the N-terminal or C-terminal region of the mannanase, pectate lyase and / or xyloglucanase of the present invention.

The enzymes described above are of suitable origin, such as of plant, animal, bacterial, fungal and yeast origin. The origin may be mesophilic or extreme (cryophilic, low-temperature, thermophilic, pressure-philic, alkaline-philic, acidophilic, salt-philic, etc.). Purified or unpurified forms of these enzymes are used. At present, it is common practice to modify natural-type enzymes by protein / gene technology to optimize their efficiency performance in the detergent compositions of the present invention. For example, variants are designed to increase the compatibility of the enzyme with commonly used components. The variants are also designed such that the optimal pH, bleaching or chelation stability, catalytic activity, etc. of the variant are suitable for a particular cleaning application.

In particular, attention should be paid to oxidation-sensitive amino acids for bleach stability and surface charge for surfactant compatibility. The isoelectric point of such enzymes can be modified by substitution of some charged amino acids, for example, increasing the isoelectric point can help improve compatibility with anionic surfactants . Enzyme stability can be further enhanced by, for example, creating additional salt bridges to increase chelator stability and reinforcing calcium binding sites.

Detergent Composition The detergent composition of the present invention must contain at least one additional detergent component. The exact nature of these additional components and their concentration will depend on the physical properties of the composition and the cleaning operation in which the composition is used. It has further been found that the performance of the detergent compositions of the present invention is enhanced by the addition of selected surfactants, builders, other enzymes and / or bleaching systems.

The detergent composition of the present invention may be in liquid, paste, gel, rod, tablet, spray, foam, powder or granular form. Particulate compositions can be in "compact" form, and liquid compositions can be in "concentrated" form. A tablet composition may be in the form of a single layer or multiple layers. Surprisingly, it has been found that pectate lyase, mannanase and xyloglucanase enzymes are optimized and maximized with time-controlled release technology. In particular, the time control technique refers to tablets in which the enzyme is isolated from other depressing / inactivating detergent components in different layers of the product and has different solubility in the wash liquor. Surprisingly, it has been found that the incorporation of the enzyme into the tablet achieves the optimum efficiency performance of the enzyme and results in excellent soil and stain cleaning effects.
Such time-controlled release technology has been found to tolerate the use of a wide range of enzymes that exhibit a high degree of instability in a standard detergent matrix. In addition, the pectate lyase and the buffer material can preferably be included in the rapidly dissolving part of the tablet. Without intending to be bound by theory, the enzymes of the present invention are released faster than other inhibitory / inert detergent components, and under buffer conditions optimal enzyme activity is obtained from the beginning of the wash, It is believed to allow the formulation of a maximum range of effective pectate lyase, mannanase and xyloglucanase detergent formulations of pectate lyase, mannanase and xyloglucanase.

Suitable tablets are detergent tablets that are not only robust enough to withstand handling and transport, but also at least partially dissolve rapidly in wash water, resulting in a rapid provision of the pectate lyase enzyme. It is preferred that at least one layer of the tablet dissolves in the wash water during the first 10 minutes, preferably 5 minutes, more preferably 4 minutes, of an automatic dishwasher or washing machine washing cycle. Preferably, the washing machine is either an automatic dishwasher or a washing machine. The dissolution time of the multi-layer or mono-layer tablet or the detergent active is determined using a dishwasher commercially available from Bosch, with a normal 65 ° C. washing program, at a water hardness of 18 ° H., at least 6 times or with reproducibility. Make sufficient measurements and measure according to DIN 44990.

A first aspect of the present invention relates to a laundry detergent and / or knit care composition comprising mannanase, pectate lyase and xyloglucanase (Examples 1-1).
5). A second aspect of the present invention relates to dishwashing or household detergent compositions (Examples 16 to 25).

The compositions of the present invention can be formulated, for example, as hand dishwashing compositions, hand and machine wash laundry detergent compositions, including, for example, laundry additive compositions, and stained knit fabrics. And compositions for use in general household hard surface cleaning operations. When formulated as a composition for use in a hand-washing dishwashing method, the compositions of the present invention preferably comprise a surfactant, and preferably an organic polymeric compound, a soap foam enhancer, a Group II metal ion, a solvent. , A hydrotrope and other detergent compounds selected from additional enzymes.

When formulated as a composition suitable for use in a washing machine method, the composition of the present invention preferably comprises both a surfactant and a builder compound, and additionally one or more detergent components. Ingredients, preferably detergent components selected from organic polymeric compounds, bleaches, additional enzymes, foam inhibitors, dispersants, lime soap dispersants, soil suspending and redeposition inhibitors, and corrosion inhibitors. It contains. Laundry compositions may also contain softening agents as additional detergent compositions. Such compositions containing pectate lyase, mannase, xyloglucanase, when formulated as a laundry detergent composition, can provide knit fabric cleaning, stain removal and color appearance.

When formulated as a composition suitable for use in a machine dishwashing method, the composition of the present invention preferably comprises an organic polymeric compound, a bleach, an additional enzyme, a foam inhibitor,
It contains one or more components preferably selected from a dispersant, a lime soap dispersant, a soil suspending agent, an anti-redeposition agent and a corrosion inhibitor, a low-foaming nonionic surfactant, and a builder system.

The compositions of the present invention may also be used as solid or liquid detergent additive materials.
Such additive materials can be added at any stage of the cleaning operation that is intended to supplement or enhance the performance of conventional detergent compositions.

If necessary, the density of the laundry detergent compositions herein can range from 400 to 1200 g / l of composition, preferably 500 to 950 g / l of composition, measured at 20 ° C. is there. The "compact" form of the compositions herein is best reflected by density and, for compositions, by the amount of inorganic filler salt. Inorganic filler salts are a conventional component of detergent compositions in powder form, where in conventional detergent compositions the filler salt is present in substantial amounts, typically 17-35% by weight of the total composition. Exists. In a compact composition, the filler salt is present in an amount not exceeding 15% by weight of the total composition,
Preferably it is present in an amount not exceeding 10%, most preferably not exceeding 5% by weight of the composition. The inorganic filler salt as meant in the composition according to the invention is selected from alkali metal and alkaline earth metal sulfates and chlorides. A preferred filler salt is sodium sulfate. The liquid detergent compositions of the present invention can also be in "concentrated form". In such a case, the liquid detergent composition of the present invention may contain a smaller amount of water than a conventional liquid detergent. usually,
The water content of the concentrated liquid detergent is preferably less than 40% by weight of the detergent composition, more preferably less than 30% by weight, and most preferably less than 20% by weight.

[0096] Detergent compounds suitable for use in the present invention are selected from the group consisting of the compounds described below.

Surfactant systems The detergent compositions of the present invention generally comprise a surfactant system, wherein the surfactant comprises
It may be selected from nonionic and / or anionic and / or cationic and / or amphoteric and / or zwitterionic and / or semipolar surfactants. Preferably, the detergent composition of the present invention contains a nonionic and / or anionic and / or cationic surfactant. In addition, the detergent compositions according to the invention, which additionally contain nonionic, anionic and / or cationic surfactants, provide enhanced cleaning, i.e. excellent stain removal, dark cleaning and white maintenance. Bring. Without intending to be bound by theory, the combined enzymatic hydrolysis of the three enzymes of the present invention is:
A nonionic surfactant known to focus on particulate soils, resulting in small particles that are easily removed. Preferred nonionic surfactants are alkyl ethoxylated AE3-AE7. Also, a knitted fabric direct cationic surfactant,
It is believed that the combination of pectate lyase, mannanase and xyloglucanase with enzymatic hydrolysis results in improved performance.

The surfactant is usually present in a concentration from 0.1% to 60% by weight. A more preferred content concentration is 1% to 35% by weight, most preferably 1% to 30% by weight of the detergent composition of the present invention.

[0099] Surfactants are preferably formulated to be compatible with the enzyme components present in the composition. In liquid or gel compositions, the surfactant is most preferably formulated such that it promotes the stability of, or at least does not degrade, any enzymes in these compositions.

Preferred surfactant systems used according to the present invention include, as surfactants,
It includes one or more nonionic and / or anionic surfactants described herein.

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 the 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 straight or branched chain form. In a preferred embodiment, ethylene oxide is present in about 2 per mole of alkylphenol.
From about 25 moles, more preferably from about 3 to about 15 moles of ethylene oxide. Commercially available nonionic surfactants of this type include Igepal® CO-630 (GAF Corporation), and Triton® X-45, X-114, X-100 and X −102 (all 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. ing. The alkyl chain of the aliphatic alcohol is straight-chain or branched,
It can be first or second and generally contains from about 8 to about 22 carbon atoms. Preferred are those having about 8 to about 20, more preferably about 10 to about 1 carbon atoms.
A condensation product of an alcohol having 8 alkyl groups with about 2 to about 10 moles of ethylene oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide per mole of alcohol, most preferably 2 to 5 moles of ethylene oxide per mole of alcohol are present in the condensation product. Examples of this type of commercially available nonionic surfactant include Tergitol® 15-S-9.
(The condensation product of linear alcohol with 9 moles ethylene oxide C ₁₁ ~C _15),
Tergitol® 24-L-6NMW (condensation product of a C ₁₂ -C ₁₄ primary alcohol with 6 moles of ethylene oxide, showing a narrow molecular weight distribution
) (Both Union Carbide Corporation), Neodol (registered trademark) 45
-9 (the condensation product of linear alcohol with 9 moles ethylene oxide C ₁₄ -C ₁₅
), Neodol (Neodol, R) 23-3 (the condensation product of linear alcohol with 3.0 moles of ethylene oxide C ₁₂ -C _13), Neodol (Neodol, R) 45-7 (C ₁₄ ~ condensation products of linear alcohol with 7 moles of ethylene oxide C _15), Neodol (Neodol, R) 45-5 (the condensation product of linear alcohol with 5 moles of ethylene oxide C ₁₄ -C ₁₅₎ ( (Shell Chemical Company)
, Km (Kyro, R) EOB (the condensation product of alcohol with 9 moles ethylene oxide _{C 13 ~C 15) (Procter &} Gamble Company), and Genapol (
Genapol) LAO3O or O5O (the condensation product of alcohols with 3 or 5 moles of ethylene oxide C ₁₂ ~C ₁₄₎ (Hoechst) and the like. HL in these substances
A preferred range for B is 8-11, most preferably 8-10.

Further useful as surfactant-based nonionic surfactants of the present invention are those disclosed in US Pat. No. 4,565,647 (Llenado, issued on Jan. 21, 1986), which comprises: A hydrophobic group containing about 6 to about 30, preferably about 10 to 16 carbon atoms, and about 1.3 to about 10, preferably about 1.3 to about 3, and most preferably about 1.3.
Polysaccharides containing a saccharide unit of -2.7, for example, a polyglycoside hydrophilic group.
Any reducing sugar containing from 5 to 6 carbon atoms, such as glucose, galactose, can be used, and the galactosyl moiety can be replaced with a glucosyl moiety (optionally, the hydrophobic group can be in 2-, 3-, 4-etc. To yield glucose or galactose as opposed to glucoside or galactoside). The sugar linkage is
For example, one position of an additional sugar unit and 2-, 3-, 4- and / or 6 on the preceding sugar unit
-Between positions. Preferred alkyl polyglycosides have the formula:

Embedded image

Wherein R ² is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl and mixtures thereof, wherein the alkyl group has about 10 to 18, preferably about 12 carbon atoms. To about 14, n is 2 or 3, preferably 2, t is 0 to about 10, preferably 0, and x is about 1.3 to about 10, preferably about 1.3 to about 3, most preferably from about 1.3 to about 2.
7). Glycosyl is preferably derived from glucose. To prepare these compounds, an alcohol or alkyl polyethoxy alcohol is first formed and then reacted with glucose, or a source of glucose, to form a glucoside (linked at the 1-position). The additional glycosyl units may then be linked between their 1-position and the preceding glycosyl unit 2-, 3-, 4- and / or 6-position, preferably predominantly 2-position.

The condensation products of ethylene oxide with the hydrophobic base formed by the condensation of propylene oxide and propylene glycol are also suitable for use as the additional nonionic surfactant system of the present invention. The hydrophobic portion of these compounds is about 1500-
It has a molecular weight of about 1800 and is water-insoluble. The addition of a polyoxyethylene component to this hydrophobic moiety tends to increase the overall water solubility of the molecule, and the liquid character of the material is such that the polyoxyethylene content is about 5% of the total weight of the condensation product.
It is kept to a point of 0%, which corresponds to a condensation with up to about 40 mol of ethylene oxide. Examples of such compounds include commercially available Plurafac,
(Registered trademark) LF404 and Pluronic (registered trademark) surfactant (
BASF).

Also suitable for use as nonionic surfactants in the nonionic surfactant systems of the present invention are the condensation products of ethylene oxide with materials resulting from the reaction of propylene oxide and ethylenediamine. . The hydrophobic component of these substances is
It consists of the reaction product of ethylenediamine and an excess of propylene oxide and generally has a molecular weight of about 2500 to about 3000. The hydrophobic component is condensed with ethylene oxide to an extent that the condensation product contains from about 40% to about 80% by weight polyoxyethylene and has a molecular weight of from about 5,000 to about 11,000. Examples of this type of nonionic surfactant include certain commercially available Tetronic® compounds (BASF).

Suitable as nonionic surfactants for the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, primary and secondary aliphatic alcohols with about 1 to about 25 moles of Condensation products with ethylene oxide, alkyl polysaccharides, and mixtures thereof. Most preferred are 3-15 alkylphenol ethoxylates C ₈ -C ₁₄ having ethoxy groups, and 2-10 alcohol ethoxylate of C ₈ -C ₁₈ having ethoxy groups (preferably having an average C ₁₀₎
, As well as mixtures thereof.

A highly preferred nonionic surfactant is a polyhydroxyfatty acid amide surfactant of the formula:

Embedded image

Wherein R ¹ is H, or R ¹ is C _1-4 hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl or a mixture thereof, and R ² is C _5-31 A hydrocarbyl, and Z has a linear hydrocarbyl chain and is at least 3
Polyhydroxyhydrocarbyl or an alkoxylated derivative thereof in which two hydroxyls are attached directly to the chain. Preferably R ¹ is methyl, R ² is a linear C _{11-1 5} alkyl or C _16-18 alkyl or alkenyl chain such coconut alkyl or mixtures thereof, and Z is in the reductive amination reaction Reducing sugars such as glucose, fructose, maltose, lactose).

Suitable anionic surfactants used are linear alkyl benzene sulfonate, alkyl ester sulfonate surfactants, as described in “The Journal
of the American Oil Chemists Society ", 52 (1975), include linear esters of C ₈ -C ₂₀ carboxylic acids sulfonated (e.g. fatty acid) using a gas SO ₃ according Pp.323-329. Suitable Suitable starting materials include natural fatty substances obtained from tallow, coconut oil, etc. Preferred alkyl ester sulfonate surfactants, especially for laundry applications, include alkyl ester sulfonate surfactants of the following structural formula:

Embedded image

Wherein R ³ is a C ₈ -C ₂₀ hydrocarbyl, preferably alkyl, or a combination thereof, R ⁴ is a C ₁ -C ₆ hydrocarbyl, preferably alkyl, or a combination thereof, and M is a cation that forms a water-soluble salt with the alkyl ester sulfonate Suitable salt-forming cations include metals such as sodium,
Potassium and lithium, and substituted or unsubstituted ammonium cations, such as monoethanolamine, diethanolamine and triethanolamine. Preferred R ³ is C ₁₀ -C ₁₆ alkyl and R ⁴ is methyl, ethyl or isopropyl. Particularly preferred is methyl ester sulfonate, wherein R ³ is C ₁₀ -C ₁₆ alkyl.

Other suitable anionic surfactants include those of the formula ROSO ₃ M, wherein R is preferably a C ₁₀ -C ₂₄ hydrocarbyl, preferably an alkyl having a C ₁₀ -C ₂₀ alkyl component. hydroxyalkyl, more preferably an alkyl or hydroxyalkyl of C ₁₂ -C _18, M is H or a cation, such as alkali metal cations (e.g., sodium, potassium, lithium), or a, or ammonium or substituted ammonium ( For example, methyl-, dimethyl- and trimethylammonium cations, and quaternary ammonium cations such as tetramethylammonium and dimethylpiperazinium cations, and alkylamines such as ethylamine, diethylamine, triethylamine and mixtures thereof. Alkyl sulphate surfactant which is a water-soluble salt or acid). Typically, C ₁₂ -C ₁₆ alkyl chains are preferred at low wash temperatures (eg, below about 50 ° C.), and C ₁₆ -C ₁₈ alkyl chains at higher wash temperatures (eg, above about 50 ° C.). Alkyl chains are preferred.

[0113] Other anionic surfactants useful for cleaning purposes can also be included in the detergent compositions of the present invention. Examples of these include soap salts (eg, sodium, potassium,
Ammonium and mono-, - di - and substituted ammonium salts such as triethanolamine salt), primary or secondary alkane sulfonates of C ₈ -C _22, olefin sulfonates of C ₈ -C _24, for example, British Patent Specification No. 1,082,179, a sulfonated polycarboxylic acid prepared by sulfonation of a pyrrolated product of an alkaline earth metal citrate, a C ₈ -C ₂₄ alkyl polyglycol ether sulfate (10 Moles of ethylene oxide), alkyl glycerol sulphonate, fatty acyl glycerol sulphonate, fatty oleyl glycerol sulphate, alkyl phenol ethylene oxide ether sulphate, paraffin sulphonate, alkyl phosphate, isethionate, e.g. acyl isothione DOO, N- acyl taurates, alkyl succinamates Mart and sulfosuccinates, (monoester especially saturated and unsaturated C ₁₂ -C ₁₈₎ sulfosulfuron monoesters of succinate, and sulfosuccinate diesters (especially Saturated and unsaturated C ₆ -C ₁₂ monoesters), acyl sarcosinates, sulfates of alkyl polysaccharides, such as sulfates of alkyl polyglucosides (nonionic non-sulfated compounds described below), branched primary alkyls sulfates, and alkyl polyethoxy carboxylates such as formula _{RO (CH 2 CH 2 O)} k -CH 2 COO-M + ( wherein, R is alkyl of C ₈ -C _22, k is from 1 to 10 And M is a soluble salt-forming cation). Resin acids and hydrogenated resin acids, such as rosin, hardened rosin, and resin acids and hydrogenated resin acids present or derived from tall oil are also suitable.

Further examples are described in “Surface Active Agents and Detergents” (Vol. I and II by
Schwartz, Perry and Berch). A variety of such surfactants are generally described in U.S. Patent No. 3,929,678 (issued December 30, 1975; Laughlin, et al., Column 23, line 58 to column 29, line 23), the contents of which are incorporated by reference. As included herein)
Is disclosed. When included therein, the laundry detergent compositions of the present invention typically comprise about 1% by weight.
From about 40%, preferably from about 3% to about 20%, by weight of such anionic surfactant.

Highly preferred anionic surfactants include those of the formula RO (A)_mSO_ThreeM Archi
Alkoxylated sulfate surfactants and their water-soluble salts or acids.
Where R is C_Ten~ C_{twenty four}Unsubstituted C with alkyl moiety_Ten~ C_{twenty four}The alkyl or
Is a hydroxyalkyl group, preferably C₁₂~ C₂₀Alkyl or hydroxyal
Kill, more preferably C₁₂~ C₁₈Alkyl or hydroxyalkyl of the
A is an ethoxy or propoxy unit and m is greater than zero, typically about 0
. 5 to about 6, more preferably about 0.5 to about 3, and M is H or cation.
Such as metal cations (eg, sodium, potassium, lithium, calcium)
, Magnesium, etc.), ammonium or substituted ammonium cation
Can be. Alkyl ethoxylated sulfate, and alkyl propoxyl
Fluoride sulfates are contemplated in the present invention. Characteristics of substituted ammonium cations
Specific examples include methyl-, dimethyl-, trimethyl-ammonium cations,
And quaternary ammonium cations such as tetramethyl-ammonium and
Tylpiperdinium cation, as well as alkylamines such as ethylamine,
Such as those obtained from diethylamine, triethylamine, and mixtures thereof
Is mentioned. Representative examples of surfactants include C₁₂~ C₁₈Alkyl polyethoxylate
(1.0) sulfate (C₁₂~ C₁₈E (1.0) M), C₁₂~ C₁₈Alkyl poly
Ethoxylate (2.25) sulfate (C₁₂~ C₁₈E (2.25) M), C₁₂~ C ₁₈ Of alkyl polyethoxylate (3.0) sulfate (C₁₂~ C₁₈E (3.0)
M) and C₁₂~ C₁₈Alkylpolyethoxylate (4.0) sulfate (C₁₂~
C₁₈E (4.0) M, where M is selected from sodium and potassium
Is convenient).

The detergent compositions of the present invention include 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.

[0117] Cationic detergent surfactants suitable for use in the detergent compositions of the present invention are those having one long-chain hydrocarbyl group. Examples of such cationic surfactants include ammonium surfactants, such as alkyltrimethylammonium halides, as well as those having the formula:

Embedded image

(Wherein, R ² is an alkyl or alkylbenzyl group having about 8 to about 18 carbon atoms in the alkyl chain, and each R ³ is —CH ₂ CH ₂ —, —CH ₂ CH (CH ₃ ) -, - CH ₂ CH
(CH ₂ OH) —, —CH ₂ CH ₂ CH ₂ —, and mixtures thereof, wherein each R ⁴ is C ₁ -C ₄ alkyl, C ₁ -C ₄ hydroxyalkyl, A benzyl ring structure formed by joining R ⁴ groups, —CH ₂ CHO—CHO
HCOR ⁶ CHOHCH ₂ OH (where R ⁶ is any hexose or hexose polymer having a molecular weight of less than about 1000), and if y is not 0, hydrogen is selected from the group consisting of hydrogen and R ⁵ is R ⁴ Or an alkyl chain, wherein the total number of carbon atoms in R ² + R ⁵ is about 18 or less, and each y is from 0 to about 10
Wherein the sum of y is from 0 to about 15 and X is any of the compatible anions.
.

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

Embedded image

Wherein R ₁ is a short chain length alkyl (C ₆ -C ₁₀ ) or an alkylamidoalkyl of the formula (II):

Embedded image Wherein y is 2-4, preferably 3. R ₂ is H or C ₁ -C ₃ alkyl; x is 0-4, preferably 0-2, most preferably 0; R ₃ , R ₄ and R ₅ can all be the same or different and can all be short-chain alkyl (C ₁ -C ₃ ) or alkoxylated alkyl of formula III;

X ^- is a counter ion, preferably a halide, such as chloride or methyl sulfate;

Embedded image (Wherein R ₆ is C ₁ -C ₄ and z is 1 or 2)). Preferred quaternary (quat) ammonium surfactants are as described in Formula I, wherein R ₁ is C ₈ , C ₁₀ or a mixture thereof, x = 0 and R _3, R ₄ = CH ₃ and _{R 5 = CH 2 CH 2 OH} .

Highly preferred cationic surfactants are water-soluble quaternary ammonium compounds useful in the compositions of the present invention having the formula:

Embedded image

(Wherein, R₁Is C₈~ C₁₆And R is_Two, R_ThreeAnd R_FourAre independently
, C₁~ C_FourAlkyl, C₁~ C_FourHydroxyalkyl, benzyl and-(C_Two
H₄₀)_xH (where x has a value of 2 to 5) and X is an anion
). R_Two, R_ThreeOr R_FourShould be only one of benzyl. R ₁ Preferred alkyl chain lengths for₁₂~ C_FifteenIn particular, the alkyl group is
It is a mixture of chain lengths derived from nuts or palm palm kernel fat, or olefin storage.
Product or obtained synthetically by OXO alcohol synthesis. R_Two, R_ThreeAnd R_FourAbout
More preferred groups are methyl and hydroxyethyl groups, wherein the anion X is a halide,
It may be selected from meso sulphate, acetate and phosphate ions. Honcho
Examples of suitable quaternary ammonium compounds of formula (i) for use in the text are set forth below.
Indicate: coconut trimethylammonium chloride or bromide, coconut methyldihydroxyethylammonium chloride or bromide, decyltriethylammonium chloride, decyldimethylhydroxyethylammonium chloride or bromide, C_12-15Dimethylhydroxyethylammonium chloride or bromide, coconut dimethylhydroxyethylammonium chloride or bromide, myristyltrimethylammonium methylsulfate, lauryldimethylbenzylammonium chloride or bromide, lauryldimethyl (ethenoxy)_FourAmmonium chloride or bromide, choline ester (compound of formula (i), wherein R₁But,

Embedded image And R ₂ , R ₃ and R ₄ are methyl). Dialkylimidazolines [Compounds of Formula (i)] Other cationic surfactants useful herein are described in US Pat. No. 4,228,
No. 044 (Cambre, published October 14, 1980) and European patent application EP000,224.
It is also mentioned in the issue.

Typical cationic knit fabric softening components include water-insoluble quaternary ammonium knit fabric softening activators or their corresponding amine precursors, but are most commonly used. Is a long alkyl chain ammonium chloride or methyl sulfate. Examples of preferred cationic softeners are: 1) ditallow dimethyl ammonium chloride (DTDMAC), 2) dihydrogenated tallow dimethyl ammonium chloride, 3) dihydrogenated tallow dimethyl ammonium methyl sulfate, 4) distearyl Dimethylammonium chloride, 5) dioleyldimethylammonium chloride 6) dipalmitylhydroxyethylmethylammonium chloride, 7) stearylbenzyldimethylammonium chloride, 8) tallow trimethylammonium chloride 9) hydrogenated tallow trimethylammonium chloride, 10) _{C12- 14} alkylhydroxyethylammonium dimethyl ammonium chloride, 11) C _12-18 alkyl dihydroxyethyl methyl ammonium chloride, 12) di (stearoyl oxy ethyl) dimethicone Ammonium chloride (DSO
EDMAC), 13) di (tallow-oxy-ethyl) dimethylammonium chloride, 14) ditallow imidazolinium methylsulfate, 15) 1- (2-tallowylamidoethyl) -2-tallowylimidazolinium methylsulfate Fate.

[0125] Biodegradable quaternary ammonium compounds have been shown as alternatives to the two long-chain alkyl ammonium chlorides and methyl sulfates traditionally used. Such quaternary ammonium compounds contain long chain alkyl (alkenyl) groups that are hindered by a functional group such as a carboxy group. Such substances and textile softening compositions containing them are disclosed in a number of publications, such as EP-A-0,040,562 and EP-A-0,239,910.

The quaternary ammonium compounds and amine precursors herein have the following formula (I) or (II):

Embedded image

(In the formula, Q represents —OC (O) —, —C (O) —O—, —OC (O) —O—, —
^{NR 4 -C (O) -,} - C (O) -NR 4 - is selected from, R ¹ is _{(CH 2) n -Q-T} 2 or T ^3, R ² is (CH _{2) m} - a Q-T ⁴ or T ⁵ or R ^3, R ³ is hydroxyalkyl or H alkyl, or C ₁ -C ₄ a C ₁ ~C ^_4, R ₄ is H or alkyl of C ₁ -C ₄ 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 of 1-4 And X ^- is a softener-compatible anion). Examples of softener compatible anions include, but are not limited to, chloride or methyl sulfate.

The alkyl or alkenyl chains T ¹ , T ² , T ³ , T ⁴ , T ⁵ must contain at least 11 carbon atoms, preferably at least 16 carbon atoms. The chains can 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.

The following are specific examples of quaternary ammonium compounds suitable for use in the aqueous textile soft composition of the present invention: 1) N, N-di (tallowyl-oxy-ethyl) -N , N-dimethylammonium chloride, 2) N, N-di (tallowyl-oxy-ethyl) -N-methyl, N (2-hydroxyethyl) ammonium methyl sulfate, 3) N, N-di (2-tallow) Yl-oxy-2-oxo-ethyl) -N, N-dimethylammonium chloride; 4) N, N-di (2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl)
-N, N-dimethylammonium chloride, 5) N- (2-tallowyl-oxy-2-ethyl) -N- (2-tallowyl-oxy-2-oxo-ethyl) -N, N-dimethylammonium chloride 6) N, N, N-tri (tallowyl-oxy-ethyl) -N-methylammonium chloride 7) N- (2-tallowyl-oxy-2-oxo-ethyl) -N- (tallowyl- N
, N-dimethylammonium chloride, and 8) 1,2-ditallowyl-oxy-3-trimethylammoniopropane chloride and mixtures of any of the foregoing. When included therein, the detergent compositions of the present invention typically comprise from 0.2% to about 25%, preferably from about 1% to about 8%, by weight of such a cationic surfactant. .

[0130] Amphoteric surfactants are also suitable for use in the detergent compositions of the present invention. These surfactants are widely described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines, wherein the aliphatic group can be straight or branched. obtain. One of the aliphatic substituents has at least about 8, and typically from about 8 to about 18, carbon atoms and at least one contains an anionic water-soluble group, such as carboxy, sulfonate, sulfate. For examples of amphoteric surfactants, see US Pat. No. 3,929,678 (Laughlin et al., Issued Dec. 30, 1975) at column 19-18.
See ~ line 35. When included therein, the detergent compositions of the present invention typically contain from 0.2% by weight to
It contains about 15% by weight, preferably about 1% to about 10% by weight of such amphoteric surfactant.

[0131] Zwitterionic surfactants are also suitable for use in the cleaning compositions.
These surfactants are widely 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. obtain. For examples of zwitterionic surfactants, see US Pat. No. 3,929,678 (Laughlin et al., December 1975).
See column 38, line 38 to column 22, line 48, issued on 30th). When included therein, the detergent compositions of the present invention typically contain from 0.2% by weight to
It contains about 15%, preferably about 1% to about 10%, by weight of such zwitterionic surfactants.

The semi-polar nonionic surfactant comprises one component having about 10 to about 18 carbon atoms and two components selected from the group consisting of an alkyl group having about 1 to about 3 carbon atoms and a hydroxyalkyl group. A water-soluble amine oxide containing: an alkyl component having about 10 to about 18 carbon atoms and two components selected from the group consisting of an alkyl group having about 1 to about 3 carbon atoms and a hydroxyalkyl group. A phosphine oxide; and a water-soluble sulfoxide containing one alkyl component having about 10 to about 18 carbon atoms and one component selected from the group consisting of an alkyl group having about 1 to about 3 carbon atoms and a hydroxyalkyl group. A special type of nonionic surfactant.

Semipolar nonionic detergent surfactants include amine oxide surfactants having the formula:

Embedded image Wherein R ³ is an alkyl, hydroxyalkyl, or alkylphenyl group having about 8 to about 22 carbon atoms or a mixture thereof, and R ⁴ is an alkylene or hydroxyalkylene group having about 2 to about 3 carbon atoms, or a group thereof. A mixture wherein x is 0 to about 3 and R ⁵ is an alkyl or hydroxyalkyl group each having about 1 to about 3 carbon atoms, or a polyethylene oxide group containing about 1 to about 3 ethylene oxide groups R ⁵ groups are linked to each other, for example via an oxygen or nitrogen atom,
A ring structure can be formed).

These amine oxide surfactants include, in particular, C ₁₀ -C ₁₈ alkyldimethylamine oxides and C ₈ -C ₁₂ alkoxyethyldihydroxyethylamine oxides. When included therein, the cleaning composition of the present invention typically comprises 0.2
% To about 15%, preferably about 1% to about 10%, by weight of such semipolar nonionic surfactants.

The detergent composition of the present invention may comprise a co-surfactant selected from the group of primary or tertiary amines
An agent may be further included. Primary amines suitable for use in the present invention include those of formula R₁
NH_Two(Where R₁Is C₆~ C₁₂Of, preferably C₆~ C_TenAn alkyl chain of_Four
X (CH_Two)_n(Wherein X is -O-, -C (O) NH- or NH-, and R is_FourIs C₆~
C₁₂Wherein n is from 1 to 5, preferably 3.
Is mentioned. R₁Alkyl chains are straight or branched and up to 12 are preferred.
Preferably it can be broken by less than 5 ethylene oxide components. The said in this specification
A preferred amine of the formula is an n-alkylamine. Suitable for use herein.
The amines obtained are 1-hexylamine, 1-octylamine, 1-decylamine and
And laurylamine. Other preferred primary amines include C ₈ ~ C_TenOxypropylamine, octyloxypropylamine, 2-ethyl
Hexyloxypropylamine, laurylamidopropylamine and amidopro
Pyramine.

[0136] Tertiary amines suitable for use herein are tertiary amines having the formula R ₁ R ₂ R ₃ N, wherein R ₁ and R ₂ are C ₁ -C ₁ . C ₈ alkyl chain or

Embedded imageAnd R_ThreeIs C₆~ C₁₂Of, preferably C₆~ C_TenIs an alkyl chain of
R_ThreeIs R_FourX (CH_Two)_n(Wherein X is -O-, -C (O) NH- or NH-, and R is _Four Is C_Four~ C₁₂And n is 1-5, preferably 2-3. R_FiveIs H
Or C₁~ C_TwoAlkyl and x is 1-6. R_ThreeAnd R_FourIs a straight or branched chain
And R_ThreeThe alkyl chain has up to 12, preferably less than 5, ethylene oxide components.
Can be interrupted in minutes.

A preferred tertiary amine is R ₁ R ₂ R ₃ N, wherein 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).

Also preferred are amidoamines of the formula:

Embedded image Wherein R ₁ is C ₆ -C ₁₂ alkyl, n is 2-4, preferably n is 3, and R ₂ and R ₃ are C ₁ -C ₄ .

The most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, C ₈ -C ₁₀ oxypropylamine, Ncoco 1-3 diaminopropane, coconut Alkyldimethylamine, lauryldimethylamine, laurylbis (hydroxyethyl) amine, cocobis (hydroxyethyl) amine, laurylamine 2 mol propoxylation, octylamine 2 mol propoxylation, laurylamidopropyldimethylamine, C _8-10 amide amidopropyl dimethylamine dimethylamine and C ₁₀ and the like. Most preferred amines for use in the compositions of the present invention are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Particularly preferred are n-dodecyldimethylamine and bishydroxyethyl coconut alkylamine and oleylamine 7-fold ethoxylation, laurylamidopropylamine and cocoamidopropylamine.

Conventional detergent enzymes, preferably detergent compositions, comprise, in addition to mannanase, pectate lyase and xyloglucanase, one or more enzymes which provide a cleaning, knitting and / or hygiene effect, preferably , Pectin lyase, protease, cellulase and / or amylase.

Examples of the enzymes include cellulase, hemicellulase, peroxidase, protease, glucoamylase, amylase, xylanase, lipase, phospholipase, esterase, cutinase, other pectinases, keratanase, reductase, oxidase, phenol oxidase, lipoxygenase, and ligninase. , Pullulanases, tannases, pentosanases, malanases, β-glucanases, arabinosidases, hyaluronidases, chondroitinases, laccases or mixtures thereof.

The various pectinolytic enzymes have unique substrate specificity, activity and stability at different hardness, pH, temperature, surfactant and other detergent component matrix conditions.
Pectin degrading enzymes are particularly directed at the degradation of pectin substrates and certain plant cell walls.
In particular, the pectate lyase enzyme essentially directs pectic acid chains in plant cell walls, such as low methoxy pectin, while the pectin lyase more specifically directs esterified pectin chains, such as high methoxy pectin. . Furthermore, pectate lyase was found to be metal sensitive, especially calcium sensitive, and pectin lyase did not require metal for stabilization and optimal enzyme activity. Surprisingly, it has been found that a wide range of substrate specificities and high adaptability to various washing conditions are achieved by further combining the pectin lyase with the pectate lyase of the invention. This results in synergistic cleaning properties, especially for removal of plant-based stains / stains and body stains.

The pectin lyase enzyme is classified as EC 4.2.2.20 in the EC classification, and is preferably substantially free from other pectin enzymes, acts on pectic acid, and has an alpha-1 activity.
-4 resulting in non-hydrolytic cleavage of the glycosidic bond and terminal 4-deoxy-6-α-
This leads to oligosaccharides of the D-galacto-enuronosyl group.
The pectin lyase of the present invention is substantially free of other pectin enzymes. By "substantially free of other pectin enzymes" is meant a pectin lyase enzyme-containing composition containing less than 25%, preferably less than 15%, more preferably less than 5% of a pectin enzyme that is not a pectin lyase enzyme. I do. Enzyme activity was determined by K. Horikoshi in Ag
r. Biol. Chem, Vol 36 (2), 286, "Assay of trans-eliminase activities towa
rd pectin and pectic acid ".

Preferred pectin lyases for the purposes of the present invention are described in co-pending international application PCT / D
K98 / 00514 (International application filed on November 24, 1998, WO 99/2708)
3, published under 3), i) a polypeptide produced by Bacillus Licheniformis, ATCC 14580, or ii) PCT / DK98 / 00514 SEQ ID NO: 2 31-49.
A polypeptide containing the amino acid sequence shown at position 4, or iii) an analog of the polypeptide defined in i) or ii), having at least 60% homology with said polypeptide, or iv) Arginine at positions 377 and 383 of SEQ ID NO: 2 of PCT / DK98 / 00514 are maintained and the derived polypeptide is at least 60%
And a polyclonal antibody derived against the peptide in a purified form derived from the substitution, deletion or addition of one or several amino acids of the peptide, provided that the peptide has immunology. That are reactive to

Cellulases that can be used in the present invention include both bacterial and fungal cellulases. Preferably, they have an optimal pH value in the range of 5-12,
Has a specific activity higher than EVU / mg (cellulose viscosity unit). Suitable cellulases are described in U.S. Patent No. 4,435,307 (Barbesgoard et al.), J610783.
No. 84, and each Humicola insolens,
Trichoderma, Thielavia and Sporotricum (
WO96 / 02653 which discloses fungal cellulases produced from Sporotrichum)
Issue. EP 739982 describes a novel cellulase isolated from Bacillus sp. A suitable cellulase is GB-A-2.075.0
No. 28, GB-A-2.095.275, DE-OS-2.2477.832 and WO 95/26398. An example of such a cellulase is Humicola grisea
var. thermoidea), in particular a cellulase produced by the Humicola DSM 1800 strain.

Other suitable cellulases have a molecular weight of about 50 KDa, an isoelectric point of 5.5, and 41
Cellulase originating from the Humicola insolens of 5 amino acids, and ^~ 43 kD from Humicola insolens DSM1800 exhibiting cellulase activity
Endoglucanase. A preferred endoglucanase component is PCT
It has the amino acid sequence disclosed in patent application WO 91/17243. Further, a suitable cellulase is Trichoderma longibrachiatum described in WO94 / 21801 (Genencor, published on September 29, 1994).
) -Derived EGIII cellulase. Particularly suitable cellulases are those having a color care effect. Examples of such cellulases are described in European Patent Application No. 9
No. 1202879.2 (Novo, filed Nov. 6, 1991). Kalezyme and cellzyme (Novo Nordisk A / S) are particularly useful. WO
See also WO 91/17244 and WO 91/21801. Other suitable cellulases for textile care and / or cleaning properties are described in WO
96/34092, WO 96/17994 and WO 95/24471. The cellulase is usually contained in the detergent composition at a concentration of 0.0001% to 2% by weight of the pure enzyme of the detergent composition.

Peroxidase enzymes are sources of oxygen, such as percarbonate, perborate, persulfate
Used in combination with salts, hydrogen peroxide, etc., and phenolic substrates as bleach enhancers
It is. They are removed from the substrate for "solution bleaching", i.e. during the washing operation.
Used to prevent the transfer of dyes or pigments to other substrates in the washing solution.
You. Peroxidase enzymes are known in the art and include, for example,
Horseradish peroxidase, ligninase and haloperoxidase, such as
Chloro and bromo-peroxidase. Peroxidase-containing washing
Agent compositions are described, for example, in PCT International Applications WO 89/099813, WO 89/09
813 and European Patent Application EP 91202882.6 (November 6, 1991).
And EP 968700133.8 (filed on February 20, 1996).
It has been disclosed. Laccase enzymes are also suitable. Enhancers are generally included at a level of from 0.1% to 5% by weight of the total composition. Good
Preferred enhancers are substituted phenthiazine and phenoxazine 10-phenothiazi.
Propionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (E
PC), 10-phenoxazine propionic acid (POP) and 10-methylphen
Noxazine (described in WO 94/12621), and substituted syringates (C _Three ~ C_FiveAnd phenol. Sodium overcarbon
Acid salts or perborates are preferred sources of hydrogen peroxide. The peroxidase is usually present in an amount of 0.0001% to 2% by weight of the detergent composition.
% Active enzyme is included in the detergent composition.

Other preferred enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for detergents include Pseudomonas (Pseu
domonas) group of microorganisms, such as those produced by Pseudomonas stutzeri ATCC 19.154 as disclosed in GB 1,372,034. Suitable lipases include those that show a positive immunological cross-reactivity with antibodies to the lipase produced by the microorganism Pseudomonas fluorescent IAM1057. This lipase is trade name of lipase P "Amano" and is available from Amano Pharmaceutical Co. Ltd.
d., Nagoya, Japan, hereinafter referred to as "Amano-P". Other suitable commercially available lipases include Amano-CES, Chromobacter viscosum (eg, Chromobacter viscosum var.
lipase derived from lipolyticum NRRLB3663) (Toyo Jozo Co., Tagata, J
apan), Chromobacter viscosum lipase and Pseudomonas gladioli (Pseu) from US Biochemical Corp., USA and Disoiynth Co., The Netherland.
domonas gladioli). Particularly suitable lipases have been found to be very effective when used in combination with the compositions of the present invention.
Lipase (registered trademark) and Lipomax (Lipomax®) (Gist-
Brocades), and lipases such as Lipolase (registered trademark) and Lipolase Ultra (registered trademark) (Novo). Further suitable are EP258068, WO92 / 05249 and WO95 / 2261.
No. 5 (Novo Nordisk) and WO 94/03578, WO 95/35381
And lipolytic enzymes described in WO 96/00292 (Unilever).

Also suitable are cutinases [EC 3.1.1.50], which can be considered to be a special type of lipase, a lipase that does not require surface activation. Addition of cutinase to the detergent composition is described, for example, in WO-A-88 / 09367.
(Genencor), WO 90/09446 (Plant Genetic System), and WO 94/14963 and WO 94/14964 (Unilever). The lipase and / or cutinase is usually included in the detergent composition at a concentration of 0.0001% to 2% pure enzyme by weight of the detergent composition.

Suitable proteases are subtilisins (subtilisins BPN and BPN ') obtained from certain strains of B. subtilis and B. licheniformis. One suitable protease is Novo, Denmark
It is obtained from one strain of the genus Bacillus which has been developed and marketed by Industries A / S (hereinafter referred to as "Novo") as ESPERASE (R) and exhibits maximum activity over the pH range of 8-12. Preparation of this and similar (analog) enzymes
It is described in British Patent 1,243,784 (Novo). Other suitable proteases include ALCALASE®, Durazyme (DUR
AZYN® and SAVINASE® (Novo), and maxatase (MAXATASE®), maxacal (MAXACAL®), properase (PROPERASE®) and maxapem (MAXAPEM®) ( (Gist-Brocades). Proteolytic enzymes are modified bacterial serine proteases, for example European Patent Application 87 303761
. No. 8 (filed on April 28, 1987) (especially pages 17, 24 and 98)
What is referred to herein as "Protease B" and European Patent Application No. 19
No. 9,404 (Venegas, published Oct. 29, 1986) and modified bacterial serine proteases, such as those referred to herein as "protease A", also referred to as modified protease serine proteases. Including. Suitable is what is referred to herein as "Protease C", which replaces lysine for arginine at position 27, tyrosine for valine at position 104, and serine for asparagine at position 123. It is a variant of the alkaline serine protease from Bacillus that replaces and replaces threonine with alanine at position 274. Protease C is described in EP 90915958: 4 corresponding to WO 91/06637 (published May 16, 1991). In particular, genetically modified variants of protease C are also included in the present invention.

A preferred protease, referred to as "Protease D", is a mutation of a carbonyl hydrolase in which the amino acid sequence is not found in nature, but is described in WO 95/105.
No. 91 and C.I. In a patent application by Gauche et al., US Serial No. 08 / 322,6
No. 77 (filed on October 13, 1994, “Bleaching composition containing protease enzyme”)
According to the numbering of Bacillus amyloliquefaciens subtilisin described in above, the position corresponding to +76 of the carbonyl hydrolase, and preferably +99, +101
, +103, +104, +107, +123, +27, +105, +109, +
126, +128, +135, +156, +166, +195, +197, +2
04, +206, +210, +216, +217, +218, +222, +26
A plurality of amino acid residues in the carbonyl hydrolase at different positions in combination with one or more amino acid residue positions corresponding to positions selected from the group consisting of 0, +265, and / or +274; And obtained from a carbonyl hydrolase precursor by substituting

Also suitable are variants of the carbonyl hydrolase of the protease described in WO 95/10591, obtained by substituting a plurality of amino acid residues in the carbonyl hydrolase precursor with different amino acids. Wherein the plurality of substituted amino acid residues in the precursor enzyme are position number +210 and one or more of the following residues: +3
3, +62, +67, +76, +100, +101, +103, +104, +1
07, +128, +129, +130, +132, +135, +156, +15
8, +164, +166, +167, +170, +209, +215, +217
, +218 and +222, where the position numbers are the naturally occurring Bacill
position numbers of subtilisin from C. us amyloliquefaciens, or position numbers of equivalent amino acid residues in other carbonyl hydrolase or subtilisin such as Bacillus lentus subtilisin (co-pending patent application US Serial No. 60 / 048,550 ( (June 4, 1997).

Also suitable for the present invention are the patent applications EP 251 446 and WO 91/0
6637, the protease BLAP® described in WO 91/02792, and variants thereof as described in WO 95/23221. See also the high pH protease from Bacillus sp. NCIMB 40338 described in WO 93 / 18140A (Novo). Enzyme detergents containing proteases, one or more other enzymes and a reversible protease inhibitor are described in WO 92 / 03529A (Novo). If desired, proteases that exhibit reduced adsorption and increased hydrolysis as described in WO 95/07791 (Procter & Gamble) can be used. Recombinant trypsin-like protease for detergents suitable herein is described in WO 94/2558.
No. 3 (Novo). Other suitable proteases are described in European Patent No. 5
No. 16200 (Unilever). Proteolytic enzymes comprise from 0.0001% to 2%, preferably from 0.001% to 0.2%, more preferably from 0.005% to 0.1% by weight of the composition.
Included in the detergent compositions of the present invention at the level of wt% pure enzyme.

Amylases (α and / or β) may be included for the removal of carbohydrate-based stains. WO 94/02597 (Novo Nordisk A / S, published February 03, 1994) describes a cleaning composition containing a mutant amylase (WO 95/10603 (N
ovo Nordisk A / S, published April 20, 1995). Other known amylases for use in the cleaning compositions include both α- and β-amylases. Alpha-amylases are known in the art and include, for example, U.S. Patent Nos. 5,003,257, EP252,666, WO91 / 00353, F.
R2,676,456, EP285,123, EP525,610, EP
368,341 and British Patent Specification No. 1,296,839 (Novo). Other suitable amylases are described in WO 94/1831
No. 4 (published August 18, 1994) and WO 96/05295 (Genencor, February 1996)
Amylase described in WO95 / 10603 (published April 1995) and amylase variants with additional modifications in the direct parent available from Novo Nordisk A / S disclosed in WO95 / 10603 (published April 1995) It is. Also appropriate is EP27
7216, WO95 / 26397 and WO96 / 23873 (all Novo
Amylase described in Nordisk).

Examples of commercially available α-amylase products are Purafect Ox Am® (Genencor), as well as Termamyl®, Ban,
(Registered trademark), Fungamyl (registered trademark) and Duramil (registered trademark) (all Novo Nordisk A / S Denmark). WO 95/26397 describes another suitable amylase, namely as measured by the Phadebas® α-amylase activity assay at a temperature range of 25 ° C. to 55 ° C. and at a pH value in the range of 8 to 10. Describe an α-amylase characterized by having a specific activity at least 25% higher than the specific activity of Termamyl (registered trademark). Suitable are variants of the aforementioned enzymes described in WO 96/23873 (Novo Nordisk). Other amylolytic enzymes exhibiting improved properties with respect to activity levels as well as the combination of thermostability and higher activity levels are described in WO 95/35382. The amylolytic enzyme is present in an amount of 0.0001% to 2%, preferably 0% by weight of the composition.
. 00018% by weight to 0.06% by weight, more preferably 0.00024% by weight
A pure enzyme at a concentration of ０．０0.048% by weight may be included in the detergent composition of the present invention.

The enzymes may be of any suitable origin, for example, of plant, animal, bacterial, fungal and yeast origin. The origin can also be mesophilic or extremophilic (cryophilic, cryogenic, thermophilic, barophilic, alkaliphilic, acidophilic, halophilic, etc). Purified or unpurified forms of these enzymes may be used.

Today, it is common practice to modify wild-type enzymes by protein / genetic engineering techniques to optimize their performance efficiency in the detergent compositions of the present invention. For example, variants can be designed to increase the suitability of the enzyme for commonly encountered components of such compositions. Alternatively, the variants can be designed such that the optimal pH of the enzyme variant, the stability of the bleach or chelating agent, the enzymatic activity, etc., are tailored to the particular cleaning application.

In particular, attention should be paid to oxidation sensitive amino acids for bleach stability and surface charge for surfactant compatibility. The isoelectric point of such enzymes can be modified by substitution of some charged amino acids, for example, increasing the isoelectric point can help improve compatibility with anionic surfactants . Enzyme stability can be further enhanced, for example, by creating additional salt bridges and enhancing calcium binding sites to increase chelator stability. Particular attention must be paid to cellulases, as most cellulases have a discrete binding region (CBD). The properties of such enzymes can be altered by altering these regions.

The enzymes are generally included in detergent compositions at a concentration of pure enzyme of 0.0001% to 2% by weight of the detergent composition. Enzymes can be separate single components (granules, granules, stabilized liquids, etc. containing one enzyme) or as a mixture of two or more enzymes (
(Eg, auxiliary granules). Other suitable detergent ingredients that may be added are described in co-pending European Patent Application 928700
No. 18.6 (filed on Jan. 31, 1992) is an enzyme oxidizing scavenger (scavenger). An example of such a scavenger is ethoxylated tetraethylene polyamine.

The range of enzyme substances and their means of inclusion in synthetic detergent compositions are described in WO 9307
No. 263A and WO 9307260 A (Genencor International), WO 89
No. 08694A (Novo) and U.S. Pat. No. 3,553,139 (January 5, 1971, McCarty et al.). The enzyme is further disclosed in U.S. Pat. No. 4,101,45.
No. 7 (Place et al., July 18, 1978) and U.S. Pat. No. 4,507,219 (Hughes).
, March 26, 1985). Enzyme substances useful in liquid detergent formulations and their inclusion in such formulations are described in U.S. Pat. No. 4,261,868 (Hora
Et al., April 14, 1981). The enzymes used in detergents can be stabilized by various techniques. Enzyme stabilization techniques are described in U.S. Pat. No. 3,600,319 (19
Gedge et al., Aug. 17, 71), EP 199,405 and EP 200,
No. 586 (October 29, 1986, Venegas) and is exemplified. Enzyme stabilization systems are also described, for example, in US Pat. No. 3,519,570. Useful Bacillus sp. AC13 that produces proteases, xylanases and cellulases is described in WO
No. 9401532A (Novo).

Color Care and Knitted Fabric Care Effects Techniques that provide one type of color care effect may also be included. Examples of these techniques are metal catalysts for color retention. Such metal catalysts are described in co-pending European Patent Application No. 92870181.2. Dye fixatives, polyolefin dispersions for anti-shrinkage and improved water absorption, perfume, and amino-functional polymers for color care treatment and perfume directness are also additional examples of color care / textile care techniques and co-pending patent applications No. 96870140.9 (filed on Nov. 7, 1996).

[0162] A fabric softener may also be included in the cleaning compositions of the present invention. These agents can be of inorganic or organic type. Inorganic softeners are exemplified by smectite clay (green clay) disclosed in GB-A-1400898 and US Pat. No. 5,019,292. GB-A-154276 and EP as organic knit fabric softeners
The water-insoluble tertiary amines as disclosed in JP -B0011340 and the like, a combination of a mono C ₁₂ -C ₁₄ quaternary ammonium salts is disclosed in Patent EP-B-0026527 and EP-B-0026528 Patent And the long-chain amide is EP-B-02
No. 42919. Other useful organic components of the fabric softening system include high molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0313146.

The concentration of smectite (green clay) is usually in the range from 2% to 20% by weight, more preferably from 5% to 15% by weight, the substance being present as a dry-mix component in the rest of the formulation. Will be added. Organic knitting fabric softeners, such as water-insoluble tertiary amines or bilong chain amide materials, are included at a concentration of 0.5% to 5% by weight, usually 1% to 3% by weight, while The high molecular weight polyethylene oxide material and the water-soluble cationic material are included at a concentration of 0.1% to 2% by weight, usually 0.15% to 1.5% by weight. These materials are usually added to the spray-dried portion of the composition, but in some cases, add them as dry mixed particles, or as a melt, the multiple solid constituents of other compositions. Spraying over the ingredients is more convenient.

Bleaching Agents Surprisingly, it has been found that the detergent compositions of the present invention further containing a bleaching agent, especially a bleaching active bleaching system, provide food stain removal and whiteness retention.
While not intending to be bound by theory, smaller plastid particles, resulting from the combined hydrolysis of pectate lyase, mannanase and xyloglucanase, are easier with bleach activators, especially at lower temperatures. Believed to be attacked.

Preferred detergent components that can be included in the detergent composition of the present invention are 400 to
Bleaching agents such as hydrogen peroxide, PB1, PB4 and percarbonate having a particle size of 800 microns. These bleach components may contain one or more oxygen bleaches, and may contain one or more bleach activators, depending on the bleach selected. The oxygen bleach compounds of the present invention may typically be present at a concentration of about 1% to about 25%.

The bleach component for use herein can be any bleach useful in cleaning compositions, including oxygen bleaches, as well as others known in the art. Bleaches suitable for the present invention can be activated or deactivated bleaches.

One class of oxygen bleaches that may be used include percarboxylic acid bleaches and salts thereof. Suitable examples of this type of drug include magnesium monoperoxyphthalate hexahydrate, magnesium salt of metachloroperbenzoic acid, 4-nonylamino-4
-Oxoperoxybutyric acid and diperoxidedecanedioic acid. Such bleaches are disclosed in U.S. Patent No. 4,483,781, U.S. Patent Application No. 740,446, European Patent Application No. 0,133,354 and U.S. Patent No. 4,412,934. Highly preferred bleaches also include 6-nonylamino-6-oxoperoxycaproic acid as described in U.S. Pat. No. 4,634,551. Another type of bleach that may be used includes halogen bleaches. Examples of hypohalite bleaches include, for example, trichloroisocyanuric acid, and sodium and potassium dichloroisocyanurate, and N-chloro and N-bromoalkanesulfonamides. Such substances are usually added at 0.5 to 10% by weight of the finished product, preferably 1 to 5% by weight.

Hydrogen peroxide releasing agents include bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-sulfonate (NOBS, described in US Pat. No. 4,412,934), 3,5-trimethylhexanoloxybenzenesulfonate (Described in ISONOBS, EP 120,591) or pentaacetylglucose (PAG), or N-nonanoyl-6-aminocaproic acid (NAC
A-OBS, described in WO 94/28106), which are perhydrolyzed to form peracids as active bleach species,
Provides improved bleaching effect. Further suitable activators are acylated citrate esters as disclosed in co-pending European Patent Application No. 91870207.7, and
The following formulation as disclosed in Procter-Gamble co-pending US Patent Application Nos. 60 / 022,786 (filed July 30, 1996) and 60 / 028,122 (filed October 15, 1996) Is an asymmetric acyclic acid imide bleach activator of the formula:

Embedded image

(Wherein, R₁Is C₇~ C₁₃Is a linear or branched saturated or unsaturated alkyl group of_TwoIs C₁~ C₈Is a linear or branched saturated or unsaturated alkyl group of_ThreeIs C ₁ ~ C_FourIs a linear or branched saturated or unsaturated alkyl group).

Useful bleaching agents, including peroxy acids for use in the detergent compositions of the present invention and bleaching systems including bleaching activators and peroxygen bleaching compounds, are described in our co-pending application U.S. Pat.
SSN08 / 136,626, PCT / US95 / 07823, WO95 /
27772, WO95 / 27773, WO95 / 27774 and WO95
/ 27775.

[0171] Hydrogen peroxide may also be present by the addition of an enzyme system (ie, an enzyme and its substrate) that can generate hydrogen peroxide at the beginning or during the washing and / or rinsing step. Such an enzyme system is described in European Patent Application No. 91202655.6 (1 January 1991).
(Filed on 09:00).

[0172] Metal-containing catalysts for use in the bleach compositions include cobalt-containing catalysts, such as pentaamine acetate cobalt (III) salts, and manganese-containing catalysts, such as EPA 549271, EPA 549272, EPA 458297, U
S5,246,621, EPA458398, US5,194,416 and US5,114,611. A bleaching composition comprising a peroxy compound, a manganese-containing bleaching catalyst and a chelating agent is described in Patent Application No. 94870206.3.

Bleaches other than oxygen bleaches are known to those skilled in the art and may be utilized in the present invention. Certain such classes of non-oxygen bleaches include light activated bleach, such as zinc sulfonate and / or aluminum phthalocyanine. These substances can deposit on the substrate during the cleaning process. Upon irradiation with light in the presence of oxygen,
For example, hanging the garment to dry in the sun activates the sulfonated zinc phthalocyanine, thus bleaching the substrate. A preferred zinc phthalocyanine and light activated bleaching method is described in U.S. Pat. No. 4,033,718. Detergent compositions can usually contain from about 0.025% to about 1.25% by weight of the sulfonated zinc phthalocyanine.

Builder System The detergent composition of the present invention preferably further comprises a builder system, more preferably an inorganic builder, most preferably zeolite A, sodium layered silica and / or sodium tripolyphosphate. Surprisingly, it has been found that the detergent compositions of the present invention further containing such builders provide enhanced cleaning properties. Without wishing to be bound by theory, it is believed that calcium adheres to pectin- and hydrocolloid gums containing stains / soils. It is therefore believed that the use of builders removes trapped calcium and aids the enzymatic action of pectate lyase, mannanase and xyloglucanase.

[0175] Any conventional builder system is suitable for use herein, examples of which include aluminosilicate materials, silicates, polycarboxylates, alkyl-
Or substances such as alkenylsuccinic and fatty acids, ethylenediaminetetraacetic acid, diethylenetriaminepentamethylene acetate, sequestering agents such as aminopolyphosphonates, especially ethylenediaminetetramethylenephosphonic acid and diethylenetriaminepentamethylenephosphonic acid. Phosphate builders can also be used in the present invention.

Suitable builders are inorganic ion exchange materials, generally inorganic hydrated aluminosilicate materials, especially hydrated synthetic zeolites, such as hydrated zeolites A, X, B, HS or MA
P. Another suitable inorganic builder material is a laminated silicate, such as SKS-6 (
Hoechst). SKS-6 is a crystalline laminated silicate composed of sodium silicate (Na ₂ Si ₂ O ₅ ). Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid, and the like as disclosed in Belgian Patent Nos. 831,368, 821,369 and 821,370. Ether derivatives thereof. Polycarboxylates containing two carboxy groups include salts of succinic acid, malonic acid, (ethylenedioxy) diacetate, maleic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid, and German published patents. Gazette No. 2,44
6,686 and 2,446,687 and U.S. Patent 3,935,25
No. 7 and Belgian Patent 840,
No. 623, for example. Examples of the polycarboxylate containing three carboxy groups include water-soluble citrate,
Aconitate and citraconic acid salts and succinate derivatives such as carboxymethyloxysuccinate as described in GB 1,379,241 and lactoxis as described in Netherlands application 72050873 Succinate, and the 2-oxa-1 described in GB 1,387,447.
Oxypolycarboxylate materials such as 1,1,3-propanetricarboxylate.

As polycarboxylates containing four carboxy groups, British Patent No. 1
Oxydisuccinate, 1,1,2,2-ethanetetracarboxylate, 1,1,3,3-propanetetracarboxylate and 1,1,2,3-propanetetracarboxylate described in JP-A-261,829. Rates. Examples of the polycarboxylate containing a sulfo substituent include British Patent No. 1,398,421,
No. 1,398,422 and U.S. Pat. No. 3,936,448 as well as sulfosuccinate derivatives and heats of sulfonation as described in GB 1,082,179. Polycarboxylates containing phosphon substituents, while degraded citrates are mentioned, are disclosed in British Patent 1,439,000.

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
5,6-hexane-hexacarboxylate and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. As the aromatic polycarboxylate, British Patent No. 1,425,343
And the derivatives of melitic acid, pyromellitic acid and phthalic acid disclosed in US Pat. Among the above, preferred polycarboxylates are hydroxycarboxylates containing up to 3 carboxy groups per molecule, especially citrate.

Preferred builder systems for use in the compositions of the present invention include a mixture of a water-soluble carboxylate chelating agent, such as citric acid, and a water-insoluble aluminosilicate builder, such as zeolite A, or a laminated silicate (SKS-6). ). Other 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 detergent compositions of the present invention are soaps and polycarboxylates.

Other builder substances that may form part of the builder system for use in the particulate composition include inorganic substances such as alkali metal carbonates, bicarbonates, silicates, and organic substances such as organic Phosphonates, aminopolyalkylenephosphonates and aminopolycarboxylates are mentioned. Other suitable water-soluble organic salts are homo- or copolymeric acids or salts thereof, in which case the polycarboxylic acid contains at least two carboxyl groups separated from each other by no more than two carbon atoms. This type of polymer is known as GB-A-1,
No. 596,756. Examples of such salts have a molecular weight of 2000-5.
000 polyacrylates and their copolymers with maleic anhydride, for example copolymers having a molecular weight of 20,000 to 70,000, especially about 40,000. Detergent builder salts usually comprise 5% to 80%, preferably 10% by weight of the composition.
% By weight, most usually 30% to 60% by weight.

Chelating Agents The detergent compositions of the present invention may also optionally contain one or more iron and / or manganese chelating agents. Such chelators may 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 benefits of these materials are due, in part, to their exceptional ability to remove iron and manganese ions from the wash solution by the formation of soluble chelators. .

Aminocarboxylates useful as optional chelating agents include ethylenediaminetetraacetate, N-hydroxyethylethylenediaminetriacetate, nitrilotriacetate, ethylenediaminetetrapropionate, triethylenetetraamine hexaacetate, diethylenetriaminepentaacetate, and ethanol. Diglycine, its 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, provided that at least low levels of total phosphorus are found in the detergent composition;
Examples include ethylenediaminetetrakis (methylene phosphonate) such as DEQUEST. These aminophosphonates preferably do not contain alkyl or alkenyl groups having more than about 6 carbon atoms.

Polyfunctionally substituted aromatic chelators are also useful in the compositions of the present invention (see US Pat. No. 3,812,044, Conner et al., Issued May 21, 1974). A preferred compound of this type in the acid form is dihydroxydisulfobenzene, for example 1,2-dihydroxy-3,5-disulfobenzene. A preferred biodegradable chelating agent for use in the present invention is ethylenediaminedisuccinate ("EDDS"), particularly US Pat. No. 4,704,233 (Hartma).
n and Perkins, November 3, 1987). The compositions herein provide a water-soluble methyl glycine diacetate (MGDA) salt (or acid form) together with a chelating agent or an auxiliary that is useful with an insoluble builder such as, for example, a zeolite, a laminated silicate. May be included as a builder. When using these chelating agents, generally about 0.1% of the detergent composition of the present invention is used.
% By weight to about 15% by weight. More preferably, when used, the chelating agent contains from about 0.1% to about 3.0% by weight of such a composition.

Foam Inhibitors Another optional ingredient is a foam inhibitor, exemplified by silicones and silica-silicone mixtures. Silicones can generally be represented by alkylated polysiloxane materials, while silica is commonly used in finely divided form and is exemplified by silica airgels and xerogels, and various types of hydrophobic silica. These materials may be included as particles in which the suds suppressor is beneficially releasably included in a water-soluble or water-dispersible, substantially non-surfactant detergent-impermeable carrier. Alternatively, the suds suppressor may be dissolved or dispersed in a liquid carrier and applied by spraying on one or more other components. Preferred silicone foam control agents are disclosed in U.S. Pat. No. 3,933,672 (Bartol).
lota et al.). Other particularly useful foam control agents are described in German Patent Application D
It is a self-emulsifying silicone foam inhibitor described in TOS 2646126 (published on April 28, 1977). An example of such a compound is DC-544, commercially available from Dow Corning, which is a siloxane-glycol copolymer. Particularly preferred suds control agents are suds suppressor systems comprising mixtures of silicone oils and 2-alkyl-alkanols. A suitable 2-alkyl-alkanol is 2-butyl-octanol, which is commercially available under the trade name Isophor 12R. Such a suds suppressor system is disclosed in co-pending European Patent Application N9887904.
. 7 (filed on November 10, 1992). Particularly preferred silicone foam control agents are described in co-pending European Patent Application N9220.
1649.8. The composition can include a silicone / silica mixture in combination with a fumed non-porous silica, such as Aerosil®. Said suds suppressor is usually used at a concentration of 0.001% to 2%, preferably 0.01% to 1% by weight of the composition.

Other Constituents Other constituents used in the detergent composition include, for example, soil suspending agents, soil releasing agents, optical brighteners, abrasives, bactericides, anti-fogging agents, coloring agents and the like. And / or encapsulated or unencapsulated fragrances may 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 U.S. Patent No. 3,455,838. These acid-ester dextrins are preferably prepared from starches such as waxy corn, waxy sorghum, sago palm, tapioca and potato. Suitable examples of such encapsulation materials include National Sta
N-Lok manufactured by rch. The N-Lok encapsulant consists of denatured corn starch and glucose. Starch is modified by adding a monofunctional substituent, such as octenyl succinic anhydride.

Suitable antiredeposition and soil suspending agents for the present invention include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or copolymeric polycarboxylic acids or salts thereof. Such polymers include the polyacrylates and maleic anhydride-acrylic acid copolymers described above as builders, and copolymers of maleic anhydride with ethylene, methyl vinyl ether or methacrylic acid. Here, maleic anhydride makes up at least 20 mol% of the copolymer. These materials usually comprise 0.5% to 10%, more preferably 0.75% by weight of the composition.
It is used at a concentration of from 8% to 8%, most preferably from 1% to 6% by weight.

Preferred optical brighteners are anionic substances of a suitable nature, examples of which are disodium 4,4′-bis- (2-diethanolamino-4-anilino-s-triazine-6- Ilamino) stilbene-2: 2'disulfonate, disodium 4,4'-bis- (2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2: 2'-disulfonate, disodium 4 , 4'-Bis- (2,4-dianilino-s-triazin-6-ylamino) stilbene-2:
2 ′ disulfonate, monosodium 4 ′, 4 ″ -bis- (2,4-dianilino-s-triazin-6-ylamino) stilbene-2-sulfonate, disodium 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, disodium 4,
4'-bis- (2-anilino-4- (1-methyl-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene-2,2'disulfonate,
Sodium 2 (stilbill-4 "-(naphth-1 ', 2': 4,5) -1,2,2
3-Triazole-2 "-sulfonate and 4,4'-bis (2-sulfostyryl) biphenyl. Highly preferred brighteners are the specific brighteners disclosed in EP 755567.

[0189] Other useful polymeric substances are polyethylene glycols, especially those having a molecular weight of 100
0-10000, more preferably 2000-8000, most preferably about 40
00. They are used at a concentration of 0.20% to 5% by weight, more preferably 0.25% to 2.5% by weight. These polymers and the aforementioned homo- or copolymeric polycarboxylate salts, in the presence of transition metal impurities, improve whiteness retention, textile ash deposition, and cleaning performance on clay, protein and oxidative soils. It is useful to.

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 arrangements. Examples of such polymers are described in commonly assigned U.S. Pat.
No. 2033. Particularly preferred polymers according to EP-A-0272033 have the following formula:

Embedded image (Wherein, PEG is - (OC ₂ H ₄₎ a O-, PO is (OC ₃ H ₆ O), and T is _{(pcOC 6 H 4 CO))} .

Also very useful are modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propanediol, where the end groups are primarily sulfobenzoate, and secondary It consists of a monoester of glycol and / or propane-diol. The goal is to obtain a polymer capped at both ends with sulfobenzoate groups, and "primarily", in the context of the present invention, most of the copolymers mentioned herein above are capped by sulfobenzoate groups. However,
Some copolymers are not yet completely capped, so their end groups consist of monoesters of ethylene glycol and / or propane 1-2 diol, and are then "secondarily" composed of such species. obtain.

The polyester selected herein comprises about 46% by weight dimethyl terephthalic acid, about 16% by weight propane-1,2-diol, about 10% by weight ethylene glycol, about 13% by weight dimethyl It contains sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid and has a molecular weight of about 3000. Polyesters and their method of manufacture are described in detail in EPA 311342.

It is well known in the art that free chlorine in tap water rapidly inactivates enzymes included in detergent compositions. Thus, the use of chlorine scavengers such as perborate, ammonium sulfate, sodium sulfite or polyethyleneimine at levels greater than 0.1% by weight of the total composition in the formulation will improve the wash-through stability of detergent enzymes. Can be provided. Compositions containing chlorine scavengers are described in European Patent Application No. 928700.
No. 18.6 (filed on Jan. 31, 1992).

[0194] Alkoxylated polycarboxylates, such as those prepared from polyacrylates, are useful herein to provide additional fat removal. Such materials are described in WO 91/08281 and PCT 90/01815 (see page 4).
) (This description is included herein by reference). Chemically, these materials include polyacrylates having one ethoxy side chain for each 7-8 acrylate unit. The side chains have the formula _{- (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 with the polyacrylate "backbone" to provide a "comb" polymer type structure. Molecular weights can vary, but typically range from about 2000 to about 50,000. Such alkoxylated polycarboxylates may be present in the compositions herein at about 0.
It may comprise from 05% to about 10% by weight.

Dispersant The detergent composition of the present invention may also contain a dispersant. Suitable water-soluble organic salts are homo-
Or a copolymer acid or a salt thereof, wherein the polycarboxylic acid contains at least two carboxyl groups separated from each other by no more than two carbon atoms. Such polymers are disclosed in GB-A-1,596,756. Examples of such salts are polyacrylates having a molecular weight of 2000 to 5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of 1,000 to 1
It has a molecular weight of 00,000.

In particular, copolymers of acrylate and methyl acrylate, for example with a molecular weight of 40
480N of 00 may be added to the detergent composition of the present invention at a concentration of 0.5 to 20% by weight of the composition.

The compositions of the present invention may contain a lime soap peptiser compound, which is preferably, as described below, no more than 8, preferably no more than 7, most preferably no more than 6 It has the following lime soap dispersing power (LSDP). The lime soap peptizer compound is preferably present at a concentration of 0% to 20% by weight.

Numerical measurements of the effectiveness of lime soap peptizers are described in HC Borghetty and CA Bergman, J.
Lime soap dispersant power (LSDP) determined using the lime soap dispersant test as described in the editorial by Am. Oil. Chem. Soc., Volume 27, pages 88-90, (1950).
Is indicated by This lime soap dispersion test method is widely used by those skilled in the art, for example as mentioned in the following review article: WN Linfeld, Surfactant science S
eries, Volume 7, page 3; WN Linfield, Tenside surf. Det. volume 27, pa
ges 159-163, (1990); and MK Nagarajan, WF Masler, Cosmetics and Toile
tries, volume 104, pages 71-73, (1989). LSDP is 333 ppm CaC
With the weight percentage ratio of dispersant to sodium oleate required to disperse the lime soap precipitate formed by 0.025 g of sodium oleate in 30 ml of O ₃ (Ca: Mg = 3: 2) equivalent hardness water. is there.

Surfactants having good lime soap deflocculant capabilities include certain amine oxides,
Includes betaines, sulfobetaines, alkyl ethoxy sulfates and ethoxylated alcohols.

Exemplary surfactants having an LSDP of 8 or less for use in the invention include C ₁₆ -C ₁₈ dimethylamine oxide, C ₁₂ -C with an average degree of ethoxylation of 1-5.
Alkyl ethoxy sulfates C _18, in particular 3 alkyl ethoxy sulfate surfactant of C ₁₂ -C ₁₅ having a degree of ethoxylation (LSDP = 4), and 12 (
LSDP = 6) or include ethoxylated alcohols C ₁₄ -C ₁₅ having an average degree of ethoxylation of 30, sold by BASF GmbH under the trade name each Lutensol (Lutensol) A012 and Lutensol (Lutensol) A030.

Polymeric lime soap peptizers suitable for use herein are described in Cosmetics and Toil
MK Nagarajan, WF Ma found in etries, volume 104, pages 71-73 (1989).
It is described in an article by sler.

Hydrophobic bleaches such as 4- [N-octanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-nonanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-decanoyl-6 [Aminohexanoyl] benzenesulfonates and their mixtures, as well as nonanoyloxybenzenesulfonates, can also be used as lime soap peptizer compounds, along with hydrophilic / hydrophobic bleach formulations.

The Detergent Compositions of the Invention Inhibit Solubilization from One Fabric to Another and the Dyeing of Suspended Dyes Encountered During Knit Laundry Operations on Colored Knitted Fabrics May also be included.

Polymer Transfer Inhibitor The detergent composition of the present invention comprises 0.001% by weight to 10% by weight, preferably 0.01% by weight.
It also contains from 2% by weight to 2% by weight, more preferably from 0.05% by weight to 1% by weight of a polymeric migration inhibitor. Said polymeric dye transfer inhibitors are usually included in the cleaning composition to suppress dye transfer from the colored fabric to the fabric with which it has been washed.
These polymers have the ability to bind or adsorb fading dyes that have been washed off the dyed fabric before the dyes have a chance to adhere to others during washing. 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 polymers also enhances the performance of the enzymes of the present invention.

A) Polyamine N-Oxide Polymers Polyamine N-oxide polymers suitable for use contain units having the following structural formula:

Embedded image (Wherein P is a polymerizable unit to which an R-N-O group may be attached, or an R-N-O group forms part of the polymerizable unit, or both. Combination

[0206]

Embedded image x is 0 or 1, and R is an aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic group, or any combination thereof, to which the nitrogen of the NO group is attached. Get or N-
The nitrogen of the O group is part of these groups).

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

Embedded image Wherein R ₁ , R ₂ and R ₃ are an aliphatic group, aromatic, heterocyclic or alicyclic group, or a combination thereof, and x and / or y and / or z are 0 or 1 And
The nitrogen of the NO group can be attached or the nitrogen of the NO group forms part of these groups).

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

Other suitable polyamine N-oxides are those in which the N—O group is attached to a polymerizable unit. Preferred types of these polyamine N-oxides are those of the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group and the nitrogen of the NO functional group is Is a polyamine N-oxide. Examples of these types 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, wherein the nitrogen of the NO functional group is attached to the R group described above. Examples of these types are polyamine oxides in which the R groups can be aromatic, for example phenyl.

As long as the resulting amine oxide polymer is water-soluble and has dye transfer inhibiting properties,
Any polymer backbone can be used. Examples of suitable polymer backbones are polyvinyl, polyalkylene, polyester, polyether, polyamide, polyimide, polyacrylate and mixtures thereof.

The amine N-oxide polymers of the present invention typically have an amine to amine N-oxide ratio of from 10: 1 to 1: 1,000,000. However, the amount of amine oxide groups present in the polyamine oxide polymer can be adjusted by appropriate copolymerization.
Or it may vary depending on the appropriate degree of N oxidation. Preferably, the ratio of amine to amine N-oxide is from 2: 3 to 1: 1,000,000. More preferably, 1: 4-1.
: 1,000,000, most preferably from 1: 7 to 1: 1,000,000. The polymers of the present invention include, in fact, random or block copolymers in which one type of monomer is an amine N-oxide and the other type is or is not an amine N-oxide. The amine oxide units of the polyamine N-oxide have a PKa value such that PKa <10, preferably PKa <7, more preferably PKa <6. Polyamine oxides can obtain almost any degree of polymerization. The degree of polymerization is not important if the material has the desired water solubility and dye suspending power. Typically, the average molecular weight is between 500 and 1,000,000, preferably 1,000.
~ 50,000, more preferably in the range of 2,000-30,000, most preferably in the range of 3,000-20,000.

B) Copolymer of N-vinylpyrrolidone and N-vinylimidazole The N-vinylimidazole N-vinylpyrrolidone polymer used in the present invention is 5,000 to 1,000,000, preferably 5,000 to 200, It has an average molecular weight in the range of 000. A highly preferred polymer for use in the detergent composition of the present invention is an N-vinylimidazole N-vinylpyrrolidone copolymer, which is 5,000 to 50,000.
00, more preferably 8,000 to 30,000, most preferably 10,000.
A polymer selected from polymers having an average molecular weight in the range of 0 to 20,000. The average molecular weight range is based on Barth HG and Mays JW Chemical Analysis Vol 113,
Determined by light scattering as described in “Modern Methods of Polymer Characterization”. Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers are
It has an average molecular weight ranging from 5,000 to 50,000, more preferably from 8,000 to 30,000, and most preferably from 10,000 to 20,000.

N-vinylimidazole N- having the above average molecular weight range
While vinylpyrrolidone copolymers provide excellent dye transfer inhibition properties, they do not adversely affect the cleaning performance of detergent compositions formulated therewith. The N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has a 1 to 0.2, more preferably 0.8 to 0.3, most preferably 0.6 to 0.4 N
-Having a molar ratio of vinylimidazole to N-vinylpyrrolidone.

C) Polyvinylpyrrolidone The detergent composition of the present invention comprises from about 2,500 to about 400,000, preferably about 5,
000 to about 200,000, more preferably about 5,000 to about 50,000,
And most preferably, polyvinylpyrrolidone ("PVP") having an average molecular weight of about 5,000 to about 15,000 may also be utilized. Suitable polyvinylpyrrolidone are the product names PVP K-15 (viscosity molecular weight 10,000), PVP K-30 (average molecular weight 40,000), PVP K-60 (average molecular weight 160,000) and PVP K-90 (average molecular weight). Molecular weight 360,000) at ISP Corporation, New York,
Commercially available from NY and Montreal, Canada. Other suitable polyvinylpyrrolidones commercially available from BASF Cooperatio include Sokalan HP165 and Sokalan (Socalane) which are polyvinylpyrrolidones known to those skilled in the detergent art.
kalan) HP12 (eg EP-A-262,897 and EP-A
-256,696).

D) Polyvinyl oxazolidone: The detergent composition of the present invention may also utilize polyvinyl oxazolidone as a polymeric migration inhibitor. The polyvinyl oxazolidone is present in an amount from about 2,500 to about 400,000.
0, preferably about 5,000 to about 200,000, more preferably about 5,000
It has an average molecular weight from 0 to about 50,000, and most preferably from about 5,000 to about 15,000.

E) Polyvinylimidazole: The detergent compositions of the present invention may also utilize polyvinylimidazole as a polymeric dye transfer inhibitor. The polyvinyl imidazole is from about 2,500 to about 400,000;
Preferably from about 5,000 to about 200,000, more preferably from about 5,000 to
It has an average molecular weight of about 50,000, and most preferably from about 5,000 to about 15,000.

F) Crosslinked polymers: Crosslinked polymers are polymers whose backbones are interconnected to a certain extent. These bonds are of chemical or physical nature, probably due to active groups on the backbone or side chains. Crosslinked polymers are available from Journal of Polymer Science, volume 2
2, pages 1035-1039. In one embodiment, the crosslinked polymers are made such that they constitute a three-dimensional rigid structure, and are capable of confining the dye in the pores formed by the three-dimensional structure. In another embodiment, the cross-linked polymer confines the dye by swelling. Such crosslinked polymers are described in co-pending patent application 94870213.9.

Cleaning Methods The compositions of the present invention may be used in essentially any cleaning or cleaning method, including, for example, dipping, pre-treatment and rinsing to which a separate rinsing aid composition can be added. Methods involving steps are included.

The method described herein comprises the step of contacting a knitted fabric, tableware or any hard surface with a cleaning solution in a conventional manner as exemplified below. Conventional laundering methods include treating the soiled knitted fabric with an aqueous liquid that dissolves or disperses an effective amount of a laundry detergent and / or fabric care composition therein. A preferred mechanical dishwashing method involves treating the soil with an aqueous liquid having an effective amount of a mechanical dishwashing or rinsing composition dissolved or dispersed therein. A conventionally effective amount of a machine dishwashing composition is
Means 8 to 60 g of material dissolved or dispersed in a washing volume of 3 to 10 liters. According to the manual dishwashing method, an effective amount of the dishwashing composition, typically from 0.5 to 20 g (per 25 dishes to be treated), is brought into contact with the soiled dish. A preferred manual dishwashing method involves applying a concentrated solution to the surface of the dish or dipping into a large dilution of the detergent composition. Conventional hard surface methods involve the use of a soiled hard / surface in which an effective amount of a hard surface cleaner and / or an undiluted composition is dissolved or dispersed in an aqueous liquid, such as a sponge, brush, cloth. And so on. It also includes soaking the hard material with a concentrated solution or a large amount of a diluted solution of the detergent composition.

The cleaning method is preferably performed at 5 ° C. to 95 ° C., especially at 10 ° C. to 60 ° C. The pH of the treatment solution is preferably 7-12.

The following examples are intended to illustrate the compositions of the present invention and are not necessarily meant to limit or define the scope of the present invention.

In detergent compositions, enzyme concentration is expressed as pure enzyme relative to total composition weight, and unless otherwise specified, detergent components are expressed relative to total composition weight. Abbreviations used in the text have the following meanings:

LAS: straight chain C _11-13 sodium alkylbenzenesulfonate. TAS: tallow sodium alkyl sulfate. CxyAS: C _{1x to} C _1y sodium alkyl sulfate. CxySAS: Second (2,3) sodium alkyl sulfate C _1x -C _1y. MBAS: Mid-branched alkyl sulfate. CxyEz: a C _{1x to} C _1y predominantly linear primary alcohol condensed with an average of z moles of ethylene oxide. CxyEzS: C _1x ~C sodium alkyl sulfate _1y condensed with an average z moles of ethylene oxide. CxEOy: Cy alcohol with average degree of ethoxylation _y Nonionic: Mixed ethoxylated / propoxylated fatty alcohol, for example
Pluraf with an average ethoxylation degree of alcohol of 3.8 and an average propoxylation degree of 4.5
ac LF404. QAS: R _{2 ·} N ⁺ (CH ₃ ) ₂ (C ₂ H ₄ OH), where R ₂ = C ₁₂ -C ₁₄ . SADS: Formula 2-R. C4H7. -1,4- (SO4-) 2 (wherein R = C _10-18
C ₁₄ -C ₂₂ alkyl disodium sulfate)

MES: x-sulfomethyl ester of C18 fatty acid APA: _C8-10 amidopropyldimethylamine. Soap: sodium linear alkyl carboxylate obtained from an 80/20 mixture of tallow and coconut fatty acids. Neodol xy-z: C _{1x to} C _1y linear primary alcohol z ethoxylate. CFAA: alkyl N- methyl glucamide of C ₁₂ -C _14. TFAA: alkyl N- methyl glucamide of C ₁₆ -C _18. TPKFA: Toppudo total cleavage of _{C 12 ~C 14 (topped whole cut} ) fatty acids. DEQA: di- (tallow-oxy-ethyl) dimethylammonium chloride. DEQA (2): di- (soft tallowyloxyethyl) hydroxyethylmethylammonium methyl sulfate. DTDMAMS: ditallow dimethyl ammonium methyl sulfate. SDASA in a 1: 2 ratio of stearyl dimethylamine: triple presed (triple pres
sed) Stearic acid. Silicate: amorphous sodium silicate (ratio of SiO ₂ : Na ₂ O = 1.6-3.2: 1)
.

Metasilicate: sodium metasilicate (ratio of SiO ₂ : Na ₂ O = 1.0). Zeolite A: hydrated sodium aluminosilicate having a primary particle size of 0.1 to 10 μm (weight based on anhydride), formula Na ₁₂ (AlO ₂ SiO ₂ ) ₁₂ · 27
H ₂ O. (Na-) SKS-6: a crystalline layered silicate of formula δ-Na ₂ Si ₂ O ₅ . Citrate: trisodium citrate dihydrate. Citric acid: citric anhydride. Borate: sodium borate. Carbonate: anhydrous sodium carbonate. Bicarbonate: anhydrous sodium bicarbonate. Sulfate: anhydrous sodium sulfate. STPP: sodium tripolyphosphate. TSPP: tetrasodium pyrophosphate. MA / AA: 4: 1 acrylate having an average molecular weight of about 70,000 to 80,000 /
Maleate random copolymer. MA / AA1: a random copolymer of 6: 4 acrylate / maleate with an average molecular weight of about 10,000. AA: sodium polyacrylate polymer having an average molecular weight of about 4,500.

Polycarboxylate: a copolymer of acrylic acid with a molecular weight of 4,500, BAS
Copolymers consisting of a mixture of carboxylate monomers, such as acrylates, maleates and methyl acrylates, with molecular weights ranging from 2,000 to 80,000, such as Sokolan, commercially available from F. PB1: anhydrous sodium perborate monohydrate. PB4: sodium perborate tetrahydrate of nominal formula NaBO ₃ .4H ₂ O. Percarbonate: anhydrous sodium percarbonate with a nominal formula of 2.74 Na ₂ CO ₃ .3H ₂ O ₂ . NaDCC: sodium dichloroisocyanurate. TAED: tetraacetylethylenediamine. NOBS: Nonanoyloxybenzenesulfonate in the form of its sodium salt. NACA-OBS: (6-nonamidocaproyl) oxybenzenesulfonate.

DOBS: sodium salt of decanoyloxybenzenesulfonate. DTPA: diethylenetriaminepentaacetic acid. HEDP: 1,1-hydroxyethanediphosphonic acid. DETPMP: diethyltriaminepenta (methylene) phosphonate, sold by Monsanto under the trade name Dequest 2060. EDDS: Sodium salt form of the (S, S) isomer ethylenediamine-N, N '
-Disuccinic acid. Chelating agent: a chelating agent selected from EEDS, HEDP, DTPA, DETPMP and / or a mixture thereof. MnTACN: manganese 1,4,7-trimethyl-1,4,7-triazacyclononane. Light activated bleach: sulfonated zinc phthalocyanine encapsulated in a dextrin soluble polymer. Light activated bleach 1: sulfonated aluminophthalocyanine encapsulated in dextrin soluble polymer. PAAC: pentaamine acetate cobalt (III) salt. Paraffin: Paraffin oil sold by Wintershall under the name Winog 70.

NaBz: sodium benzoate. Pectate lyase: pectate lyase from Bacillus agaradhaerens, NCIMB 404482 or DSM8721. Xyloglucanase: E described in WO98 / 50513 and WO94 / 14953.
Xyloglucan-specific endoglucanase mannanase described as GII: Mannanase from Bacillus agardhaerens, NCIMB 40482. Proteases: Savinase, Alcalase, Durazyme
Proteolytic enzymes sold by Novo Nordisk A / S under the trade name (Durazyme), Maxacal, Gist-Brocades under the trade name Maxapem, and patents WO 91/06637 and / or WO 95 / No. 10591 and / or the proteases described in EP 251446. Amylase: described in WO 94/18314, WO 96/05295 and under the trade name Purafact Ox AM® by Genencor, WO
Novo under the tradenames Termamyl (registered trademark), Fungamyl (registered trademark) and Duramyl (registered trademark) described in US Patent No. 95/26397.
An amylolytic enzyme sold by Nordisk A / S.

Lipases: Novo Nordisk A / S under the trade name Lipolase, Lipolase Ultra and Gist-Broc under the trade name Lipomax
A lipolytic enzyme sold by ades. Cellulase: Cellulolytic enzyme sold by Novo Nordisk A / S under the trade name of Carezyme, Celluzyme and / or Endolase. Pectin lyase: Pectin lyase produced by Bacillus licheniformis, ATCC 14580. CMC: sodium carboxymethyl cellulose. PVNO: polyvinyl pyridine-N-oxide having an average molecular weight of 50,000. PVPVI: a copolymer of vinylimidazole and vinylpyrrolidone with an average molecular weight of 20,000. Brightener 1: 4,4'-bis (2-sulfostyryl) biphenyl disodium. Brightener 2: 4,4'-bis (4-anilino-6-morpholino-1.3.5-triazin-2-yl) stilbene-2: 2'-disodium disulfonate. Silicone defoamer: a polydimethylsiloxane foam control agent containing a siloxaneoxyalkylene copolymer as a dispersant and having a foam control agent to dispersant ratio of 10: 1 to 100: 1. Foaming inhibitor: 12% silicone / silica, 18% stearyl alcohol, 70%
Starch (granular form).

Opacifier: Aqueous monostyrene latex mixture (sold by BASF Aktiengesellschaft under the trade name Lytron 621). Thickener: high molecular weight crosslinked polyacrylate such as Carbopol from BFGoodrich Chemical Company and Polygel 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 ( where, n = 20~30). SCS: sodium cumene sulfonate. HMWPEO: high molecular weight polyethylene oxide. PEGx: polyethylene glycol of molecular weight x. PEO: polyethylene oxide having an average molecular weight of 5,000. TEPAE: tetraethylene pentaamine ethoxylate. BTA: benzotriazole. pH: Measured as a 1% solution in distilled water at 20 ° C.

[0231]

【Example】

 Example 1 The following high density, bleach-containing, laundry detergent composition was prepared according to the present invention.

[Table 5]

[Table 6]

Example 2 The following particulate or tablet laundry composition was prepared according to the present invention.

[Table 7]

[Table 8]

Example 3 The following high density laundry detergent composition was prepared in accordance with the present invention.

[Table 9]

[Table 10]

Example 4 The following particulate or tablet laundry composition was prepared in accordance with the present invention.

[Table 11]

[Table 12]

Example 5 The following high density laundry detergent composition was prepared according to the present invention.

[Table 13]

[Table 14]

Example 6 The following particulate detergent was prepared according to the present invention.

[Table 15]

[Table 16]

Example 7 The following laundry detergent composition was prepared according to the present invention.

[Table 17]

[Table 18]

Example 8 The following laundry detergent composition was prepared according to the present invention.

[Table 19]

[Table 20]

Example 9 The following liquid detergent composition was prepared according to the present invention (concentrations are given in parts by weight, the enzyme is expressed as pure enzyme).

[Table 21]

Example 10 The following liquid detergent composition was prepared according to the present invention (concentrations are given in parts by weight, the enzyme is expressed as pure enzyme).

[Table 22]

[Table 23]

Example 11 The following liquid detergent composition was prepared according to the present invention (concentrations are given in parts by weight, the enzyme is expressed as pure enzyme).

[Table 24]

Example 12 A particulate knitted fabric detergent composition providing the following "softening by washing" ability was prepared according to the present invention (concentrations are given in parts by weight, enzymes are expressed as pure enzymes).

[Table 25]

Example 13 The following rinsed knitted fabric softener composition was prepared in accordance with the present invention.

[Table 26]

Example 14 The following knitted fabric softener and dry-added knitted fabric conditioner composition was prepared in accordance with the present invention.

[Table 27]

Example 15 The following laundry bar detergent composition was prepared according to the present invention (concentrations are given in parts by weight, the enzyme is expressed as pure enzyme).

[Table 28]

Example 16 The following compact high density (0.96 Kg / l) dishwashing detergent composition was prepared according to the present invention.

[Table 29]

Example 17 The following particulate dishwashing detergent composition having a bulk density of 1.02 Kg / L was prepared according to the present invention.

[Table 30]

Example 18 A particulate dishwashing detergent composition was prepared using a standard 12-head rotary press using a 13-head rotary press.
The following tablet detergent composition was prepared according to the present invention by compressing at a pressure of KN / cm ² .

[Table 31]

Example 19 The following automatic dishwashing tablet was prepared according to the present invention (raw material is expressed in g and enzyme is expressed as pure enzyme).

[Table 32]

Tablet compositions I and II were prepared as follows. A Phase 1 cleaning active composition was prepared by mixing the particulate and liquid components and passing them through a conventional rotary press die. The press includes a suitably shaped punch that forms the mold. The cross section of the die is about 30 × 38 mm. Subjecting the composition to a compression force of 940 kg / cm ² ,
The punch is raised and the upper surface exposes the first layer of tablets contained in the mold. A phase 2 cleaning active composition was similarly prepared and passed through a die. 170 kg of particulate active composition
/ Cm ² , the punch was lifted, and multiple layers of tablets were removed from the tablet press. The tablets obtained dissolve or disintegrate in the washing machine described above within 12 minutes and the phase 2 tablets dissolve within 5 minutes. Tablets, with their excellent dissolution properties,
It shows improved strength on long term storage.

Tablet composition III was prepared as follows: The active cleaning composition was fed into the punch cavity of a modified rotary tablet press, and the compressed portion was compressed by compressing the composition at a pressure of 940 Kg / cm ^2. Prepare. Improved tablet presses provide tablets whose compressed parts have pores. For the purpose of Example III, the uncompressed portion is in particulate form. The non-compressed part is actually supplied to the holes of the compressed part using a nozzle feeder. The uncompressed portion is adhered to the compressed portion by coating the uncompressed portion on a coating layer that contacts the compressed portion.

Example 20 The following liquid dishwashing composition having a density of 1.40 Kg / L was prepared according to the present invention.

[Table 33]

Example 21 The following liquid rinse aid composition was prepared in accordance with the present invention.

[Table 34]

Example 22 The following manual liquid dishwashing composition was prepared in accordance with the present invention.

[Table 35]

Example 23 The following liquid hard surface cleaning composition was prepared according to the present invention.

[Table 36] * Na4 ethylenediamine diacetic acid ** diethylene glycol monohexyl ether

Example 24 The following spray composition for cleaning hard surfaces and removing domestic mold was prepared according to the present invention.

[Table 37] * Diethylene glycol monobutyl ether

Example 25 The following disinfecting composition was prepared according to the present invention.

[Table 38]

──────────────────────────────────────────────────続 き Continued on the front page (51) Int.Cl. ⁷ Identification symbol FI Theme court ゛ (Reference) D06L 3/11 D06L 3/11 (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, TZ, 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, CR, CU, CZ, DE, DK, D , 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, MA, MD, MG, MK, MN, MW, MX, NO, NZ, PL, PT, RO, RU, SD, SE, SG, SI, SK, SL, TJ, TM, TR TT, TZ, UA, UG, US, UZ, VN, YU, ZA, ZW (72) Inventor Schewell, Michael Stanford Compton, Lord, Cincinnati, Ohio, USA 685 (72) Inventor Jew, Jong, Ohio, United States of America State, Cincinnati, Bromyard, Avenue 4348 (72) Inventor Wells, Eric Sea Ohio, Cincinnati, AW, Kemper, Road, Number 1601 1440 (72) Inventor Moses, Rosa Laura, Ohio, United States, West, Chester, Eagle, Creek, Court 8815 (72) Inventor Bettyol, Jean-Luc Philippe Belgium 1200, Brussels, Avigne, Slejour 93 (72) Inventor Bush, Alfred Belgium 1840, Rondersere, Handelsstraat 210 (72) Inventor Shoichi Yoshikawa 3-6-23 Sumiyoshinomiyacho, Higashinada-ku, Kobe-shi, Hyogo (72) Inventor Behiman, Georg Belgium 1970, Wezembek-Oppem, Clossan, Georg 5F term (reference) 4H003 AB19 AB27 AC08 AE06 DA01 DA05 DA17 DA19 EA09 EA12 EA15 EA20 EA27 EA28 EB08 EB12 EB19 EB22 EB24 EB32 FA04 EB36 EB37 EB37 FA04

Claims (8)

[Claims] 1. A detergent composition comprising a detergent component, a mannanase enzyme, a pectate lyase enzyme and a xyloglucanase enzyme. 2. The concentration of the pure enzyme, wherein the mannanase is present in an amount of 0.0001 to 2%, preferably 0.0005 to 0.5%, more preferably 0.001 to 0.02% by weight of the total composition. The detergent composition according to claim 1, which is present in the composition. 3. The pectate lyase comprises 0.0001 to 2% by weight of the total composition, preferably 0.0005 to 0.5% by weight, more preferably 0.001 to 0.5%.
3. A detergent composition according to claim 1 or 2 which is present at a concentration of 1% by weight of pure enzyme. 4. The xyloglucanase comprises 0.0001 to 2% by weight of the total composition, preferably 0.0005 to 0.5% by weight, more preferably 0.001 to 0.
4. The detergent composition according to claim 1, which is present in a concentration of 1% by weight of pure enzyme. 5. The weight ratio of pure enzyme of mannanase: pectate lyase: xyloglucanase is from 10: 1: 1 to 1: 10: 1 to 1: 1: 10, preferably 5
Detergent composition according to claims 1 to 4, being present in a ratio of 1: 1 to 1: 5: 1 to 1: 1: 5, more preferably 1: 1: 1. 6. The detergent composition according to claim 1, wherein the detergent component is selected from an anionic, nonionic, cationic surfactant and / or a mixture thereof. 7. The detergent composition according to claim 1, wherein said detergent component is a bleaching agent, preferably a bleaching activator bleaching system. 8. The detergent composition according to claim 1, wherein the detergent component is a builder, preferably a builder selected from zeolite A, layered sodium silicate, sodium tripolyphosphate and / or a mixture thereof.