CN1276005A - Detergent compositions comprising mannase and clay - Google Patents

Detergent compositions comprising mannase and clay Download PDF

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Publication number
CN1276005A
CN1276005A CN98810218A CN98810218A CN1276005A CN 1276005 A CN1276005 A CN 1276005A CN 98810218 A CN98810218 A CN 98810218A CN 98810218 A CN98810218 A CN 98810218A CN 1276005 A CN1276005 A CN 1276005A
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Prior art keywords
mannanase
laundry detergent
fabric care
enzyme
alkyl
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J·-L·P·贝蒂奥尔
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Procter and Gamble Co
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Procter and Gamble Co
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    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/39—Organic or inorganic per-compounds
    • C11D3/3942—Inorganic per-compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/38—Cationic compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/0005—Other compounding ingredients characterised by their effect
    • C11D3/0036—Soil deposition preventing compositions; Antiredeposition agents
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3723—Polyamines or polyalkyleneimines
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38609—Protease or amylase in solid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • C11D2111/12—

Abstract

The present invention relates to laundry detergent compositions, comprising a saccharide gum degrading enzyme providing excellent cleaning performance, especially food stain/soil removal, dingy cleaning and whiteness benefits.

Description

Detergent compositions comprising mannanase and clay
Technical Field
The present invention relates to laundry detergent and/or fabric care compositions comprising a mannanase enzyme and a clay.
Background
The performance of a detergent product is judged by a number of factors, including detergency and the ability to prevent redeposition of soil or the breakdown products of the soil onto the articles in the wash. Thus, current detergent compositions comprise a complex combination of active ingredients that meet certain specific needs. In particular, current detergent formulations typically include surfactants and detergent enzymes to provide cleaning and fabric care benefits. Furthermore, the need for detergent compositions which exhibit not only good cleaning properties but also fabric softening performance and other fabric care benefits has been well established in the prior art.
Softening clays are commonly used in current laundry detergent and fabric care compositions to provide a soft feel. In EP-A-177165, the use of softening clays and cellulases in detergent compositions is disclosed. EP-A-495258 describes detergent compositions comprising ｃA surfactant, ｃA builder system, ｃA softening clay and ｃA cellulase.
Food and cosmetic stains/soils represent the majority of consumer-related stains/soils and typically contain food additives such as thickeners/stabilizers. Indeed, hydrocolloid gums and emulsifiers are commonly used as food additives. The term "gums" refers to a group of industrially used polysaccharides (long chain polymers) or their derivatives that hydrate in hot or cold water to form viscous solutions, dispersions or gels. Gums are classified as natural and modified. The natural gums include seaweed extracts, plant extracts, gums derived from seeds or roots, and gums derived from microbial fermentation. Modified (semi-synthetic) Gums include cellulose and starch derivatives and certain synthetic Gums such as lower methoxy pectin, propylene glycol alginate, and carboxymethyl and hydroxypropyl guar (gum in Encyclopedia of Chemical Technology) volume 4th Ed.12, page 842-862, J.Baird, Kelco division of Merck). See also carbohydrate Chemistry in food science (carbohydrate Chemistry for food Scientists) (eagon Press-1997), R.L.Whistler and J.N.BeMiller, Chapter 4, pages 63-89 and direct food Additives in Fruit Processing (direct food Additives in front Processing), P.Laslo, Bioprincolled Applications, volume 1, Chapter II, page 313-325 (1996) Tech noomicublishing. These gum fractions, such as guar gum (E412), carob gum (E410), alone or in combination, are widely used in food applications (Gums in ECT 4th Ed. Vol.12, pp.842-.
Guar Gum used in these Food and cosmetic stains is obtained from the seed endosperm of the legume cyamopsistragonoloba plant guar Gum (also known as guar) extracted from dicotyledonous seeds consists of a 1-4, b-D-mannopyranosyl unit backbone, is used as a thickener in seasonings and frozen products and cosmetics (h. -D. beitz, Food Chemistry, page 243, second edition english text, Springer-verag, 1987, ISBN 0-387 & (US)) (Carbohydrate Chemistry for Food Scientists, r.l. wilstler, eagan Press, 1977, ISBN 0-913250-92-9) & (Industrial Gum, second edition, r.l. ist 308, Aca microbial Press, 1973, ISBN 0-913250-92-9) & (normal Gum, second edition, r.l. ist 308, Aca dietary Press, 1973, ISBN, 0-12-6274-74-9) in the case that the side chain of guar Gum is different from galactose in the plant mannan domain, also known as guar Gum having a galactose residue in the case where no more than galactose oligosaccharide residue, the guar Gum is used in the plant mannan domain, and the plant mannan domain, also known as a galactomannan-20, or a galactomannan domain, which has no more than galactose residue in the case where no pectin residue is used in the plant mannan domain.
However, clays are not compatible with certain hydrocolloid gums contained in these food and cosmetic stains. It is recognized in the prior art that guar Gum causes precipitation of clay due to its potential to coagulate mud or clay particles (see Industrial Gum, 2 nd edition, r.l. whistler, p.307, Academic Press, 1973, ISBN, 0-12-74-6252-x).
It is therefore an object of the present invention to provide laundry detergent and/or fabric care compositions which exhibit optimum softening performance and provide optimum stain removal and cleaning performance, especially on cosmetic and food stains.
The above objects can be met by formulating laundry detergent and/or fabric care compositions comprising a mannanase enzyme and a clay for use as a softening agent.
We have also found that the performance of the detergent compositions of the present invention is improved by the addition of a laundry detergent and/or fabric care ingredient selected from builders, cellulases and/or cationic surfactants.
Mannanases have been identified in several Bacillus organisms, e.g.Appl. environ. Microbiol., Vol.56, No.11, 3505-3510 (1990) describe a β -mannanase in the form of a dimer obtained from Bacillus stearothermophilus, which has a molecular weight of 162kDa and an optimum pH of 5.5-7.5, WorldJ.Micobio Boitech.of Mendoza et al, Vol.10, No.5, 551-555(1994) describes a MW of 38kDa obtained from Bacillus subtilis, a β -mannanase with an optimum activity of 37 kDa, determined by the gel filtration method, of pH5.0/55 ℃ and pl 4.8. 030J 4706 discloses a mannanase obtained from Bacillus, which has a MW of 37+/-3kDa, an optimum pH of 8-10 and pl 5.3-5.4, a mannanase of 37 kDa, a pH of 8-6389, and a alkaline mannanase preparation temperature for the alkaline hydrolysis of mannanase enzymes from alkaline mannanase enzymes of starch produced by the strain of Bacillus subtilis, e.g.12, WO 6789, WO 48,89, WO 48,46,89, a mannanase from Bacillus stearothermophilus, a mannanase, which has been described in the alkaline hydrolysis of alkaline xylanase, a strain produced by the alkaline hydrolysis of alkaline strain of alkaline cellulose, which is described in the alkaline cellulose, which is used for the preparation of alkaline cellulose, or for the alkaline hydrolysis of alkaline cellulose, which is described in the alkaline cellulose, for the alkaline hydrolysis of alkaline cellulose, for the preparation of alkaline cellulose, for the degradation of alkaline cellulose, for the preparation of alkaline cellulose, for the alkaline hydrolysis of the alkaline cellulose, for the alkaline hydrolysis of the.
However, to date, there has been no recognition of a synergistic combination of mannanase and clay in laundry detergent and/or fabric care compositions to provide optimum softening performance and optimum stain removal and cleaning performance, especially on cosmetic and food stains.
Summary of The Invention
The present invention relates to laundry detergent and/or fabric care compositions, especially for cosmetic and food stains, comprising a mannanase enzyme and clay to provide optimum softening performance and optimum stain removal and cleaning performance.
Detailed description of the invention
It is known in the prior art that clays are not compatible with certain hydrocolloid gums contained in, for example, food and cosmetic stains. It has been recognized that guar Gum causes precipitation of clay due to its potential to coagulate mud or clay particles (see Industrial Gum, 2 nd edition, r.l. whistler, p.307, Academic Press, 1973, ISBN, 0-12-74-6252-x).
While not intending to be bound by theory, we believe that the flocculated clay has a reduced softening effect. Furthermore, we have observed that clay and wash-load soils redeposit on guar gum residues, forming stains. We have surprisingly found that mannanases hydrolyse hydrocolloid gums, in particular guar gum. This enzymatic hydrolysis process results in the absence of guar gum in the wash. Thus, without clay flocculation, the clay retains its full fabric care potential. Furthermore, there is no residual guar gum residue on the fabric and therefore no re-deposition of clay and stains in the subsequent wash load and thus no stain formation. Mannanase
An essential component of the laundry detergent and/or fabric care compositions of the invention is a mannanase enzyme.
Included in the present invention are three mannose-degrading enzymes EC3.2.1.25: β -mannosidase, EC3.2.1.78: endo-1, 4- β -mannosidase, hereinafter referred to as "mannanase" and EC3.2.1.100: 1, 4- β -mannobiosidase (IUPAC classification-enzyme nomenclature 1992 ISBN 0-12-227165-3 Academic Press).
The laundry detergent and/or fabric care compositions of the invention more preferably contain β -1, 4-mannosidase (e.c.3.2.1.78) known as mannanase the term "mannanase" or "galactomannanase" denotes an officially defined mannanase according to the prior art, which is known as endo-mannanase 1, 4- β -mannosidase and is additionally known as β -mannanase and endo-1, 4-mannanase and catalyzes the random hydrolysis of the 1, 4- β -D-mannoside bonds in mannans, galactomannans, glucomannans and galactoglucomannans.
Mannanases (EC 3.2.1.78) constitute in particular a group of polysaccharidases, which degrade mannans, meaning enzymes capable of cleaving polysaccharide chains containing mannose units, i.e. enzymes capable of cleaving glycosidic bonds in mannans, galactomannans, glucomannans and galactoglucomannans, mannans being polysaccharides having a backbone consisting of β -1, 4-linked mannose, glucomannans being polysaccharides having a backbone of β -1, 4-linked mannose and glucose, which are more or less regularly alternating, galactomannans and galactoglucomannans being mannans and glucomannans with α -1, 6-linked galactose side chains, these compounds being acetylated.
In addition, the degradation of acetylated mannans, glucomannans, galactomannans and galactoglucomannans is facilitated by complete or partial deacetylation, acetyl groups can be removed by base or mannan acetyl esterase, oligomers released by a mixture of mannanases or mannanases and α -galactosidase and/or mannan acetyl esterase can be further degraded to release free maltose by β -mannosidase and/or β -glucosidase.
Mannanases have been identified in several Bacillus organisms, for example, Talbot et al, appl.Environ.Microbiol., Vol.56, No.11, 3505-3510 (1990) describe β -mannanase in the form of a dimer obtained from Bacillus stearothermophilus, which has a molecular weight of 162kDa and an optimum pH of 5.5-7.5, Mendoza et al, WorldJ.Microbiol.Biotech., Vol.10, No.5, 551-555(1994) describes a MW of 38kDa obtained from Bacillus subtilis, an optimum activity of β -mannanase at pH5.0/55 ℃ and pl 4.8. JP-0304706 discloses a mannanase from Bacillus having a MW of 38kDa determined by gel filtration, an optimum pH of 8-10 and a pH of 5.3-5.4 obtained by alkaline mannanase preparation of alkaline mannanase, a pH of 8-10 and a pH of 5.3-5.4, a pH of alkaline mannanase prepared by hydrolyzing a mannanase in alkaline mannanase, such as alkaline mannanase from Bacillus subtilis, a xylanase obtainable by hydrolyzing a strain of cellulose, such as described in alkaline mannanase from alkaline mannanase, alkaline mannanase from Bacillus subtilis, a strain, a xylanase, a.
The mannanase is especially an alkaline mannanase as defined below, most preferably a mannanase obtained from a bacterial source. The laundry detergent compositions of the invention especially comprise an alkaline mannanase selected from the mannanase obtainable from strain Bacillus agaradherens and/or Bacillus subtilis strain 168, gene yght.
The term "alkaline mannanase" refers to an enzyme comprising at least 10%, preferably at least 25%, more preferably at least 40% of its enzymatic activity with its maximum activity in a given pH range of 7-12, preferably 7.5-10.5.
Most preferably the laundry detergent and/or fabric care compositions of the invention comprise an alkaline mannanase enzyme obtainable from Bacillus agaradherens. The mannanase is: i) a polypeptide prepared from Bacillus agaradherens, NCIMB40482, or ii) a polypeptide comprising the amino acid sequence set forth in SEQ ID NO: 2 or iii) an analogue of a polypeptide as defined in i) or ii) which is at least 70% homologous to said polypeptide or is derived from said polypeptide by substitution, deletion or addition of one or several amino acids or is immunoreactive with a polyclonal antibody in pure form raised against said polypeptide.
The invention also includes an isolated polypeptide having mannanase activity, selected from the group consisting of: (a) a polynucleotide molecule encoding a polypeptide having mannanase activity and comprising the amino acid sequence set forth in seq id NO: 1 by nucleotide 97 to nucleotide 1029; (b) (ii) a species homolog of (a); (c) a polynucleotide molecule encoding a polypeptide having mannanase activity, substantially as shown in SEQ ID NO: 2 by amino acid residue 32 to amino acid residue 343 is at least 70% identical; (d) a molecule complementary to (a), (b) or (c); and (e) a degenerate nucleotide sequence of (a), (b), (c) or (d).
Plasmid pSJ1678, which contains a polynucleotide molecule (DNA sequence) encoding a mannanase enzyme according to the invention, was transformed into a strain of E.coli deposited by the inventors under the Budapest Treaty on the International Recognition of the microbial Deposit of the Patent program (Budapest treat on the International Recognition of the deposite of Microorganismsfor the microorganisms of the Patent Producer) at the Deutsche Sammlung von Mikroorganismen und Zellkul tur GmbH, Mascherder Weg lb, D-38124 Braunschweig, Federal Republic of Germany on 18 th 1998 with the Deposit number DSM 12180.
The second most preferred enzyme is a mannanase from bacillus subtilis strain 168, which mannanase: i) encoded by the DNA sequence shown in SEQ ID No.5 or a coding part of an analogue of said sequence and/or ii) a DNA sequence comprising the sequence shown in SEQ ID NO: 6 or iii) an analogue of a polypeptide as defined in ii), which is at least 70% homologous to said polypeptide, or is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunoreactive with a polyclonal antibody in purified form raised against said polypeptide.
The invention also includes an isolated polypeptide having mannanase activity, selected from the group consisting of: (a) a polynucleotide molecule encoding a polypeptide having mannanase activity and comprising the amino acid sequence set forth in SEQ ID NO: 5; (b) (ii) a species homolog of (a); (c) a polynucleotide molecule encoding a polypeptide having mannanase activity, substantially as shown in SEQ ID NO: 6, a polypeptide which is at least 70% identical in amino acid sequence; (d) a molecule complementary to (a), (b) or (c); and (e) a degenerate nucleotide sequence of (a), (b), (c) or (d). Definition of
Before discussing the present invention in further detail, the following terms are first defined:
the term "ortholog" (or "species homolog") refers to a polypeptide or protein obtained from a species that has homology to similar polypeptides or proteins from different species.
The term "paralog" denotes a polypeptide or protein obtained from a given species that has homology to a different polypeptide or protein from the same species.
The term "expression vector" means a linear or circular DNA molecule containing a segment encoding a polypeptide of interest operably linked to additional segments that provide for its transcription. Such additional segments may include promoter and terminator sequences, optionally including one or more origins of replication, one or more selectable markers, enhancers, polyadenylation signals, and the like. Expression vectors are typically derived from plasmid or viral DNA, or may contain both parts. The expression vector of the present invention may be any expression vector which may conveniently be subjected to recombinant DNA procedures, the choice of vector generally depending on the host cell into which the vector is to be introduced. Thus, the vector may be an autonomously replicating vector, i.e., a vector which exists as an extra chromosomal entity, the replication of which is independent of chromosomal replication, e.g., a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the host cell genome and replicated together with the chromosome(s) into which it has been integrated.
The terms "recombinant expression" or "recombinantly expressed" as used in connection with the expression of a polypeptide or protein in the present invention are defined according to the standard definitions of the prior art. Recombinant expression of proteins is generally carried out by using the above-mentioned expression vectors.
The term "isolated" when used with respect to a polynucleotide molecule means that the polynucleotide has been removed from its native genetic environment, and thus has no other extraneous or unwanted coding sequences, in a form suitable for use in a genetically engineered protein production system. The isolated molecules are materials isolated from their natural environment, including cDNA and genomic clones. The isolated DNA molecules of the invention are free of other genes with which they are normally associated, but may include naturally occurring 5 'and 3' untranslated regions, such as promoters and terminators. The identification of the association region will be apparent to those of ordinary skill in the art (see, e.g., Dynan and Tijan, Nature 316: 774-78, 1985).
Furthermore, the term "isolated polynucleotide" may be referred to as "cloned polynucleotide". The term "isolated" when used with respect to a protein/polypeptide refers to a protein that is found under conditions other than its native environment. In a preferred form, the isolated protein is substantially free of other proteins, particularly other homologous proteins (i.e., "homologous impurities" (see below)). Preferably, the protein is provided in greater than 40% pure form, more preferably greater than 60% pure form. More preferably, the protein is preferably provided in highly pure form, i.e., greater than 80% pure, more preferably greater than 95% pure, and most preferably greater than 99% pure as determined by SDS-PAGE.
Furthermore, the term "isolated protein/polypeptide" may be referred to as "purified protein/polypeptide".
The term "homologous impurities" denotes any impurities (e.g. other polypeptides than the polypeptide of the invention) which are produced by the homologous cell from which the polypeptide of the invention was originally obtained. The term "derived from … …" as used herein with respect to a particular microbial source refers to polynucleotides and/or polypeptides made from the particular source or from cells into which genes from the source have been inserted.
The term "operably linked" when referring to DNA segments means that the segments are arranged such that they function in concert for their intended purposes, e.g., transcription begins from a promoter and proceeds through the encoded segment to a terminator.
The term "polynucleotide" means a single-or double-stranded polymer of deoxyribonucleotide or ribonucleotide bases read from the 5 'to the 3' end. Polynucleotides include RNA and DNA, and may be isolated from natural sources, synthesized in vitro, or prepared from a combination of natural and synthetic molecules.
The term "complementary of a polynucleotide molecule" refers to a polynucleotide molecule having a complementary base sequence and reverse orientation as compared to a reference sequence. For example, the sequence 5 'ATGCACGGG 3' is complementary to 5 'CCCGTGCAT 3'.
The term "degenerate nucleotide sequence" means a nucleotide sequence that includes one or more degenerate codons (as compared to a reference polynucleotide molecule encoding a polypeptide). Degenerate codons contain different triplets of nucleotides, but encode the same amino acid residue (i.e., GAU and GAC triplets each encode Asp).
The term "promoter" denotes a portion of a gene containing a DNA sequence that provides for the binding of RNA polymerase and initiation of transcription. Promoter sequences are typically, but not always, found in the 5' non-coding region of a gene.
The term "secretory signal sequence" refers to a DNA sequence that encodes a polypeptide ("secreted polypeptide") as a component of a larger polypeptide, which is directed through the secretory pathway of the cell in which the larger polypeptide is synthesized. Larger polypeptides are typically cleaved to remove the secretory peptide when transported through the secretory pathway. How to use the sequences of the invention to obtain other related sequences:
the sequence information disclosed herein relating to the polynucleotide sequences encoding the mannanase enzymes of the invention can be used as a means to identify other homologous mannanase enzymes. For example, Polymerase Chain Reaction (PCR) can be used to amplify sequences encoding other homologous mannanases from various microbial sources, particularly microbial sources of different Bacillus species. Assays for Activity assays
Polypeptides having mannanase activity may be tested for mannanase activity according to standard test methods known in the art, e.g.by applying the solution tested to 4mm diameter wells punched out on agar plates containing 0.2% AZCL galactomannan (carob bean gum), i.e.a substrate for endo-1, 4- β -D-mannanase analysis obtained as Cat No.1-AZGMA per 3g US $110.00 by the company Megazyme (Internet address of Megazyme: http:// www.megazyme.com/Purchase/index).
An isolated polynucleotide of the invention will hybridize to a region of similar size of seq id NO1 or the sequence complementary thereto under conditions of at least moderate stringency.
The polynucleotides of the invention hybridize under at least moderately stringent conditions, as detailed below, but preferably under highly stringent conditions, particularly to a polynucleotide comprising the sequence of SEQ ID NO: 1 or a denatured double-stranded DNA probe comprising the entire sequence shown in positions 97-1029 of seq id NO: 1. Suitable experimental conditions for determining hybridization at medium or high stringency between a nucleotide probe and a homologous DNA or RNA sequence include presoaking a filter containing the DNA fragment or RNA in 5 XSSC (sodium chloride/sodium citrate, Sambrook et al, 1989) for 10 minutes of hybridization, presybridization of the filter in 5 XSSC, 5 XDenhardt's solution (Sambrook et al, 1989), 0.5% SDS and 100. mu.g/ml denatured sonicated salmon sperm DNA (Sambrook et al, 1989) solution, followed by hybridization of the same hybridization solution containing a random primer (Feinberg, A.P. and Vogelstein B. (1983) anal. biochem. 132: 6-13), 32P-dCTP tag (greater than 1X 109 cpm/. mu.g) probe at a concentration of 10ng/ml for 12 hours at about 45 ℃. The filter is then washed twice in 2 x SSC, 0.5% SDS at least 60 ℃ (medium stringency), more preferably at least 65 ℃ (medium/high stringency), still preferably at least 70 ℃ (high stringency) and most preferably at least 75 ℃ (very high stringency).
Molecules to which the oligonucleotide probe hybridizes under these conditions are detected with an x-ray film.
As described above, the isolated polynucleotides of the present invention include DNA and RNA. Methods for isolating DNA and RNA are known in the art. The DNA and RNA encoding genes of interest can be cloned in gene banks or DNA libraries by methods known in the art.
Polynucleotides encoding polypeptides having mannanase activity of the invention are then identified and isolated, for example, by hybridization or PCR.
The invention also provides counterpart polypeptides and polynucleotides from different bacterial strains (orthologs or paralogs). Of particular interest are mannanase polypeptides obtained from gram-positive alkaliphilic strains, including bacillus species.
Species homologs of polypeptides having mannanase activity of the invention can be cloned using the information and compositions provided herein in conjunction with conventional cloning techniques. For example, the DNA sequences of the present invention may be cloned using chromosomal DNA obtained from a cell type expressing the protein. Suitable sources of DNA can be determined by probing Northern blots with probes designed with the sequences disclosed herein. Libraries were then prepared from chromosomal DNA of positive cell lines. The DNA sequences of the invention encoding polypeptides having mannanase activity can then be isolated by various methods, for example, by probing with probes designed with the sequences disclosed in the specification and claims of the invention or with one or more sets of degenerate probes based on the disclosed sequences. The DNA sequences of the invention may also be cloned using polymerase chain reaction or PCR (Mullis, US4683202) using primers designed from the sequences disclosed herein. In other Methods, the DNA library may be used to transform or transfect host cells, and the expression of the DNA of interest may be expressed and purified as described in Materials and Methods and example 1, detected with antibodies (monoclonal or polyclonal) produced with mannanase from clones of b.agaradherens, NCIMB40482, or by activity assays associated with polypeptides having mannanase activity.
The mannanase enzyme encoding a DNA sequence which is partially cloned into the plasmid pSJ1678 present in E.coli DSM12180 and/or into an analogous DNA sequence of the invention may be cloned from a strain of the bacterial species Bacillus agaradherens, preferably strain NCIMB40482, or other or related organisms as described herein, which produces an enzyme with mannan degrading activity.
Furthermore, similar sequences can be constituted according to the DNA sequence obtainable from the plasmid present in Escherichia coli DSM12180 (which is regarded as identical to the appended SEQ ID NO: 1), for example a subsequence thereof, and/or by introducing nucleotide substitutions which do not result in a further amino acid sequence of the mannanase encoded by the DNA sequence, but which correspond to the codon usage of the host organism required for the production of the enzyme, or by introducing nucleotide substitutions which result in a different amino acid sequence (i.e.a variant of the mannanase of the invention). Polypeptide:
SEQ ID NO: 2 is the mature mannanase sequence.
The invention also provides mannanase polypeptides which are substantially identical to SEQ ID NO: 2 and its species homologues (paralogues or orthologues). The term "substantially homologous" as used herein means having a sequence identity of at least 70%, preferably at least 80%, more preferably at least 85%, most preferably at least 90% to SEQ ID NO: 2 or orthologs or paralogues thereof or a symbiotic homologue thereof, and amino acids nos. 32-343. More preferably, the polypeptide is at least 95%, most preferably 98% or more identical to SEQ ID NO: 2 or orthologs or paralogues thereof and amino acids nos.32-343 of the paralogues. The percentage of sequence identity is determined by conventional methods, for example using Computer programs known in the art, for example GAP (Program Manual for the Wisconsin Package, 8 th edition, month 8 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) as disclosed in Needleman, S.B. and Wunsch, C.D. (1970), Journal of Molecular Biology (Journal of Molecular Biology), 48, 443-. GAP performs polypeptide sequence comparisons using the following settings: GAP creation offset (penalty)3.0 and GAP extension offset 0.1.
Sequence identity of polypeptide molecules is determined by a similar method, GAP performs DNA sequence comparisons with the following settings: GAP generation offset 5.0 and GAP extension offset 0.3.
The enzyme preparation of the invention is preferably obtained from a microorganism, preferably from a bacterium, archea or a fungus, especially from a bacterium, for example a bacterium belonging to the genus Bacillus, preferably an alkalophilic Bacillus strain, which may be selected from the species Bacillus agaradherens and the very related Bacillus species, wherein all species are preferably at least 95%, more preferably at least 98% homologous to Bacillus agaradherens based on the aligned 16S rDNA sequence. Substantially homologous proteins and polypeptides are characterized as having one or more amino acid substitutions, deletions or additions. These changes are preferably of a minor nature, namely conservative amino acid substitutions (see table 2) and other substitutions that do not significantly affect protein or polypeptide folding or activity; minor deletions, typically 1 to about 30 amino acids; and small amounts of amino-or carboxy-terminal extensions, such as amino-terminal methionine residues, small linker peptides of up to about 20-25 residues or small extensions (affinity tags) that aid in purification, such as poly-histidine tract, protein A (Nilsson et al, EMBO J.4: 1075, 1985; Nilsson et al, Methods enzymol.198: 3, 1991). See generally Ford et al, Protein Expression and Purification (Protein Expression and Purification) 2: 95-107, 1991, incorporated herein by reference. DNA-encoded affinity tags are available from commercial suppliers (e.g., Pharmacia Biotech, Piscataway, NJ; New England Biolabs, Beverly, Mass.). However, even if the above-mentioned alteration is preferably of a minor nature, the alteration may also be of a major nature, e.g., a larger polypeptide of up to 300 amino acids or more fused as an amino-or carboxy-terminal extension to a mannanase polypeptide of the invention. Table 1 conservative amino acid substitutions are basic: arginine, lysine, histidine acidic: glutamic acid, aspartic acid polar: glutamine, asparagine, hydrophobic: leucine, isoleucine, valine aromatic: phenylalanine, tryptophan, tyrosine, minor amounts: glycine, alanine, serine, threonine, methionine
In addition to the 20 standard amino acids, non-standard amino acids (e.g., 4-hydroxyproline, 6-N-methyllysine, 2-aminoisobutyric acid, isovaline, and a-methylserine) may be used to replace amino acid residues of the polypeptides of the present invention. A limited number of non-conserved amino acids, amino acids not encoded by the genetic code, and unnatural amino acids may replace an amino acid residue. "unnatural amino acids" are modified after protein synthesis and/or have a different chemical structure in their side chains than standard amino acids. Unnatural amino acids can be chemically synthesized or, preferably, are commercially available and include 2-pipecolic acid, thiazolidine carboxylic acid, dehydroproline, 3-and 4-methylproline and 3, 3-dimethylproline.
The essential amino acids in the mannanase polypeptides of the invention can be determined according to methods known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, Science 244: 1081-1085, 1989). In the latter technique, a single alanine mutation is introduced at each residue in the molecule, and the resulting mutant molecules are tested for biological activity (i.e., mannanase activity) to determine the amino acid residues that are critical to the activity of the molecule. See also Hilton et al, j.biol.chem.271: 4699-4708, 1996. The active site of the enzyme or other biological interaction may also be determined by physical analysis of the structure, as determined by this technique, such as nuclear magnetic resonance, crystallography, electron diffraction or photoaffinity labeling, in combination with mutations in the putative contact site amino acids. See, e.g., de Vos et al, Science 255: 306-312, 1992; smith et al, J.mol.biol.224: 899-904, 1992; wlodaver et al, FEBS Lett.309: 59-64, 1992. The identity of the essential amino acids can also be deduced from analysis of homologues having a polypeptide related to the polypeptide of the invention.
Multiple amino acid substitutions may be made and tested by mutagenesis, recombination and/or shuffling and subsequent preparation and testing by known methods of relevant scanning techniques, for example as described by Reidhaar-Olson and Sauer (Science 241: 53-57, 1988), Bowie and Sauer (Proc. Natl. Acad. Sci. USA 86: 2152-2156, 1989), WO95/17413 or WO 95/22625. Briefly, these authors disclose methods of randomizing two or more positions simultaneously in a polypeptide, or recombining/scrambling different mutations (WO95/17413, WO95/22625), followed by selection of functional polypeptides and then sequencing the mutagenized polypeptides to determine the spectrum of permissible substitutions at each position. Other methods that can be used include phage display (e.g., Lowman et al, biochem. 30: 10832-.
The above mutagenesis/shuffling methods can be combined with high throughput, automated scanning methods to detect the activity of cloned, mutagenized polypeptides in host cells. Mutagenized DNA molecules encoding active polypeptides can be recovered from host cells and rapidly sequenced using modern equipment. These methods enable the rapid determination of the importance of individual amino acid residues in a polypeptide of interest and can be used for polypeptides of unknown structure. Using the methods described above, one of ordinary skill in the art can identify and/or make sequences similar to SEQ ID NOs: 2, and residues 32-343 of the wild-type protein, maintaining the mannanase activity of the wild-type protein. Protein preparation:
the proteins and polypeptides of the invention, including full-length proteins, fragments thereof, and fusion protein markers, can be prepared in genetically engineered host cells according to conventional techniques. Suitable host cells are those cell types which can be transformed or transfected with exogenous DNA and grown in culture, including bacterial, fungal, and higher eukaryotic cells in culture. Bacterial cells, in particular cultured cells of gram-positive organisms, are preferred. Particularly preferred are gram-positive cells from the genus Bacillus, for example those from Bacillus subtilis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus (Bacillus lautus), Bacillus thuringiensis, Bacillus licheniformis and Bacillus agaradherens, especially Bacillus agaradherens.
Techniques for manipulating cloned DNA molecules and introducing foreign DNA in various host cells are described by Sambrook et al, Molecular Cloning: a Laboratory Manual, second edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989; ausubel et al, (eds.), current protocols in Molecular Biology (CurrentProtocols in Molecular Biology), John Wiley and Sons, inc., NY, 1987; and "Bacillus subtilis and other gram-positive bacteria", Sonensheim et al, 1993, American Society for Microbiology, Washington D.C., which is incorporated herein by reference. Typically, the DNA sequence encoding the mannanase of the invention is operably linked to other genetic elements required for its expression, typically including a transcription promoter and terminator in an expression vector. The vector will also typically contain one or more selectable markers and one or more origins of replication, although those skilled in the art will recognize that in some systems, selectable markers may be provided on a separate vector and replication of the exogenous DNA may be provided by integration into the host cell genome. The selection of promoters, terminators, selectable markers, vectors, and other elements is a matter of routine design for one of ordinary skill in the art. Many of these elements are described in the literature and are available through commercial suppliers.
To direct the polypeptide into the secretory pathway of the host cell, a secretory signal sequence (also referred to as a leader, prepro, or pre-sequence) is provided in the expression vector. The secretory signal sequence may be a polypeptide sequence or may be derived from other secretory proteins or synthesized de novo. Various suitable secretion signal sequences are known in the art, see "Bacillus subtilis and other gram bacteria", Sonensheim et al, 1993, American society for Microbiology, Washington D.C.; and Cutting, S.M "(eds)" molecular biology method of bacillus ", John Wiley and Sons, 1990, which further describes suitable secretion signal sequences particularly suitable for secretion by bacillus host cells. The secretory signal sequence is linked to the DNA sequence in the correct reading frame. Secretion signal sequences are typically located 5' to the DNA sequence encoding the polypeptide of interest, although certain signal sequences may be located elsewhere in the DNA sequence of the polypeptide of interest (see, e.g., Welch et al, US 5037743; Holland et al, US 5143830).
The transformed or transfected host cells are cultured according to conventional methods in a medium containing nutrients and other components required for growth of the selected host cell. Various suitable media, including media of known composition and complex media, are known in the art and typically include carbon sources, nitrogen sources, essential amino acids, vitamins and minerals. The medium may also include components such as growth factors or serum as desired. The growth medium will typically be selected by, for example, drug selection, based on cells containing exogenously added DNA, or based on defects in the essential nutrients complemented by selectable markers carried in the expression vector or co-transfected into the host cell. Protein separation:
when the expressed recombinant polypeptide is secreted, the polypeptide may be purified from the growth medium. The expression host cells are preferably removed from the culture medium (e.g., by centrifugation) prior to purification of the polypeptide.
When the expressed recombinant polypeptide is not secreted by the host cell, the host cell is preferably disrupted and the polypeptide is released into an aqueous "extract", which is the first stage of the purification technique. The expression host cells are preferably harvested from the culture medium (e.g., by centrifugation) prior to cell disruption.
Cell disruption can be performed by conventional techniques, such as by lysozyme digestion or by applying pressure to the cells by high pressure. See (Robert k. scenes, "protein purification," 2 nd edition, Springer-Verlag), which further describes this cell disruption technique.
Regardless of whether the expressed recombinant polypeptide (or chimeric polypeptide) is secreted, it can be purified using fractionation and/or conventional purification methods and media.
Ammonium sulfate precipitation and acid or chaotrope extraction may be used for fractionation of the sample. Exemplary purification steps may include hydroxyapatite, size exclusion, FPLC and reverse phase high performance liquid chromatography. Suitable anion exchange media include derivatized dextrins, agarose, cellulose, polyacrylamide, specialty silicas, and the like. PEI, DEAE, QAE and Q derivatives are preferred, DEAE Fast-Flow Sepharose (Pharmacia, Piscataway, NJ) being particularly preferred. Exemplary chromatographic media include media derivatized with Phenyl, butyl or Octyl groups, such as Phenyl-Sepharose FF (Pharmacia), Toyopearl butyl 650(TosoHaas, Montgomeryville, Pa.), Octyl-Sepharose (Pharmacia), and the like; or polyacrylic resins such as Amberchrom CG 71(Toso Haas). Suitable solid supports include glass beads, silica-based resins, cellulose resins, agarose beads, cross-linked agarose beads, polystyrene beads, cross-linked polyacrylamide resins, and the like, which are insoluble under the conditions of their use. These carriers can be modified with reactive groups so that proteins can be attached via amino, carboxyl, thiol, hydroxyl and/or carbohydrate moieties. Examples of coupling chemistry methods include cyanogen bromide activation, N-hydroxysuccinimide activation, epoxide activation, sulfhydryl activation, hydrazide activation, and carboxyl and amino derivatives used in carbodiimide coupling chemistry. These and other solid media are known and widely used in the art and are available from commercial suppliers.
The choice of a particular method is a matter of routine design only, and is determined in part by the nature of the vector chosen. See, e.g., affinity chromatography: principles and Methods (Affinity Chromatography: Principles & Methods), Pharmacia LKB Biotechnology, Uppsala, Sweden, 1988.
The polypeptides of the invention or fragments thereof may also be prepared by chemical synthesis. The polypeptides of the invention may be monomeric or multimeric, glycosylated or non-glycosylated; pegylated or non-pegylated; and may or may not include the initial methionine amino acid residue.
Based on the sequence information disclosed herein, a full length DNA sequence encoding the mannanase of the invention and comprising the DNA sequence shown in SEQ ID No1, at least from position 97 to position 1029, can be cloned.
Cloning is carried out by standard techniques known in the art, for example by preparing a genomic library from a strain of bacillus, especially strain b. agaradherens, NCIMB 40482; plating the library on a suitable substrate plate; identifying clones containing the polynucleotide sequence of the invention by standard hybridization techniques using probes based on SEQ ID No 1; or by identifying clones from the Bacillus agaradherens NCIMB40482 genomic library by reverse polymerase chain reaction strategy using primers based on the sequence information of SEQ ID No 1. See m.j.mcpherson et al ("PCR, a practical method)" Information Press Ltd, Oxford England), which further details the inverse polymerase chain reaction.
It is only routine work for a person skilled in the art to use a similar strategy to isolate a homologous polynucleotide sequence encoding the homologous mannanase of the invention from a genomic library of a relevant microorganism, in particular from other strains of Bacillus, e.g.Alcaligenes sp, based on the sequence information disclosed herein (SEQ ID No1, SEQ ID No 2).
Furthermore, the DNA encoding the mannan or galactomannan-degrading enzyme of the invention may be conveniently cloned according to known methods from suitable sources, such as any of the above mentioned organisms, by using synthetic oligonucleotide probes prepared on the basis of DNA sequences obtained from the plasmid present in E.coli DSM 12180.
Thus, the polynucleotide molecule of the invention can be isolated from E.coli DSM12180, wherein a plasmid obtained by e.g.the above-described cloning is deposited. Furthermore, the invention relates to an isolated substantially pure biological culture of the strain escherichia coli DSM 12180.
In the present invention, the term "enzyme preparation" refers to a conventional enzyme fermentation product obtained from a single kind of microorganism, which can be isolated and purified, and which usually contains many different enzyme active substances; or a mixture of single-component enzymes, preferably enzymes obtained by using conventional recombinant techniques from bacterial or fungal species, which have been fermented and possibly separately isolated and purified, which may be obtained from different species, preferably fungal or bacterial species; or a fermentation product of a microorganism which serves as a host cell for the expression of the recombinant mannanase, but which simultaneously produces other enzymes, such as pectin degrading enzymes, proteases or cellulases, is a naturally occurring fermentation product of the microorganism, i.e. an enzyme complex conventionally prepared by the corresponding naturally occurring microorganism.
A method of preparing an enzyme preparation of the invention, the method comprising culturing a microorganism, e.g.a wild-type strain capable of producing mannanase under conditions permissive for the production of the enzyme, and recovering the enzyme from the culture. Culturing can be carried out using conventional fermentation techniques, e.g., culturing in shake flasks or fermentors with agitation to ensure adequate aeration of the growth medium, inducing mannanase production. The growth medium may contain a conventional N-source, such as peptone, yeast extract or casamino acids, a reduced amount of a conventional C-source, such as glucose or sucrose, and an inducer, such as guar gum or carob gum. Recovery may be carried out using conventional techniques, for example separation of the biological material and supernatant by centrifugation or filtration, and if the enzyme of interest is intercellular, recovery of the supernatant or cell disruptor, perhaps followed by further purification by crystallization as described in EP0406314 or as described in WO 97/15660. Immunological cross-reactivity:
polyclonal antibodies for determining immunological cross-reactivity may be prepared by using purified mannanase. More specifically, antisera to the mannanase enzymes of the invention may be raised by immunizing rabbits (or other rodents) according to the methods described in N.Axelsen et al, "quantitative immunoelectrophoresis handbook", Blackwell Scientific Publications, 1973, Chapter 23 or A.Johnstone and R.thorpe, "immunochemical practice", Blackwell Scientific Publications, 1982, (more specifically pages 27-31). Purified immunoglobulins can be obtained from antisera by e.g.salt precipitation (ammonium sulphate) followed by dialysis and ion exchange chromatography, e.g.in DEAE-Sephadex. Immunochemical characterization of proteins can be carried out by Outcherlony double diffusion analysis (O.Ouchterlony in "A.S.A. (D.M.Weir, Ed.) Blackwell Scientific Publications, 1967, p.655-706), by cross-immunoelectrophoresis (N.Axelsen et al, chapters 3 and 4, supra) or by rocket immunoelectrophoresis (N.Axelsen et al, chapter 2).
Examples of useful bacteria for producing the enzyme or enzyme preparation of the invention are gram-positive bacteria, preferably obtained from Bacillus/lactobacillus subclasses, preferably from strains of Bacillus, more preferably from Bacillus agaradherens, especially the strain Bacillus agaradherens, NCIMB 40482.
The invention includes isolated mannanases having the above-described properties, which are free of homologous impurities and are produced using conventional recombinant techniques. Determination of catalytic Activity of mannanase (ManU)
Colorimetric test: substrate: 0.2% AZCL-galactomannan from carob beans (Megazyme, Australia) in 0.1M p-hydroxyphenylglycine (Glycin) buffer, pH 10.0. The tests were carried out on a hot mixer with stirring and temperature control at 40 ℃ in Eppendorf Micro tubes 1.5 ml. 0.750ml of substrate was incubated with 0.05ml of enzyme for 20 minutes and stopped by centrifugation at 15000rpm for 4 minutes. The color of the supernatant was measured at 600nm in a 1cm cuvette. One ManU (mannanase unit) in 1cm gave 0.24 (absolute). Obtaining BACILLUS AGARADHERENS mannanase NCIMB40482 strain
Coli strain E.coli SJ2 cells (Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, B.R., Sjoholm, C. (1990) clone aldB, encoding α -acetolactate decarboxylase, an extracellular enzyme from Brevibacillus, J.Bacteriol., 172, 4315-4321), using Gene Pulser obtained from BIO-RADTMThe electroporation was converted by electroporation as described by the supplier.
Bacillus subtilis PL2306. this strain is Bacillus subtilis DN 1885(Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, B.R., Sjoholm, C. (1990) clone aldB, which encodes α -acetolactate decarboxylase, an extracellular enzyme from Brevibacillus brevis, J.Bacteriol., 172, 4315-.
Such as Yasbin, r.e., Wilson, g.a., and Young, F.E. (1975) "transformation and transfection in lysogenic strains of bacillus subtilis: demonstration of selection for introduction of prophages in competent cells ", j. bacteriol.121: 296-304 and transformation. Plasmid pSJ1678 (described in detail in WO94/19454, incorporated herein by reference). pMOL 944: this plasmid is a pUB110 derivative which mainly contains elements for preparing a plasmid that can be propagated in Bacillus subtilis, kanamycin resistance gene, and a signal peptide cloned from amyL gene of Bacillus licheniformis ATCC14580 with a strong promoter. The signal peptide contains a Sacll position, which makes it convenient to clone the DNA encoding the mutant part of the protein fused to the signal peptide. This results in the expression of a proprotein, which is directed to the outside of the cell.
Plasmids were constructed by conventional genetic engineering techniques as briefly described below. Construction of pMOL 944:
the pUB110 plasmid (McKenzie, T. et al, 1986, "plasmid" 15: 93-103) was digested with a single restriction enzyme Ncil. Plasmid pSJ2624 was obtained by digesting the PCR fragment amplified from the amyL promoter encoded on plasmid pDN1981 (P.L. Jorgensen et al, 1990, "Gene", pages 96, 37-41) with Ncil and inserting it into Ncil-digested pUB 110.
The two PCR primers used had the following sequences:
#LWN5494 5′-
GTCGCCGGGGCGGCCGCTATCAATTGGTAACTGTATCTCAGC-3′
#LWN5495 5′-
GTCGCCCGGGAGCTCTGATCAGGTACCAAGCTTGTCGACCTGCAGAA
TGAGGCAGCAAGAAGAT-3′
primer # LWN5494 was inserted at the Notl position in the plasmid.
Plasmid pSJ2624 was subsequently digested with Sacl and Notl, the new PCR fragment amplified from the amyL promoter encoded on pDN1981 was digested with Sacl and Notl, and the DNA fragment was inserted into Sacl-Notl digested pSJ2624 to give plasmid pSJ 2670.
This clone replaced the first amyL promoter cloned with the same promoter but in the opposite direction. Two primers used for PCR amplification had the following sequences:
#LWN5938 5′-
GTCGGCGGCCGCTGATCACGTACCAAGCTTGTCGACCTGCAGAATG
AGGCAGCAAGAAGAT-3′
#LWN5939 5′-GTCGGAGCTCTATCAATTGGTAACTGTATCTCAGC-3′
plasmid pSJ2670 was digested with restriction enzymes Pstl and Bcl, the PCR fragment amplified from the cloned DNA sequence encoding alkaline amylase SP722 (disclosed in International patent application publication WO95/26397, incorporated herein by reference) was digested with Pstl and Bcl, and inserted into plasmid pMOL 944. Two primers used for PCR amplification had the following sequences:
#LWN7864 5′-AACAGCTGATCACGACTGATCTTTTAGCTTGGCAC-3′
#LWN7901 5′-AACTGCAGCCGCGGCACATCATAATGGGACAAATGGG-3′
primer # LWN7901 was inserted into the Sacll site of the plasmid. Cloning of the genomic DNA of the mannanase gene from Bacillus agaradherens:
the strain Bacillus agaradherens NCIMB40482 was propagated in a liquid medium as described in WO 94/01532. After 16 hours of incubation at 30 ℃ and 300rpm, the cells were harvested and genomic DNA was isolated by the method described by Pitcher et al (Pitcher, D.G., Saunders, N.A.Owen, R.J. (1989) "Rapid extraction of bacterial genomic DNA with guanidine thiocyanate", Lett.appl.Microbiol., 8, 151-. Construction of a genomic library:
the genomic DNA was partially digested with the restriction enzyme Sau3A and size-fractionated by electrophoresis on a 0.7% agarose gel. Fragments of size between 2 and 7kb were separated by electrophoresis on DEAE-cellulose paper (Dretzen, G.Bellard, M., Sassone-Corsi, P., Chambon, P. (1981) "reliable method for the recovery of DNA fragments from agarose and acrylamide gels" anal.biochem., 112, 295-.
The isolated DNA fragment was ligated to BamHI-digested pSJ1678 plasmid DNA and the ligation mixture was used to transform E.coli SJ 2. Identification of positive clones:
the E.coli DNA library constructed as described above was screened on LB agar plates containing 0.2% AZCL-galactomannan (Megazyme) and 9. mu.g/ml chloramphenicol and incubated overnight at 37 ℃. Clones expressing mannanase activity showed a blue spreading halo. Plasmid DNA from one of these clones was isolated by Qiagen plasmid spin preps in 1ml overnight culture broth (cells were cultured in TY containing 9. mu.g/ml chloramphenicol at 37 ℃ and shaken at 250 rpm).
This clone (MB525) was further characterized by DNA sequencing of the cloned Sau3A DNA fragment. DNA sequencing was performed by primer walking using a Taq deoxy-end cycle sequencing device (Perkin-Elmer, USA) a fluorescent agent-labeled terminator and appropriate oligonucleotides for use as primers.
The analysis of the sequence data was performed as described in Devereux et al (1984) "nucleic acids research", 12, 387-. The sequence encoding the mannanase is shown in SEQ ID No 1. The derived protein sequence is shown in SEQ ID No. 2. Subcloning and expression of mannanase in bacillus subtilis:
the mannanase encoding the DNA sequence of the invention is PCR amplified with a PCR primer set consisting of two oligonucleotides: mannanase, supra Sacll
5′-CAT TCT GCA GCC GCG GCA GCA AGT ACA GGC TTT TAT GTT GAT GG-
3' mannanase, Notl
5′-GAC GAC GTA CAAGCG GCC GCG CTA TTT CCC TAA CAT GAT GAT
ATTTTCG-3′
The restriction bits Sacll and Notll are underlined.
Chromosomal DNA isolated as described above by b.agaradherns NCIMB40482 was used as template in a PCR reaction using Amplitaq DNA polymerase (Perkin Elmer) according to the manufacturer's instructions. The PCR reaction was set up in PCR buffer (10mM Tris-HCl, pH8.3, 50mM potassium chloride, 1.5mM magnesium chloride, 0.01% (w/v) gelatin) containing 200. mu.M of each dNTP, 2.5 units of AmpliTaq polymerase (Perkin-Elmer, Cetus, USA) and 100pmol of each primer.
The PCR reaction was performed using a DNA thermal cycler (Landgraf, Germany). Incubation at 94 ℃ for 1 min followed by 30 cycles of PCR using cycles of denaturation at 94 ℃ for 30 sec, annealing at 60 ℃ for 1 min and extension at 72 ℃ for 2 min. A5. mu.l aliquot of the amplified product was analyzed electrophoretically in a 0.7% agarose gel (NuSieve, FMC), and the appearance of a DNA fragment size of 1.4kb indicated proper amplification of the gene fragment. Subcloning of PCR fragments
A45. mu.l aliquot of the PCR product generated above was purified using the QlAquick PCR purification equipment (Qiagen, USA) according to the manufacturer's instructions. The purified DNA was eluted with 50. mu.l of 10mM Tris-HCl, pH 8.5.
Mu.g of pMOL944 and 25. mu.l of the purified PCR fragment were digested with Sacll and Notl, electrophoresed on a 0.8% low-gel temperature agarose (SeaPlaque GTG, FMC) gel, and the relevant fragment excised from the gel and purified using a QlAquick gel extraction apparatus (Qiagen, USA) according to the manufacturer's instructions. The isolated PCR DNA fragment was then ligated into Sacll-Notl digested and purified pMOL 944. Ligation was performed overnight at 16 ℃ with 0.5. mu.g of each DNA fragment, 1U of T4DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany).
The ligation mixture was used to transform competent Bacillus subtilis PL2306. Transformed cells were plated on LBPG-10. mu.g/ml kanamycin plates. After incubation at 37 ℃ for 18 hours, colonies were visible on the plates. Several clones were analyzed by isolating plasmid DNA from overnight culture broth.
This positive clone was restreaked (restreak) several times on the agar plate used above and was designated as MB 594. Clone MB594 was grown overnight at 37 ℃ at TY-10. mu.g/ml kanamycin, and the next day the Plasmid was isolated from this with 1ml cells using the Qiaprep Spin Plasmid Miniprep Kit #27106, according to the manufacturer's instructions for the Plasmid preparation procedure in Bacillus subtilis. The DNA was sequenced and showed a mature part corresponding to the mannanase, i.e. the attached SEQ ID NO: 3, the DNA sequence of positions 94-1404. The derived mature protein is represented in SEQ ID NO: 4, respectively. It is shown by SEQ ID NO: 1 was changed to the 3' end of the mannanase enzyme encoded by the sequence of SEQ id no: 3, or a sequence shown in seq id no. The resulting amino acid sequence is shown in SEQ ID NO: 4, it is apparent that SEQ ID NO: 2 (SHHVREIGVQFSAADNS SGQTALYVDNVTLR) to SEQ ID NO: 4 (IIMLGK). Culture medium: TY (as described in Ausubel, F.M., et al (eds.) "Current protocols in Molecular Biology". John Wiley and Sons, 1995). LB agar (as described in Ausubel, F.M. et al (eds.) "Current protocols in Molecular biology". John Wiley and Sons, 1995). LBPG is LB agar (described above) supplemented with 0.5% glucose and 0.05M potassium phosphate, pH 7.0. BPX medium is described in EP0506780(WO 91/09129). Expression, purification and characterization of mannanase from Bacillus agaradherens
Clone MB594, obtained as described in the above Materials and Methods, was grown in 500ml double baffle shake flasks in 25X 200ml BPX medium containing 10. mu.g/ml kanamycin at 37 ℃ and 300rpm for 5 days.
6500ml of the shake flask culture fluid of clone MB594 (batch #9813) was collected and pH adjusted to 5.5. During stirring, 146ml of cationic agent (C521) and 292ml of anionic agent (A130) were added for flocculation. The flocculated material was separated by centrifugation with a Sorval RC 3B centrifuge at 9000rpm for 20 minutes at 6 ℃. The supernatant was clarified by Whatman glass filters GF/D and C and finally concentrated by filtration with a cut-off of 10 kDa. 750ml of the concentrate are adjusted to pH7.5 with sodium hydroxide. The clear solution was used for anion exchange chromatography using a 900ml Q-Sepharose column equilibrated with 50 mmole Tris pH 7.5. The mannanase activity conjugate was eluted with a sodium chloride gradient.
The pure enzyme gave a single band in SDS-PAGE with a molecular weight of 38 kDa. The amino acid sequence of the mannanase, i.e., the translated DNA sequence, is shown in SEQ ID No. 2.
And (3) determining a kinetic constant: substrate: carob bean gum (arob) and reduced sucrose assay (PHBAH). Carob bean gum obtained from Sigma (G-0753). Kinetic measurements with different concentrations of carob gum, incubated at 40 ℃ for 20 minutes at pH10 gave Kcat: 467K/sm: 0.08 g/lMW: 38kDapl (isoelectric point): 4.2 temperature optimum of mannanase is 60 ℃. The pH activity curve shows a maximum activity between pH 8-10. The DSC differential scanning calorimeter gave a melting point of 77 ℃ in Tris buffer at pH7.5, indicating that the enzyme is very thermostable. Detergent compatibility determined using 0.2% AZCL-galactomannan derived from carob gum as a substrate and incubated at 40 ℃ as described above showed excellent compatibility with conventional liquid detergents and good compatibility with conventional powder detergents. Obtaining of Bacillus subtilis mannanase 168
The Bacillus subtilis β -mannanase was characterized and purified as follows:
homology of the Bacillus subtilis genome was searched using the known Bacillus β -mannanase GENE sequence (Mendoza et al, Biochemica et Biophysica Acta 1243: 552-554, 1995), the coding region of ydhT, the product of which was unknown, showed 58% similarity to the known Bacillus β -mannanase. oligonucleotides were designed to amplify the sequence of the mature part encoding the putative β -mannanase 5'-GCT CAA TTG GCG CAT ACTGTG TCG CCT GTG-3' and 5'-GAC GGA TCC CGG ATT CAC TCA ACG ATT GGCG-3'. the total genomic DNA obtained from Bacillus subtilis strain 1A95 was used as a template to amplify the ydhT mature region using the above primers. the PCR was performed using the GENE-AMP PCR Kit with AMPLITAQDNA polymerase (Perkin Elmer, Applied Biosystems, Foster City, CA.) first melting at 95 ℃ for 5 minutes followed by 25 cycles of 1 minute melting at 95 ℃, annealing at 55 ℃ for 2 minutes, extension at 72 ℃ for 2 minutes after the last cycle, the reaction was performed with 10 minutes at 72 ℃ and purification was performed using the Chackwork apparatus of PCR (Qiagen).
The ydhT mature region amplified by Bacillus subtilis strain 1A95 was inserted into the expression vector pPG1524 (previously described) as follows.the amplified 1028bp fragment was digested with Mfe I and BamHI.the expression vector pPG1527 was digested with EcoR I and BamH I.the restriction products were purified using QlAquick PCR purification equipment (Qiagen, Chatsworth, CA). the two fragments were ligated using T4DNA ligase (13 hours, 16 ℃) for transformation of competent E.coli strains DH5- α. ampicillin resistant colonies were grown for DNA preparation.
7 kanamycin-resistant Bacillus subtilis clones and 1 PG632 control clone were selected, grown in 20ml 20/20/5 medium (20g/l tryptone, 20g/l yeast extract and 5g/l sodium chloride) supplemented with 1ml 25% maltrin, 120. mu.l 10mM manganese dichloride and 20. mu.l 50mg/ml kanamycin. the clones were grown overnight at 37 ℃ in 250ml baffled flasks shaken at 250rpm to express the protein. the cells were spun for 15 minutes at 14000 rpm. 1. mu.l of each supernatant was diluted with 99. mu.l of 50mM sodium acetate (pH 6.0). 1. mu.l of this dilution was assayed according to the manufacturer's instructions with endo-1, 4- β -mannanase β -mannazyme Tabs (Megazyme, Ireland.) the absorbance was measured at 590nm in a Beckman DU640 spectrophotometer clone 7. the highest absorbance of 1.67 was shown at 590 nm. the PG control did not show absorbance at 590 nm.
The supernatant was analyzed by SDS-PAGE in a 10-20% Tris-glycine gel (Novex, San Diego, Ca) to confirm the expected protein size of 38 kDa. The samples were prepared as follows. A500. mu.l sample of the supernatant of ydhT clone 7 and PG632 was precipitated with 55.5. mu.l of 100% trichloroacetic acid (Sigma), washed with 100. mu.l of 5% trichloroacetic acid, resuspended in 50. mu.l of Tris-glycine SDS sample buffer (Novex) and boiled for 5 minutes. Mu.l of each sample was electrophoresed in a gel at 30mA for 90 minutes. The observation of a large band of protein indicated that ydhT clone 7 was 38 kDa.
10l fermentation of Bacillus subtilis ydhT clone 7 was performed in a B.Braun Biostat C fermenter, the fermentation conditions were as follows.cells were grown in a rich medium similar to 20/20/5 at 37 ℃ for 18 hours at the end of the fermentation experiment, the cells were removed, the supernatant was concentrated to 11 with a tangential flow filtration system and the final yield of β -mannanase in the concentrated supernatant was determined to be 3 g/l.
Purification of β -mannanase from fermentation supernatant is carried out by centrifugation of 500ml of supernatant at 10000rpm for 10 minutes at 4 ℃ the centrifuged supernatant is then dialyzed overnight at 4 ℃ against two 4 l10 mM potassium phosphate (pH7.2) changes by Spectrapor 12000-14000mol.wt. cut-off membrane (Spectrum). the dialyzed supernatant is centrifuged at 10000rpm for 10 minutes at 4 ℃ 200ml Q Sepharose fast flow (Pharmacia) anion exchange column is equilibrated at 20 ℃ with 1l 10mM potassium phosphate (pH7.2), 300ml of supernatant is loaded in the column, two flow-through fractions 210ml (sample A) and 175ml (sample B) are collected and analyzed as above, except that the sample is diluted with 199. mu.l 50mM potassium phosphate (pH6.0) which show the absorbance of 2. mu.l of the protein fraction of 38 and 52. mu.l each of a 8. mu.M glycine-SDS buffer (Novex, the sample is diluted with 199. mu.l 50mM protein (pH6.0) to give a single gel containing more than 1 mg of protein in the same sample of Tris-95. mu.l protein as the gel sample, and the two samples of protein in which are analyzed by spraying the same gel with the amino acid gel (Tris-3. mu.5. mu.M protein in the gel with the sample of the gel containing the amino acid fraction of the amino acid, 95. protein, 95. 10. mu.0, respectively, 95. mu.0, 95. mu.5. mu.0, 95. protein, 95. mu.0, 95. mu.1.
All assays were performed using the above described endo-1, 4- β -mannanase β -mannanase Tabs (Megazyme Eleland.) with activity in the pH range 3.0-9.0 in 50mM citrate phosphate buffer, for activity determination at pH9.5 50mM CAPSO (Sigma) was used, and for the pH range 10.0-11.0, 50mM CAPS buffer was used, the optimum pH for Bacillus subtilis β -mannanase was pH6.0-6.5, the temperature activity profile was performed in 50mM citrate phosphate (pH6.5), the enzyme showed optimum activity at 40-45 deg.C, the Bacillus subtilis β -mannanase maintained significant activity at below 15 deg.C and above 80 deg.C, the sequence for endo-1, 4- β -mannanase Tabs (Megazyme Tabs) was determined using the amino acid sequences of SEQ ID No.1, 4- β -mannanase 7- β, the amino acid sequence of the mannanase was shown in SEQ ID No. 7.8.8.8-35000 and the amino acid sequence for the mannanase at pH 1.0-11.0 range.
The mannanase is preferably added to the compositions of the invention at a level of from 0.0001% to 2%, more preferably from 0.0005% to 0.1%, most preferably from 0.001% to 0.02% pure enzyme by weight of the composition.
The enzyme of the invention comprises, in addition to the enzymatic core comprising the catalytic domain, a Cellulose Binding Domain (CBD), the cellulose binding domain of the enzyme and the enzymatic core (catalytically active domain) being operably linked. The Cellulose Binding Domain (CBD) may be present as an integral part of the encoded enzyme, or CBDs from other sources may be introduced into the enzyme to form an enzyme hybrid. Herein, the term "cellulose binding domain" is understood as meaning, as by Peter Tomme et al, "cellulose binding domain: classification and properties ", defined in" enzymatic degradation of insoluble carbohydrates ", John n.saddler and Michael h.penner (Eds), ACS Symposium Series, No.618, 1996. This definition divides more than 120 cellulose binding domains into 10 families (I-X), suggesting that CBDs are present in various enzymes, such as cellulases, xylanases, mannanases, arabinofuranosidases, acetyl esterases and chitinases. CBD has also been found in algae, for example the red alga Porphyra purpurea, which is a non-hydrolytic polysaccharide binding protein, see Tomme et al, supra cited references. However, most CBDs are derived from cellulases and xylanases, with the CBDs at the N-and C-termini or in the middle of the protein. Enzyme hybrids are known in the art, see for example WO90/00609 and WO95/16782, and may be prepared by transforming a DNA construct containing at least one DNA fragment encoding a cellulose binding domain linked, with or without a linker, to a DNA sequence encoding a mannanase enzyme into a host cell and growing the host cell to express the fused gene. The enzyme hybrid can be described by the following formula:
CBD-MR-X wherein CBD is the N-terminal or C-terminal region of the amino acid sequence corresponding to at least the cellulose binding domain; MR is the middle region (linker) and can be a bond, or a short linking group of preferably about 2 to about 100 carbon atoms, more preferably 2 to 40 carbon atoms; or preferably from about 2 to about 100 amino acids, more preferably from 2 to 40 amino acids; and X is the N-terminal or C-terminal region of the enzyme of the invention.
The enzyme may be of any suitable origin, for example of plant, animal, bacterial, fungal and yeast origin. The source may also be mesophilic or extremophilic (extreme conditions) (psychrophilic, thermophilic, barotropic, alkalophilic, acidophilic, halophilic, etc.). These enzymes can be used in pure or impure form. At present, it is common practice to modify wild-type enzymes via protein/genetic engineering techniques to optimize their performance efficiency in the washing and/or fabric care compositions of the present invention. For example, variants can be designed to increase the compatibility of the enzyme with components commonly encountered in such compositions. Furthermore, the variants can be designed such that the optimum pH, bleach or chelant stability, catalytic activity, etc. of the enzyme variant can be tailored to a particular wash application.
In the case of bleach stability, particular attention should be paid to oxidation-sensitive amino acids, and to surface charge for surfactant compatibility. The isoelectric point of such enzymes can be modified by substitution of certain charged amino acids, for example increasing the isoelectric point will help to improve compatibility with anionic surfactants. The stability of the enzyme can be further improved by creating, for example, additional salt bridges, while enhancing the metal binding sites to increase chelator stability. Soft clay
The second essential component of the laundry detergent and/or fabric care compositions of the present invention is a softening clay. Any clay or mixture thereof used in the prior art may be used in the present invention. Preferred examples are disclosed in GB1400898 or US 5019292.
Included among these clays are various heat-treated kaolins and various multi-layered smectites or bentonites, also known as montmorillonites. As is known in the art, the preferred smectite clays exhibit a cation exchange capacity of at least 50meq/100g of clay, which corresponds to a layer charge of 0.2-0.6. More preferred are clays having a particle size of 5-50 microns.
Other preferred smectite clays are hectorite clays of the formula:
wherein y is 0; or Me if y is 0IIIIs Al, Fe or B; mn+Is a monovalent (n ═ 1) or divalent (n ═ 2) metal ion, for example selected from sodium, potassium, magnesium, calcium, strontium. The value of (x + y) is the layer charge of the hectorite clay. The hectorite clay suitable for use in the detergent compositions of the present invention has a layered charge distribution such that at least 50% is in the range of 0.23-0.31.
Preference is given to hectorite clays of natural origin which have a layer charge distribution such that at least 65% is in the range from 0.23 to 0.31.
Specific non-limiting examples of fabric softening smectite clay minerals are: -sodium montmorillonite: borck(R)，Volclay BC(R)，Gelwhite GP(R)，Thixo-Jel(R)，Ben-A-Gel(R). -spodumene sodium: veegum F(R)And Laponite SP(R)-sodium talc: barasym NAS 100(R)-calcium montmorillonite: soft Clark(R)，Gelwhite L(R)，Imvite K(R)，CSM-Clay(R)Spodumene from Kimoulos: barasym LIH 200R。
The amount of softening clay used in the present invention depends on the form of the laundry detergent and/or fabric care composition. Typically, it may range from a lower limit of 0.1%, 3% or 4% to an upper limit of 50%, 25% or 15%. Detergent component
The laundry detergent and/or fabric care compositions of the present invention must contain at least one other detergent component. The specific nature of these additional components and the amounts in which they are added will depend on the physical form of the composition and the nature of the washing operation used.
The laundry detergent and/or fabric care compositions of the present invention preferably further comprise a laundry detergent and/or fabric care ingredient selected from cellulases, builders selected from zeolites, sodium tripolyphosphate and/or layered silicates, cationic surfactants and/or mixtures thereof.
The laundry detergent and/or fabric care compositions of the present invention may be liquid, paste, gel, bar, tablet, spray, foam, powder or granule. The particulate composition may also be in "compact" form and the liquid composition may also be in "concentrated" form.
The compositions of the present invention may be formulated, for example, as hand and machine laundry detergent compositions, including laundry additive compositions and compositions suitable for the soaking and/or pretreatment of soiled fabrics and rinse-added fabric softener compositions.
When formulated as a composition for use in a machine wash laundry process, the composition of the present invention preferably contains both a surfactant system, which may contain anionic, cationic, nonionic, zwitterionic or a mixture of surfactants, and a builder system, which may contain phosphate-based builders, non-phosphate-based inorganic zeolites, layered silicates, organic builders, such as citrates, and additionally one or more detergent components, preferably selected from organic polymers, bleaches, additional enzymes, suds suppressors, dispersants, lime soap dispersants, soil suspending agents and anti-redeposition and corrosion inhibitors. The laundry compositions may also contain softening agents other than the inorganic clays claimed herein as additional detergent components. When formulated as a laundry detergent composition, the compositions comprising the mannanase enzyme and clay provide fabric laundering, soil removal, softness and color appearance.
The compositions of the present invention may also be used as detergent additive products in solid or liquid form. The additive product is used to supplement or enhance the performance of conventional detergent compositions and may be added at any stage of the laundering process.
The laundry detergent composition of the present invention has a density, as measured at 20 ℃ of 400-1200 g/l, preferably 500-950 g/l, as desired.
The "compact" form of the composition of the invention is best reflected by the density and, for the composition, the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salt is present in a large amount, typically from 17 to 35% by weight of the total composition. In the compact composition, the filler salt is present in an amount of no more than 15%, preferably no more than 10%, most preferably no more than 5% by weight of the total composition. Inorganic filler salts, such as those referred to in the compositions of the present invention, are selected from the group consisting of alkali and alkaline earth metal sulfates and chlorides. A preferred filler salt is sodium sulfate.
The liquid detergent compositions of the present invention may also be in "concentrated form", in which case they will contain lower amounts of water than conventional liquid detergents. The water content of the concentrated liquid detergent is typically less than 40%, more preferably less than 30%, most preferably less than 20% by weight of the detergent composition.
Suitable detergent compounds for use in the present invention are selected from the compounds described below. Surfactant system
The laundry detergent and/or fabric care compositions of the present invention may additionally contain a surfactant system wherein the surfactant may be selected from nonionic and/or anionic and/or cationic and/or amphoteric and/or zwitterionic and/or semi-polar surfactants. The laundry detergent and/or fabric care compositions of the present invention preferably further comprise a cationic surfactant. We have surprisingly found that compositions containing cationic surfactants provide improved cleaning and softening performance.
Other surfactants are typically present in amounts of 0.1% to 60% by weight. More preferably, the amount added is from 1% to 35% by weight, most preferably from 1% to 30% by weight, in the laundry detergent and/or fabric care compositions of the present invention.
The surfactant is preferably formulated to be compatible with the enzymatic components present in the composition. In liquid or gel compositions, the surfactant is most preferably formulated such that it promotes, or at least does not disrupt, the stability of any enzyme in these compositions.
Polyoxyethylene, polyoxypropylene and polyoxybutylene condensates of alkyl phenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyoxyethylene condensates being preferred. These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, in either a straight chain or branched chain configuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to about 2 to about 25 moles, more preferably, per mole of alkylphenolPreferably from about 3 to about 15 moles of ethylene oxide. Commercially available nonionic surfactants of this type include Igepal sold by the GAF companyTMC0-630 from Rohm&Triton sold by Haas corporationTMX-45, X-114, X-100 and X-102. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkylphenol ethoxylates).
Condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant system of the present inventionA surfactant. The alkyl chain of the aliphatic alcohol can be straight or branched, primary or secondary, and typically contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, more preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide per mole of alcohol. From about 2 to about 7 moles of ethylene oxide, most preferably from 2 to 5 moles of ethylene oxide, per mole of alcohol in the condensation product. Examples of commercially available nonionic surfactants of this type include TergitolTM15-S-9(C11-C15Condensation products of linear alcohols with 9 moles of ethylene oxide), TergitolTM24-L-6NMW (C with narrow molecular weight distribution)12-C14Condensation products of primary alcohols with 6 moles of ethylene oxide), all sold by Union carbonization); neodolTM45-9(C14-C15Condensation products of linear alcohols with 9 moles of ethylene oxide), NeodolTM23-3(C12-C13Condensation products of linear alcohols with 3.0 moles of ethylene oxide), NeodolTM45-7(C14-C15Condensation products of linear alcohols with 7 moles of ethylene oxide), NeodolTM45-5(C14-C15Condensation products of linear alcohols with 5 moles of ethylene oxide), all sold by shell chemical company, KyroTMEOB(C13-C15Condensation product of an alcohol with 9 moles of ethylene oxide), from Procter&Gamble; and GenapolLA030 or 050 (C)12-C14Condensation products of alcohols with 3 or 5 moles of ethylene oxide), sold by Hoechst. The preferred HLB range for these products is from 8 to 11, most preferably from 8 to 10.
Nonionic surfactants that can also be used as the surfactant system of the present invention are the alkyl polysaccharides disclosed in US4565647 to lleado, issued on 21/1/1986, which contain a hydrophobic group of from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms, and polysaccharides containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units, such as the polyglycoside hydrophilic group. Any reducing saccharide containing 5 or 6 carbon atoms can be used, for example glucose, galactose and galactosyl groups can be used instead of glucosyl groups (the hydrophobic group is selectively attached at 2-, 3-, 4-, etc. positions, resulting in glucose or galactose as opposed to glucoside or galactoside). The intersaccharide linkage may be, for example, between one position of the added saccharide unit and the 2-, 3-, 4-, and/or 6-position of the preceding saccharide unit.
Preferred alkylpolyglycosides have the formula:
R2O(CnH2nO)t(sugar base)xWherein R is2Selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof, wherein the alkyl group contains from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is 0 to about 10, preferably 0; x is from about 1.3 to about 10, preferably from about 1.3 to about 3, and most preferably from about 1.3 to about 2.7. The glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpolyethoxy alcohol is first formed and then reacted with glucose or a source of glucose to form the glucoside (attachment at the 1-position). The additional glycosyl groups can then be attached between their 1-position and the preceding glycosyl units 2-, 3-, 4-and/or 6-position, preferably predominantly in the 2-position.
The condensation products of ethylene oxide with hydrophobic groups formed by the condensation of propylene oxide with propylene glycol are also suitable for use as the additional nonionic surfactant system of the present invention. The hydrophobic portion of these compounds preferably has a molecular weight of from about 1500 to about 1800 and exhibits water insolubility. The addition of polyoxyethylene groups to the hydrophobic portion will increase the water solubility of the molecule as a whole, and the liquid character of the product is maintained to a polyoxyethylene content of about 50% of the total weight of the condensation product, which corresponds to condensation of up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain commercially available PlurafacTMLF404 and PluronicTMSurfactants, all sold by BASF.
Nonionic surfactants that are also suitable for use as the nonionic surfactant system of the present invention are the condensation products of ethylene oxide with the product obtained by reacting propylene oxide with ethylenediamine. The hydrophobic groups of these products consist of the reaction product of ethylenediamine and excess propylene oxide, and generally have a molecular weight of from about 2500 to about 3000. The hydrophobic group is condensed with ethylene oxide to give a condensed productThe composition contains about 40% to about 80% by weight polyoxyethylene and has a molecular weight of about 5000 to about 11000. Examples of this type of nonionic surfactant include certain commercially available Tetronic surfactantsTMCompound, sold by BASF.
Preferred nonionic surfactants for use as the surfactant system of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide, alkyl polysaccharides, and mixtures thereof. Most preferably C containing 3 to 15 ethoxy groups8-C14Alkylphenol ethoxylates and C containing 2-10 ethoxy groups8-C18Alcohol ethoxylate (preferably average C)10) And mixtures thereof.
Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula:
R2-C(O)-N(R1) -Z wherein R1Is H, or R1Is C1-4Hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl or mixtures thereof, R2Is C5-31A hydrocarbon group, and Z is a linear hydrocarbon group having at least 3 hydroxyl groups directly bonded theretoChain polyhydroxyhydrocarbyl groups, or alkoxylated derivatives thereof. Preferably R1Is methyl, R2Is straight chain C11-15Alkyl or C16-18Alkyl or alkenyl chains, such as coconut oil alkyl or mixtures thereof, and Z is obtained in a reductive amination reaction from a reducing sugar, such as glucose, fructose, maltose, lactose.
Suitable anionic surfactants which may be used are linear alkylbenzene sulphonate, alkyl ester sulphonate surfactants including C8-C20Linear esters of carboxylic acids (i.e.fatty acids) which have been sulfonated with gaseous sulfur trioxide according to the method of the American Petroleum chemical society, 52(1975), pages 323-329. Suitable starting materials would include natural fatty materials derived from tallow, palm oil, and the like.
Preferred alkyl ester sulfonate surfactants, especially for laundry applications, include alkyl ester sulfonate surfactants of the formula:
R3-CH(SO3M)-C(O)-OR4wherein R is3Is C8-C20Hydrocarbyl, preferably alkyl or combinations thereof, R4Is C1-C6A hydrocarbyl group, preferably an alkyl group or a combination thereof, and M is a cation which forms a water soluble salt with the alkyl ester sulfonic acid. Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations such as monoethanolamine, diethanolamine, and triethanolamine. Preferably R3Is C10-C16Alkyl, and R4Is methyl, ethyl or isopropyl. Especially preferred is where R3Is C10-C16Alkyl methyl ester sulfonates.
Other suitable anionic surfactants include alkyl sulfate surfactants which are of the formula ROSO3Water soluble salts or acids of M, wherein R is preferably C10-C24Hydrocarbyl, preferably containing C10-C20Alkyl or hydroxyalkyl of the alkyl moiety, more preferably C12-C18Alkyl or hydroxyalkyl, M is H or a cation, such as an alkali metal cation (e.g., sodium, potassium, lithium), or ammonium or substituted ammonium (methyl-, dimethyl-, and trimethyl-ammonium cations and quaternary ammonium cations, such as tetramethyl-ammonium and dimethyl piperidinium cations and quaternary ammonium cations derived from alkylamines, such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like). For low wash temperatures (e.g., below about 50 ℃), C is generally preferred12-C16Alkyl chain of (a), preferably C for higher washing temperatures (e.g., greater than about 50 deg.C)16-18An alkyl chain.
Other anionic surfactants suitable for use in laundry applications may also be included in the laundry detergent and/or fabric care compositions of the present invention. They may include soap salts (including, for example, sodium, potassium, ammonium and substituted ammonium salts such as mono-, di-and triethanolamine salts), C8-C22Primary or secondary alkanesulfonates, C8-C24Olefin sulfonates, preparation of pyrolysis products by sulfonation of alkaline earth metal citrates as described, for example, in GB1082179Prepared sulfonated polycarboxylic acid, C8-C24Alkyl radicalPolyethylene glycol ether sulfates (containing up to 10 moles of ethylene oxide); alkyl glyceryl sulphonates, fatty acyl glyceryl sulphonates, fatty oil acyl glyceryl sulphates, alkylphenol ethylene oxide ether sulphates, paraffin sulphonates, alkyl phosphates, isethionates, e.g. acyl isethionates, N-acyl taurates, alkyl succinamates and sulphosuccinates, sulphosuccinate monoesters (especially saturated and unsaturated C's)12-C18Monoesters) and sulfosuccinate diesters (especially saturated and unsaturated C's)6-C12Diesters), acyl sarcosinates, sulfates of alkyl polysaccharides, e.g. alkyl polyglucoside sulfates (non-ionic unsulfated compounds described below), branched primary alkyl sulfates and alkyl polyethoxy carboxylates, e.g. of the formula RO (CH)2CH2O)k-CH2COO-M+Wherein R is C8-C22Alkyl, k is an integer from 1 to 10, and M is a cation which forms a soluble salt. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil.
Other examples are described in "surfactants and detergents" (Vol.I and II, Schwartz, Perry and Berch). Various such surfactants are also generally described in US3929678 to Laughlin et al, issued on 30/12/1975, column 23, line 58 to column 29, line 23 (incorporated herein by reference).
If included, the laundry detergent and/or fabric care compositions of the present invention typically contain from about 1% to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants.
A highly preferred anionic surfactant comprising an alkyl alkoxylated sulphate surfactant is of the formula RO (A)mSO3Water soluble salts or acids of M, wherein R is unsubstituted C10-C24Alkyl or containing C10-C24Hydroxyalkyl of the alkyl moiety, preferably C12-C20Alkyl or hydroxyalkyl, more preferably C12-C18Alkyl or hydroxyalkyl, a is ethoxy or propoxy units, M is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3, M is H or a cation which may be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or a substituted ammonium cation. Alkyl ethoxylated sulfates and alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl-, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and cations derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. An exemplary surfactant is C12-C18Alkyl polyethoxylate (1.0) sulfate (C)12-C18E(1.0)M)、C12-C18Alkyl polyethoxylate (2.25) sulfate (C)12-C18E(2.25)M)、C12-C18Alkyl polyethoxylate (3.0) sulfate (C)12-C18E (3.0) M) and C12-C18Alkyl polyethoxylate (4.0) sulfate (C)12-C18E (4.0) M), where M is typicallySelected from sodium and potassium.
The laundry detergent and/or fabric care compositions of the present invention may also contain amphoteric, zwitterionic and semi-polar surfactants as well as nonionic and/or anionic surfactants other than those already described above.
Amphoteric surfactants are also suitable for use in the detergent compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight or branched chain. One of the aliphatic substituents contains at least about 8 carbon atoms, usually from about 8 to about 18 carbon atoms and at least one contains an anionic water-solubilizing group, e.g., carboxy, sulfonate, sulfate. See US3929678 to Laughlin et al, issued on 30/12/1975, column 19, lines 18-35, for illustrative amphoteric surfactants.
If included, the laundry detergent and/or fabric care compositions of the present invention typically contain from 0.2% to about 15%, preferably from about 1% to about 10% by weight of the amphoteric surfactant.
Zwitterionic surfactants are also suitable for use in laundry detergent and/or fabric care compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines or heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See US3929678 to Laughlin et al, issued on 30/12/1975, column 19, lines 38-22, lines 48, for illustrative zwitterionic surfactants.
If included, the laundry detergent and/or fabric care compositions of the present invention typically contain from 0.2% to about 15%, preferably from about 1% to about 10% by weight of the zwitterionic surfactant.
Semi-polar nonionic surfactants are a particular class of nonionic surfactants comprising a water-soluble amine oxide containing one alkyl group of from about 10 to about 18 carbon atoms and two moieties selected from the group consisting of alkyl and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and two moieties selected from the group consisting of alkyl and hydroxyalkyl moieties containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and one moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.
Semi-polar nonionic detergent surfactants include amine oxide surfactants having the formula:
Figure A9881021800371
wherein R is3Is an alkyl, hydroxyalkyl or alkylphenyl group containing from about 8 to about 22 carbon atoms; r4Is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof; x is 0 to about 3; each R5Is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyoxyethylene group containing from about 1 to about 3 ethylene oxide groups. R5The groups may be linked to each other, for example, through oxygen or nitrogen atoms to form a ring structure.
These amine oxide surfactants include, inter alia, C10-C18Alkyl dimethyl amine oxide and C8-C12Alkoxyethyl dihydroxyethyl amine oxide.
If included, the cleaning compositions of the present invention generally contain from 0.2% to about 15%, preferably from about 1% to about 10%, by weight, of a semi-polar nonionic surfactant.
The laundry detergent and/or fabric care compositions of the present invention may also contain a co-surfactant selected from primary or tertiary amines.
Suitable primary amines for use in the present invention include formula R1NH2Wherein R is1Is C6-C12Preferably C6-C10Alkyl chain or R4X(CH2)nX is-O-, -C (O) NH-or-NH-, R4Is C6-C12Alkyl chains, n is 1 to 5, preferably 3. R1The alkyl chain may be straight or branched and may be interrupted by up to 12, preferably less than 5, ethylene oxide moieties.
The preferred amines of the above formula of the present invention are n-alkylamines. Suitable amines for use in the present invention are selected from the group consisting of 1-hexylamine, 1-octylamine, 1-decane and laurylamine. Other preferred primary amines include C8-G10Oxypropylamine, octyloxypropylamine, 2-ethylhexyloxypropylamine, laurylamidopropylamine and acylaminopropylamine.
Suitable tertiary amines for use in the present invention include those having the formula R1R2R3Tertiary amines of N, in which R1And R2Is C1-C8Alkyl chain or
Figure A9881021800372
R3Is C6-C12Preferably C6-C10Alkyl chain or R3Is R4X(CH2)nAnd X is-O-, -C (O) NH-or-NH-, R4Is C4-C12And n is 1 to 5, preferably 2 to 3. R5Is H or C1-C2Alkyl and x are 1-6.
R3And R4May be straight or branched; r3The alkyl chain may be interrupted by up to 12, preferably less than 5, ethylene oxide moieties.
Preferably the tertiary amine is R1R2R3N, wherein R1Is C6-C12Alkyl chain, R2And R3Is C1-C3Alkyl or
Figure A9881021800381
Wherein R is5Is H or methyl and x ═ 1-2.
Also preferred are amidoamines of the formula:
Figure A9881021800382
wherein R is1Is C6-C12An alkyl group; n is 2 to 4, preferably n is 3; r2And R3Is C1-C4。
The most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, C8-C10Oxypropylamine, N-cocoanut oil 1, 3 diaminopropane, cocoanut oil alkyldimethylamine, lauryl dimethylamine, lauryl bis (hydroxyethyl) amine, cocoanut oil bis (hydroxyethyl) amine, 2 moles propoxylated laurylamine, 2 moles propoxylated octylamine, lauryl amidopropyl dimethylamine, C8-C10Acylamidopropyldimethylamine and C10Amidopropyl dimethylamine.
The most preferred amines for use in the compositions of the present invention are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Particularly suitable are n-dodecyldimethylamine and dihydroxyethyl cocoalkylamine and the 7-fold ethoxylated oleyl amine, lauryl amidopropylamine and cocoamidopropylamine. Bleaching agent
The laundry detergent and/or fabric care compositions of the present invention may also comprise bleaching agents such as hydrogen peroxide, PB1, PB4 and percarbonate having a particle size of 400-800 microns. These bleach components may include one or more oxygen bleaches and, depending on the bleach selected, one or more bleach activators. The oxygen bleaching compound, if present, is typically present at a level of from about 1% to about 25%.
The bleach component for use in the present invention may be any bleach used in laundry detergent and/or fabric care compositions, including oxygen bleaches as well as other bleaches known in the art. The bleaching agents suitable for use in the present invention may be activated or unactivated bleaching agents.
One type of oxygen bleaching agent that may be used includes percarboxylic acid bleaching agents and salts thereof. Suitable examples of such bleaches include magnesium monoperoxyphthalate hexahydrate, the magnesium salt of m-chloroperbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaches are disclosed in US4483781, US patent application 740446, EP0133354 and US 4412934. Highly preferred bleaches also include 6-nonanamido-6-oxoperoxyhexanoic acid as described in US 4634551.
Another class of bleaching agents that can be used includes halogen bleaches. Examples of hypohalite bleaching agents include, for example, trichloroisocyanuric acid and dichloroisocyanuric acid sodium and potassium and N-chloro and N-bromo alkane sulfonamides. This material is generally added in an amount of 0.5-10% by weight, preferably 1-5% by weight, based on the weight of the final product.
The hydrogen peroxide releasing agent may be used in combination with a bleach activator, such as Tetraacetylethylenediamine (TAED), nonanoyloxybenzenesulfonate (NOBS, described in US 4412934), 3, 5, -trimethylhexanoyloxybenzenesulfonate (ISONOBS, described in EP 120591) or Pentaacetylglucose (PAG) or N-nonanoyl-6-aminocaproic acid phenolsulfonate (NACA-OBS, described in WO 94/28106), which are perhydrolyzed to form a peracid as the active bleaching species, resulting in improved bleaching. Also suitable as bleach activators are acylated citrates, as disclosed, for example, in pending European patent application 91870207.7, in Procter&Gamble's unexamined patent applications US 60/022786(1996 application No. 7/30) and 60/028122(1996 application No. 10/15) disclose asymmetric acyclic imide bleach activators of the formula:wherein R is1Is C7-C13Linear or branched saturated or unsaturated alkyl, R2Is C1-C8Linear or branched saturated or unsaturated alkyl and R3Is C1-C4Linear or branched, saturated or unsaturated alkyl.
Useful bleaching agents for use in the laundry detergent and/or fabric care compositions of the present invention, including peroxyacids and bleaching systems comprising a bleach activator and a peroxygen bleaching compound, are described in our co-pending applications USSN08/136626, PCT/US95/07823, WO95/27772, WO95/27773, WO95/27774 and WO 95/27775.
The hydrogen peroxide may also be present by adding an enzymatic system (i.e. the enzyme and its substrate) which is capable of generating hydrogen peroxide at the beginning or during the washing and/or rinsing process. This enzyme system is disclosed in EP patent application 91202655.6, filed on 9/10/1991.
Metal-containing catalysts for use in bleach compositions include cobalt-containing catalysts, such as pentamine cobalt (III) acetate salts, and manganese-containing catalysts, such as the compounds described in EPA549271, EPA549272, EPA458397, US5246621, EPA458398, US5194416 and US 5114611. Bleaching compositions comprising a peroxygen compound, a manganese-containing bleach catalyst and a chelating agent are described in patent application No. 94870206.3.
Bleaching agents other than oxygen bleaching agents are also known in the art and may be used in the present invention. One non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as sulfonated zinc and/or aluminum phthalocyanines. These substances can deposit on the substrate during the washing process. The sulfonated zinc phthalocyanine is activated and subsequently the substrate is bleached, under light irradiation and in the presence of oxygen, for example, when the garment is dried by hanging it in sunlight. Preferred zinc phthalocyanine and photoactivated bleaching processes are described in US 4033718. Laundry detergent and/or fabric care compositions will typically contain from about 0.025% to about 1.25% by weight of a sulfonated zinc phthalocyanine. Builder system
The laundry detergent and/or fabric care compositions of the present invention may also contain a builder. The laundry detergent and/or fabric care compositions of the present invention will preferably contain a builder selected from zeolites, sodium tripolyphosphate and/or layered silicates. We have surprisingly found that said compositions additionally containing a builder selected from zeolites, sodium tripolyphosphate and/or layered silicates provide improved wash and softening performance.
Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates, alkyl or alkenyl succinic acids and fatty acids, materials such as ethylenediamine tetraacetate, diethylenetriamine pentamethylene acetate, metal ion sequestrants such as aminopolyphosphonates, especially ethylenediamine tetramethylene phosphonic acid and diethylenetriamine pentamethylene phosphonic acid. Phosphate builders may also be used in the present invention.
Suitable builders can be inorganic ion exchange materials, typically inorganic hydrated aluminosilicate materials, more particularly hydrated synthetic zeolites such as hydrated zeolite A, X, B, HS or MAP.
Other suitable inorganic builder materials are layered silicates, for example SKS-6 (Hoechst). SKS-6 is made of sodium silicate (Na)2Si2O5) A crystalline layered silicate of composition.
Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and their ether derivatives as disclosed in belgian patents 831368, 821369 and 821370. Polycarboxylates containing two carboxyl groups include the water-soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, maleic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid and the ether carboxylates described in DE2446686 and 2446687 and US3935257 and the sulfinyl carboxylates described in belgian patent 840623. Polycarboxylates containing three carboxyl groups include in particular the water-soluble citrates, aconitates and citraconates and succinate derivatives, for example carboxymethoxysuccinates as described in GB1379241, lactoxysuccinates as described in Netherlands application 7205873 and oxypolycarboxylate substances as described in GB1387447, for example 2-oxa-1, 1, 3-propane tricarboxylate.
Polycarboxylates containing four carboxy groups include oxydisuccinates, 1, 2, 2-ethane tetracarboxylates, 1, 3, 3-propane tetracarboxylates and 1, 1, 2, 3-propane tetracarboxylates as disclosed in GB 1261829. Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in GB1398421 and 1398422 and US3936448 and the sulphonated pyrolysed citrates described in GB1082179, whilst polycarboxylates containing phosphine substituents are disclosed in GB 1439000.
Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis, cis-tetracarboxylates, cyclopentadiene (cyclopentadienide) pentacarboxylates, 2, 3, 4, 5-tetrahydrofuran-cis, cis-tetracarboxylates, 2, 5-tetrahydrofuran-cis-dicarboxylates, 2, 5, 5-tetrahydrofuran tetracarboxylates, 1, 2, 3, 4, 5, 6-hexane hexacarboxylates and carboxymethyl derivatives of polyhydric alcohols, such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include mellitic, pyromellitic and phthalic acid derivatives as disclosed in GB 1425343.
Among them, preferred polycarboxylates are hydroxycarboxylic acid salts containing up to three carboxyl groups per molecule, more particularly citrates.
Preferred builder systems for use in the compositions of the present invention include mixtures of a water-insoluble aluminosilicate builder, such as zeolite A or layered silicate (SKS-6), and a water-soluble carboxylate chelating agent, such as citric acid. Other preferred builder systems include mixtures of water-insoluble aluminosilicate builders, for example zeolite a, and water-soluble carboxylate chelating agents, for example citric acid. Preferred builder systems for use in the liquid laundry detergent and/or fabric care compositions of the present invention include soaps and polycarboxylates.
Other builder materials which may form part of the builder system for the particulate composition include inorganic materials such as alkali metal carbonates, bicarbonates, silicates and organic materials such as the organic phosphonates, aminopolyalkylene phosphonates and aminopolycarboxylates.
Other suitable water-soluble organic salts are homo-or co-polymeric acids or their salts, wherein the polycarboxylic acid contains at least two carboxyl groups separated from each other by not more than two carbon atoms. Polymers of this type are disclosed in GB-A-1596756. Examples of such salts are polyacrylates of MW2000-5000 and their copolymers with maleic anhydride, which copolymers have a molecular weight of 20000-70000, in particular about 40000.
Detergent builder salts are typically present in an amount of from 5% to 80%, preferably from 10% to 70%, most commonly from 30% to 60% by weight of the composition. Conventional detergent enzymes
In addition to the mannanase enzyme, the laundry detergent and/or fabric care compositions may also contain one or more enzymes which provide wash performance, fabric care and/or hygiene benefits. The laundry detergent and/or fabric care compositions of the present invention will preferably also contain cellulase. We have surprisingly found that the compositions additionally comprising cellulase provide improved wash and softening performance.
The enzyme comprises an enzyme selected from the group consisting of cellulase, hemicellulase, peroxidase, protease, glucoamylase, amylase, xylanase, lipase, phospholipase, phosphatase, esterase, cutinase, pectinase, keratinase, reductase, oxidase, phenoloxidase, lipoxygenase, ligninase, pullulanase, tannase, pentosanase, malic enzyme, β -glucanase, arabinosidase, hyaluronidase, chondroitinase, laccase, and mixtures thereof.
Preferred combinations are laundry detergent and/or fabric care compositions containing a mixture of a conventionally applied enzyme, such as a protease, amylase, lipase, cutinase and/or cellulase in combination with one or more plant cell wall degrading enzymes.
Suitable proteases are subtilisins (subtilisin BPN and BPN') obtained from particular strains of Bacillus subtilis and Bacillus licheniformis. A suitable protease is obtained from a specific strain of Bacillus having maximum activity over the entire pH range of 8-12, developed by Novo Industries A/S (Denmark) and sold as ESPERASE @, hereinafter referred to as "Novo". The preparation of this and similar enzymes is described in Novo, GB 1243784. Other suitable proteases include ALCALASE, DURAZYM and SAVINASE obtained from Novo and MAXATASE, MAXALASE, MAXALCAL, PROPERASE and MAXALE PEPEPEME (protein engineered Maxacal) obtained from Gist-Brocades. Proteolytic enzymes also include modified bacterial serine proteases, such as those described in European patent application 87303761.8 (especially pages 17, 24 and 98) filed on 28.4.1987, which is referred to herein as "protease B" and EP199404 to Venegas published on 29.10.1986, which relates to modified bacterial serine proteases, which is referred to herein as "protease A". Suitable is a protease referred to herein as "protease C", which is a variant of the alkaline serine protease from Bacillus, in which lysine is substituted for arginine at position 27, tyrosine for valine at position 104, serine for asparagine at position 123 and alanine for threonine at position 274. Protease C EP90915958.4, published 16.5.1991, corresponds to that described in WO 91/06637. Genetically modified variants, in particular those of protease C, are also encompassed by the invention.
Preferred proteases referred to as "protease D" are carbonyl hydrolase variants having an amino acid sequence not found in nature, as described in WO95/10591 and the patent application entitled "protease-containing bleaching composition" by C.Ghosh et al, 1994, Ser. No. 10/13, by substituting various amino acid residues with different amino acids at the + 76-equivalent positions in the above-mentioned carbonyl hydrolases, and preferably also the combined substitution corresponds to the substitution at one or more amino acid residues selected from the group consisting of positions +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265 and/or +274 in accordance with Bacillus amyloliquefaciens subtilisin. Also suitable are carbonyl hydrolase variants of the proteases described in WO95/10591 which have been modified by substitution of various amino acid residues at the position corresponding to +210 of the precursor enzyme in combination with one or more of the following residues: +33, +62, +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, +218, and +222, where the numbered positions correspond to naturally occurring subtilisin from Bacillus amyloliquefaciens or to the corresponding amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin (unexamined patent application US serial No. 60/048550, filed on 6/4/1997).
Also suitable for use in the present invention are the proteases described in EP251446 and WO91/06637, the protease BLAP described in WO91/02792 and their variants described in WO 95/23221.
See also WO93/18140A to Novo for a high pH protease from Bacillus NCIMB 40338. WO92/03529A to Novo describes enzyme-added detergents comprising a protease, one or more other enzymes and a reversible protease inhibitor. If desired, proteases with reduced absorption and improved hydrolysis can be obtained as described in WO95/07791 to Procter & Gamble. WO94/25583 to Novo describes a recombinant trypsin-like protease suitable for use in the detergents of the invention. Other suitable proteases are described in EP516200 to Unilever.
Proteolytic enzymes are incorporated in the laundry detergent and/or fabric care compositions of the invention at levels of from 0.0001% to 2%, preferably from 0.001% to 0.2%, more preferably from 0.005% to 0.1% pure enzyme by weight of the composition.
Cellulases for use in the present invention include bacterial or fungal cellulases. They preferably have a pH optimum of between 5 and 12 and a specific activity of more than 50CEVU/mg (cellulose viscosity units). Suitable cellulases are described in US4435307, J61078384 and WO96/02653 to Barbesgoard et al, which disclose fungal cellulases produced by Humicola insolens, Trichoderma (Trichoderma), rhizopus (Thielavia) and sporothrix (Sporotrichum), respectively. EP739982 describes cellulases isolated from novel bacillus species. Suitable cellulases are also disclosed in GB-A-2075028, GB-A-2095275, DE-OS-2247832 and WO 95/26398.
An example of such a cellulase is the cellulase produced by a strain of Humicola insolens (Humicola griseavar. thermophili dea), especially the Humicola strain DSM 1800.
Other suitable cellulases are cellulases having a molecular weight of about 50kDa, an isoelectric point of 5.5 and containing 415 amino acids obtained from Humicola insolens; and a 43kD endoglucanase exhibiting cellulase activity obtained from Humicola insolens DSM 1800; a preferred endoglucanase component has an amino acid sequence disclosed in PCT patent application WO 91/17243. Also suitable are the EGIII cellulases derived from Trichoderma longibrachiatum as described in WO94/21801 of Genencor, published on 29/9 of 1994. Especially suitable cellulases are the cellulases having color care benefits. An example of such a cellulase is the cellulase described in EP patent application No. 91202879.2(Novo) filed on 6.11.1991. Carezyme and Celluzyme (Novo Nordisk A/S) are particularly useful. See also WO91/17244 and WO 91/21801. Other suitable cellulases for use in fabric care and/or cleaning performance are described in WO96/34092, WO96/17994 and WO 95/24471.
The cellulase is typically incorporated into the laundry detergent and/or fabric care composition at a level of from 0.0001% to 2% pure enzyme by weight of the laundry detergent and/or fabric care composition.
Peroxidases are used in combination with a source of oxygen, such as percarbonate, perborate, persulfate, hydrogen peroxide, etc., and a phenolic substrate which acts as a bleach booster molecule. They are used for "solution bleaching", i.e. to avoid the transfer of dyes or pigments removed from the substrate during the washing operation to other substrates in the wash solution. Peroxidases are known in the art and include, for example, horseradish peroxidase, ligninase and haloperoxidase, such as chloro-and bromo-peroxidase. Laundry detergent and/or fabric care compositions comprising peroxidase enzymes are disclosed, for example, in PCT International applications WO89/099813, WO89/09813 and European patent application EP91202882.6, filed 11/6/1991 and EP No 96870013.8 filed 2/20/1996. Also suitable are laccases.
The synergist is typically present at a level of from 0.1% to 5% by weight of the total composition. Preferred synergists are substituted phenothiazines and phenoxazines, 10-phenothiazinepropionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-methylphenoxaziridine (described in W094/12621) and substituted syringates (C3-C5 substituted alkyl syringates) and phenols. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide.
Such peroxidases are typically incorporated in laundry detergent and/or fabric care compositions at levels of from 0.0001% to 2% pure enzyme by weight of the laundry detergent and/or fabric care composition.
Other preferred enzymes which may be included in the laundry detergent and/or fabric care compositions of the present invention include lipases. Suitable lipases for detergent use include those derived from microorganisms of the genus Pseudomonas, such as Pseudomonas stutzeri ATCC19.154 as disclosed in GB 1372034. Suitable lipases include those which show a positive immunological cross-reaction with the lipase antibody, which are produced by the microorganism Pseudomonas fluorescens IAM 1057. This lipase is available from Amano pharmaceutical Co.Ltd. (Nagoya, Japan) under the trade name lipase P "Amano", hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, lipase from Chromobacterium viscosum such as Toyo Jozo Co. (Tagata, Japan) Chromobacterium viscosum var.lipolyticum NRRLB 3673; chromobacter viscosum lipases from U.S. Biochemical Corp. (US) and Disoynth (Netherlands); and lipase derived from Pseudomonas gladioli. Particularly suitable lipases are lipases, for example M1 LipaseRAnd LipomaxR(Gist-Broxades) and LipolaseRAnd Lipolase UltraR(Novo), which have been found to be very effective when used in combination with the compositions of the present invention. Also suitable are the lipolytic enzymes described in EP258068, WO92/05249 and WO95/22615 of Novo Nordisk and WO94/03578, WO95/35381 and WO96/00292 of Unilever.
Also suitable are cutinases [ EC3.1.1.50], which are considered to be a special class of lipases, i.e.lipases which do not require interfacial activation. The addition of cutinases to laundry detergent and/or fabric care compositions is described, for example, in WO-A-88/09367 (Genencor); WO90/09446 (plantagenic System) and WO94/14963 and WO94/14964 (Unilever).
The lipase and/or cutinase are typically incorporated into the laundry detergent and/or fabric care compositions at levels of from 0.0001% to 2% pure enzyme by weight of the laundry detergent and/or fabric care composition.
Amylases (α and/or β) may be included to remove carbohydrate-based stains WO94/02597 to Novo Nordisk A/S published on 3.2.1994 describes laundry detergent and/or fabric care compositions incorporating mutant amylases also see WO95/10603 to Novo Nordisk A/S published on 20.4.1995 other amylases known for use in detergent compositions including α -and β -amylases α -amylases are known in the prior art and include those described in US5003257, EP 666, WO 91/48353, FR2676456, EP285123, EP525610, EP368341 and GB1296839 (Novo). other suitable amylases are described in WO94/18314 to 8.18.1994 to Genencor and those described in WO96/05295 to 1996 and WO 05225/05295 to Novo Nordisk A/363970 and those described in Novo WO 2.3.3.2/26873 and WO 26873 to improve the stability of Novo Nordisk A/363970 and WO 26873 to Novo Nordisk A/363970.
Examples of commercial α -amylase products are Purafect OxAM and Termamyl, Ban, Fungamyl and Duramyl, available from Genencor, both from NovoNordisk A/S Danish WO95/26397 describes other suitable amylases α -amylase which are characterized by a specific activity in the temperature range of 25 ℃ to 55 ℃ and at a pH of 8 to 10, which is at least 25% higher than the specific activity of Termamyl, determined by the Phadebas α -amylase activity test.
The amylolytic enzymes are incorporated in the laundry detergent and/or fabric care compositions of the present invention at a level of from 0.0001% to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition.
The enzyme may be of any suitable origin, for example of plant, animal, bacterial, fungal and yeast origin. The source may also be mesophilic or extremophilic conditions (psychrophilic, thermophilic, barotropic, alkalophilic, acidophilic, halophilic, etc.). These enzymes can be used in pure or impure form. At present, it is common practice to modify wild-type enzymes via protein/radical engineering techniques to optimize their performance efficiency in laundry detergent and/or fabric care compositions of the present invention. For example, variants can be designed to increase the compatibility of the enzyme with components commonly encountered in such compositions. Furthermore, the variants can be designed such that the optimum pH, bleach or chelant stability, catalytic activity, etc. of the enzyme variant can be tailored to a particular wash application.
In the case of bleach stability, particular attention should be paid to oxidation-sensitive amino acids, and to surface charge for surfactant compatibility. The isoelectric point of such enzymes can be modified by substitution of certain charged amino acids, for example increasing the isoelectric point will help to improve compatibility with anionic surfactants. The stability of the enzyme can be further improved by creating, for example, additional salt bridges, while enhancing the calcium binding sites to increase chelator stability. Cellulases are of particular interest, as most cellulases have separate binding domains (CBS). The properties of this enzyme can be altered by modifications in these domains.
The enzyme is incorporated into laundry detergent and/or fabric care compositions at levels of from 0.0001% to 2% pure enzyme by weight of the laundry detergent and/or fabric care composition. The enzymes may be added as a single component (pellets, granules, stabilized liquids, etc. containing one enzyme) or as a mixture of two or more enzymes (e.g. a complex granule).
Other suitable detergent ingredients which may be added are enzymatic oxidation scavengers, described in co-pending European patent application 92870048.6 filed on.1.31.1992. An example of such an enzymatic oxidation scavenger is ethoxylated tetraethylene polyamine.
WO9307263A and WO9307260A to Genencor International, WO8908694A to Novo, and US3553139 to McCarty et al, issued on 5.1.1971, also describe various enzyme materials and methods for their incorporation into synthetic detergent compositions. Enzymes are further disclosed in US4101457 to Place et al, published 1978 at 18 and US4507219 to Hughes, published 1985 at 26. US4261868 to Hora et al, issued 4, 14, 1981, discloses raw stocks for liquid wash formulations, and methods of their incorporation into such formulations. Enzymes used in detergents can be stabilized in various ways. Enzyme stabilization techniques are disclosed and exemplified in US3600319 by Gedge et al, published 8/17 1971, and in EP199405 and EP200586 by Venegas, 10/29 1986. Enzyme stabilization systems are also described, for example, in US 3519570. WO9401532A to Novo describes useful Bacillus AC13 that enables proteases, xylanases and cellulases. Color care and fabric care effects
Techniques for providing types of color care effects may also be included. Examples of such techniques are organometallic catalysts for color protection. The organometallic catalyst is described in pending european patent application 92870181.2. Dye fixatives, polyolefin dispersants for wrinkle resistance and improved water adsorption capacity, perfumes and amino-functional polymers for color care treatment and perfume substantivity (PCT/US97/16546) are further examples of color care/fabric care technology and are described in pending patent application No. 96870140.9, filed on 7/11/1996.
Fabric softeners may also be added to the laundry detergent and/or fabric care compositions of the present invention. These substances may be of inorganic or organic type. Organic fabric softeners include water-insoluble tertiary amines as described in GB-A1514276 and EP-B0011340, mixtures of these with mono-C12-C14 quaternary ammonium salts as disclosed in EP-B-0026527 and EP-B-0026528, and di-long chain amides as disclosed in EP-B0242919. Other useful organic components of the fabric softener system include the high molecular weight polyethylene oxide materials disclosed in EP-a0299575 and 0313146.
Organic fabric softeners such as water insoluble tertiary amines or dilong chain amide materials are added in amounts of 0.5% to 5%, usually 1% to 3% by weight, while high molecular weight polyethylene oxide materials and water soluble cationic materials are added in amounts of 0.1% to 2%, usually 0.15% to 1.5% by weight. These materials are typically added to the spray-dried portion of the composition, although in some cases they may be more conveniently added as dry-blended granules or sprayed onto other solid components of the composition as a molten liquid. Chelating agents
The laundry detergent and/or fabric care compositions of the present invention may optionally further comprise one or more iron and/or manganese chelating agents. Such chelating agents may be selected from the group consisting of amino carboxylates, amino phosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures thereof, as hereinafter defined. While not wishing to be bound by theory, it is believed that the effectiveness of these materials is due in part to their superior ability to remove iron and manganese ions from the wash liquor by forming soluble chelates.
Aminocarboxylates useful as optional chelating agents include ethylenediaminetetraacetate, N-hydroxyethylethylenediaminetriacetate, nitrilotriacetate, ethylenediaminetetrapropionate, triethylenetetramine hexaacetate, diethylenetriaminepentaacetate and ethanoldiglycine, alkali metal, ammonium, and substituted ammonium salts thereof and mixtures thereof.
Amino phosphonates are also suitable for use as chelating agents in the compositions of the present invention when at least a minimum level of total phosphorus is permitted in the detergent composition and include ethylenediamine tetra (methylene phosphonate), DEQUEST. These amino phosphonates preferably do not contain alkyl or alkenyl groups with more than about 6 carbon atoms.
Polyfunctionally substituted aromatic chelating agents are also suitable for use in the compositions of the present invention. See Connor et al, US3812044, issued 5, 21, 1974. Preferred compounds of this type in the acid state are dihydroxydisulfobenzenes, such as 1, 2-dihydroxy-3, 5-disulfobenzene.
The preferred biodegradable chelants for use in the present invention are ethylenediamine disuccinate ("EDDS"), particularly the [ S, S ] isomer, disclosed in US4704233 to Hartman and Perkins, issued 11/3 1987.
The compositions of the present invention may also contain a water-soluble methylglycine diacetic acid (MGDA) salt (or acid form) for use as a chelating agent or co-builder with, for example, insoluble builders, such as zeolites, layered silicates and the like.
If used, these chelants typically comprise from about 0.1% to about 15% by weight of the laundry detergent and/or fabric care compositions of the present invention. More preferably, these chelating agents, if used, comprise from about 0.1% to about 3.0% by weight of the composition. Suds suppressor
Another optional component is a suds suppressor, such as a polysiloxane and silica-polysiloxane mixture. Polysiloxanes can be generally represented as alkylated polysiloxane materials, while silica is generally used in finely divided forms, such as various types of silica aerosols, xerogels, and hydrophobic silicas. These materials may be incorporated as granules, wherein the suds suppressor is advantageously releasably incorporated in a water-soluble or water-dispersible, non-surfactant detergent substantially impermeable carrier. In addition, the suds suppressor may be dissolved or dispersed in a liquid carrier and added by spraying onto one or more of the other components. Preferred silicone foam control agents are disclosed in US3933672 to Bartollota et al. Other particularly suitable suds suppressors are the self-emulsifying silicone suds suppressors described in DTOS2646126, published on day 4/28 1977. An example of such a compound is DC-544, commercially available from Dow Corning, which is a polysiloxane-ethylene glycol copolymer. Particularly preferred foam control agents are suds suppressor systems comprising a mixture of silicone oil and 2-alkyl alkanol. A suitable 2-alkyl-alkanol is 2-butyloctanol, which is commercially available under the trade name Isofol 12R.
The suds suppressor system is described in pending European patent application 92870174.7 filed on.11/10 1992.
Particularly preferred silicone foam control agents are described in the pending European patent application 92201649.8. The composition may contain fumed non-porous silica, e.g. AerosilRA combined polysiloxane/silica mixture.
The suds suppressors described above are generally used at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight. Others
Other components used in laundry detergent and/or fabric care compositions may be used, such as soil suspending agents, soil release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, colorants and/or encapsulated or unencapsulated perfumes.
Particularly suitable encapsulating materials are water-soluble capsules consisting of a matrix of polysaccharide and polyol as described in GB 1464616. Other suitable water-soluble encapsulating materials include dextrins obtained from ungelatinized starch acid esters of substituted dicarboxylic acids as described in US 3455838. These acid ester dextrins are preferably prepared from starches, such as soft corn, soft sorghum, sago, tapioca and potato. Suitable examples of such encapsulation materials include N-Lok, manufactured by national starch. The N-Lok capsule encapsulating material consists of modified corn starch and glucose. The starch is modified by the addition of monofunctional substituent groups, such as octenyl succinic anhydride.
Suitable anti-redeposition and soil suspension agents of the present invention include cellulose derivatives such as methyl cellulose, carboxymethyl cellulose and homo-or copolymers of hydroxyethyl cellulose and polycarboxylic acids or salts thereof. Polymers of this type include the previously mentioned polyacrylates and maleic anhydride-acrylic acid copolymers as builders, and copolymers of maleic anhydride with ethylene, methyl vinyl ether or methacrylic acid, the maleic anhydride comprising at least 20 mole percent of the copolymer. These materials are generally used in amounts of 0.5% to 10% by weight, more preferably 0.75% to 8%, most preferably 1% to 6% by weight of the composition.
Preferred optical brighteners are anionic in character, examples being 4, 4' -bis- (2-ethylamino-4-anilino-s-triazin-6-ylamino) stilbene-2: disodium 2 'disulfonate, 4' -bis- (2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2: disodium 2 'disulfonate, 4' -bis- (2, 4-dianilino-s-triazin-6-ylamino) stilbene-2: disodium 2 'disulfonate, 4', 4 ″ -bis- (2, 4-dianilino-s-triazin-6-ylamino) stilbene-2: 2 'monosodium disulfonate, 4' -bis- (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene-2: disodium 2 'disulfonate, 4' -bis- (4-phenyl-2, 1, 3-triazol-2-yl) stilbene-2: disodium 2 'disulfonate, 4' -bis- (2-anilino-4- (1-methyl-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene-2: disodium 2 'disulfonate, sodium 2- (stilbenyl-4' - (naphtho-1 ', 2': 4, 5) -1, 2, 3-triazole-2 '-sulfonate and 4, 4' -bis (2-sulfostyryl) biphenyl a highly preferred brightener is the specific brightener disclosed in EP 753567.
Other useful polymers are polyethylene glycols, especially those having a molecular weight of 1000-. They are used in amounts of 0.20% to 5%, more preferably 0.25% to 2.5% by weight. These polymers and the above mentioned homo-or co-polymeric polycarboxylates are valuable in improving whiteness maintenance, fabric dust deposition and cleaning performance on clay, protein and oxidizable soils in the presence of transition metal impurities.
Soil release agents useful in the compositions of the present invention are conventional copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are described in commonly assigned US4116885 and 4711730 and EP 0272033. According to EP-A-0272033, particularly preferred polymers have the formulｃA:
(CH3(PEG)43)0.75(POH)0.25[T-PO)2.8(T-PEG)0.4]T(POH)0.25((PEG)43CH3)0.75wherein PEG is- (OC)2H4) O-, PO is (OC)3H6O) and T are (pcOC)6H4CO)。
Also useful are modified polyesters such as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol, and 1-2 propylene glycol, the end groups consisting primarily of sulfobenzoate and secondarily of monoesters of ethylene glycol and/or propylene glycol. The goal is to obtain a polymer capped at both ends with sulfobenzoate, and in the present invention, most of the above copolymers of the present invention are "predominantly" capped with sulfobenzoate. However, some copolymers will not be fully capped and, thus, their end groups may consist of monoesters of ethylene glycol and/or propylene 1-2 glycol, which "secondarily" constitute the material.
The selected polyester of the present invention contains about 46% by weight dimethyl terephthalate, about 16% by weight propane-1, 2 diol, about 10% by weight ethylene glycol, about 13% by weight dimethyl sulfobenzoate, and about 15% by weight sulfoisophthalic acid having a molecular weight of about 3000. Polyesters and their preparation are described in detail in EPA 311342.
It is known in the art that free chlorine present in tap water rapidly inactivates enzymes present in detergent compositions. Thus, the use of chlorine scavengers such as perborate, ammonium sulphate, sodium sulphite or polyethyleneimine in the formulation at levels above 0.1% by weight of the total composition will provide improved stability of the detergent enzyme during the wash process. Compositions containing chlorine scavengers are described in european patent application 92870018.6 filed on 31.1.1992.
Alkoxylated polycarboxylates prepared from polyacrylates are useful herein to provideAdditional grease removal performance. This material is described on page 4 and below of WO91/08281 and PCT90/01815, which are incorporated herein by reference. Chemically these materials include polyacrylates having an ethoxy side chain per 7-8 acrylate units. The side chain has the formula- (CH)2CH2O)m(CH2)nCH3Wherein m is 2 to 3 and n is 6 to 12. The pendant chain esters are attached to the polyacrylate "backbone" to provide a "comb" polymeric structure. The molecular weight can vary, but is typically from about 2000 to about 50000. The alkoxylated polycarboxylates may comprise from about 0.05% to about 10% by weight of the present compositions. Dispersing agent
The laundry detergent and/or fabric care compositions of the present invention may also contain a dispersant: suitable water-soluble organic salts are homo-or co-polymeric acids or salts thereof, wherein the polycarboxylic acid contains at least two carboxyl groups separated from each other by not more than two carbon atoms. Polymers of this type are disclosed in GB-A-1596756. Examples of such salts are polyacrylates of MW2000-5000 and their copolymers with maleic anhydride, which have a molecular weight of 1000-100000.
Especially copolymers of acrylates and methacrylates, for example 480N having a molecular weight of 4000, may be incorporated in the laundry detergent and/or fabric care compositions of the invention at a level of from 0.5 to 20% by weight of the composition.
The compositions of the present invention may contain a lime soap peptiser compound having a Lime Soap Dispersancy (LSDP) of not more than 8, preferably not more than 7, most preferably not more than 6, as defined below. The lime soap peptizer compound is preferably present in an amount of 0% to 20% by weight.
Various measurements of lime soap peptizer effect are given by lime soap peptizer capacity (LSDP), which is determined by using the lime soap dispersion test described in the articles h.c. borghetty and c.a. bergman, j.am.oil.chem.soc. volume 27, pages 88-90. This calcium soap dispersion test method is widely used by practitioners in the art, and is relevant, for example, to the following review articles; linfield, Surfactant science series, volume 7, page 3; W.N.Linfield, Tenside surf.det. volume 27, pages 159-163 (1990) and M.K.Nagarajan, W.F.Masler, Cosmetics and Toiletries, volumes 104, pages 71-73 (1989). LSDP is the% weight ratio of dispersant to sodium oleate required to disperse a lime soap precipitate formed from 0.025g of sodium oleate in 30ml of water having 333ppm calcium carbonate equivalent hardness (ca: mg ═ 3: 2).
Surfactants with good lime soap peptizing ability include certain amine oxides, betaines, sulfobetaines, alkyl ethoxy sulfates, and ethoxylated alcohols.
Examples of the surfactant having an LSDP of not more than 8 for use in the present invention include C16-C18Dimethylamine oxide, C having an average degree of ethoxylation of from 1 to 512-C18Alkyl ethoxy sulfates, especially C having an average degree of ethoxylation of 312-C15Alkyl ethoxy sulfate surfactant (LSDP ═ 4) and C with average degree of ethoxylation of 12(LSDP ═ 6) or 3014-C15Ethoxylated alcohols, sold by BASF GmbH under the trade names Lutensol a012 and Lutensol a030, respectively.
Polymeric lime soap peptizers suitable for use in the present invention are described in an article by M.K. Nagarajan, W.F. Masler in Cosmetics and Toiletries, Vol.104, pp.71-73 (1989).
Hydrophobic bleaching agents such as 4- [ N-octanoyl-6-aminocaproyl ] benzenesulfonate, 4- [ N-nonanoyl-6-aminocaproyl ] benzenesulfonate, 4- [ N-decanoyl-6-aminocaproyl ] benzenesulfonate and mixtures thereof and nonanoyloxybenzenesulfonate together with hydrophilic/hydrophobic bleach formulations may also be used as lime soap peptizer compounds. Dye transfer inhibition
The laundry detergent and/or fabric care compositions of the present invention also contain compounds which inhibit the transfer of dissolved and suspended dyes from one fabric to another encountered during laundering operations involving colored fabrics. Polymeric dye transfer inhibitors
The laundry detergent and/or fabric care compositions of the present invention also contain from 0.001% to 10%, preferably from 0.01% to 2%, more preferably from 0.05% to 1% by weight of a polymeric dye transfer inhibiting agent. The polymeric dye transfer inhibiting agents are typically added to laundry detergent and/or fabric care compositions in order to inhibit the transfer of dyes from colored fabrics to other fabrics laundered therewith. The polymer has the ability to complex or adsorb fugitive dyes washed out of dyed fabrics during the washing process before the dyes have the opportunity to contact other items.
Particularly suitable polymeric dye transfer inhibiting agents are polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
The addition of the polymer also improves the performance of the enzyme of the invention. a) Polyamine N-oxide polymers
Suitable polyamine N-oxide polymers contain units having the following structural formula:
Figure A9881021800541
wherein P is a polymerizable unit to which an R-N-O group may be attached or wherein an R-N-O group forms part of the polymerizable unit or a combination of both. A is
Figure A9881021800542
-O-, -S-, -N-; x is O or 1; r is an aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic group or any combination thereof to which the nitrogen of the N-O group may be attached or wherein the nitrogen of the N-O group is part of these groups.
The N-O group can be represented by the following general structural formula:
Figure A9881021800543
wherein R1, R2 and R3 are aliphatic, aromatic, heterocyclic or alicyclic groups or combinations thereof, and x or/and y or/and z is 0 or 1, wherein the nitrogen of the N-O group may be attached thereto or wherein the nitrogen of the N-O group forms part of these groups.
The N-O group may be part of the polymerizable unit (P) or may be attached to the polymeric backbone or a combination of both.
Suitable polyamine N-oxides wherein the N-O group forms part of the polymerizable unit include polyamine N-oxides wherein R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups.
One class of the above-described polyamine N-oxides comprises a group of polyamine N-oxides wherein the nitrogen of the N-O group forms part of the R-group. Preferred polyamine N-oxides are compounds wherein R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof.
Another class of the foregoing polyamine N-oxides comprises the class of polyamine N-oxides wherein the nitrogen of the N-O group is attached to the R group.
Other suitable polyamine N-oxides are polyamine oxides wherein the N-O group is attached to a polymerizable unit.
A preferred class of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group wherein the nitrogen of the N-O functionality is part of said R group.
Examples of such compounds are polyamine oxides, wherein R is a heterocyclic compound, such as pyridine, pyrrole, imidazole and derivatives thereof.
Another preferred class of polyamine N-oxides are polyamine oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic group wherein the nitrogen of the N-O functional group is attached to said R group.
Examples of such compounds are polyamine oxides, wherein the R groups may be aromatic, such as phenyl.
Any polymer backbone can be used so long as the amine oxide polymer formed is water soluble and has dye transfer inhibiting properties. Examples of suitable polymeric backbones are polyethylenes, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates and mixtures thereof.
Typically, the amine N-oxide polymers of the present invention have an amine to amine N-oxide ratio of from 10: 1 to 1: 1000000. However, the amount of amine oxide groups present in the polyamine oxide polymer can be varied by suitable copolymerization or by a suitable degree of N-oxidation. The ratio of amine to amine N-oxide is preferably from 2: 3 to 1: 1000000, more preferably from 1: 4 to 1: 1000000, and most preferably from 1: 7 to 1: 1000000. The polymers of the present invention actually include random or block copolymers in which one monomer type is an amine N-oxide and the other monomer type is an amine N-oxide or not. The amine oxide units of the polyamine N-oxide have a pKa < 10, preferably a pKa < 7, more preferably a pKa < 6.
Polyamine oxides can be obtained in almost any degree of polymerization. The degree of polymerization is not critical, so long as the material has the desired water solubility and dye suspending ability.
The average molecular weight is generally 500-1000000; preferably 1000-. b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole
The N-vinylimidazole N-vinylpyrrolidone polymer used in the present invention has an average molecular weight of 5000-.
Highly preferred polymers for use in the detergent compositions of the present invention include polymers selected from N-vinylimidazole N-vinylpyrrolidone copolymers wherein the polymer has an average molecular weight of 5000-.
The average molecular weight range is determined by light scattering as described in Barth H.G. and Mays J.W. Chemicals 113, volume, "modern methods of Polymer characterization".
Highly preferred N-vinylimidazole N-vinylpyrrolidone copolymers have 5000-; more preferably 8000-; most preferably 10000-.
N-vinylimidazole N-vinylpyrrolidone copolymers characterized by the above average molecular weight provide excellent dye transfer inhibition properties without adversely affecting the cleaning performance of detergent compositions formulated therewith.
The N-vinylimidazole N-vinylpyrrolidone copolymers of the present invention have a molar ratio of N-vinylimidazole to N-vinylpyrrolidone of from 1 to 0.2, more preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4. c) Polyvinyl pyrrolidone
The laundry detergent and/or fabric care compositions of the present invention may also employ polyvinylpyrrolidone ("PVP") having an average molecular weight of from about 2500 to about 400000, preferably from about 5000 to about 200000, more preferably from about 5000 to about 50000, most preferably from about 5000 to about 15000. Suitable polyvinylpyrrolidones are commercially available from ISP Corporation, New York, NY and Montreal, Canada under the product names PVP K-15 (viscosity molecular weight 10000), PVP K-30 (average molecular weight 40000), PVP K-60 (average molecular weight 160000) and PVP K-90 (average molecular weight 360000). Other suitable polyvinylpyrrolidones commercially available from BASF corporation include Sokalan HP165 and Sokalan HP 12; polyvinylpyrrolidones known to the person skilled in the art of detergents (see, for example, EP-A-262897 and EP-A-256696). d) Polyvinyl oxazolidinone:
the laundry detergent and/or fabric care compositions of the present invention may also use a polyvinyl oxazolidinone as a polymeric dye transfer inhibitor. The polyvinyl oxazolidinones have an average molecular weight of from about 2500 to about 400000, preferably from about 5000 to about 200000, more preferably from about 5000 to about 50000, most preferably from about 5000 to about 15000. e) Polyvinyl imidazole:
the laundry detergent and/or fabric care compositions of the present invention may also use polyvinylimidazoles as polymeric dye transfer inhibitors. The polyvinylimidazole has an average molecular weight of from about 2500 to about 400000, preferably from about 5000 to about 200000, more preferably from about 5000 to about 50000, most preferably from about 5000 to about 15000. f) Crosslinked polymer:
crosslinked polymers are polymers whose backbones are linked to one another to some extent; these linkages may be chemical or physical in nature, possibly with reactive groups on the backbone or branches; crosslinked polymers are described in journal of Polymer science 22, page 1035-1039. In one embodiment, the crosslinked polymers are prepared in such a way that they form a three-dimensional rigid structure that is capable of trapping the dye in the pores formed by the three-dimensional structure. In another embodiment, the crosslinked polymer captures the dye by swelling. Such crosslinked polymers are described in pending patent application 94870213.9. Washing method
The compositions of the present invention can be used in essentially any washing or cleaning process that includes a soaking process, a pretreatment process, and a rinse step process where a separate rinse aid composition can be added.
The process described herein comprises contacting the fabric with a wash solution in the manner generally and hereinafter described. The process of the invention is generally carried out in a washing process. The washing process is preferably carried out at from 5 ℃ to 95 ℃ and in particular at from 10 ℃ to 60 ℃. The pH of the treatment solution is preferably 7 to 12.
The following examples are intended to illustrate the compositions of the present invention without limiting or otherwise defining the scope of the invention. In laundry detergent and/or fabric care compositions, the level of enzyme is expressed as pure enzyme by weight of the total composition, unless otherwise indicated, the detergent components are expressed by weight of the total composition. The abbreviated component symbols have the following meanings: and (3) LAS: straight chain C11-13Sodium alkylbenzenesulfonate TAS: tallow alkyl sodium sulfate CxyAS: c1x-C1ySodium alkyl sulfate cxyssa: c1x-C1ySodium secondary (2, 3) alkyl sulfate CxyEz: c condensed with an average of z moles of ethylene oxide1x-C1yPrimary, predominantly linear alcohols CxyEzS: c condensed with an average of z moles of ethylene oxide1x-C1ySodium alkyl sulfate QAS: r2+N+(CH3)2(C2H4OH)，R2＝C12-C14QAS1 ：R2+N+(CH3)2(C2H4OH)，R2＝C8-C11APA ：C8-10Acylamidopropyl dimethylamineSoap: straight chain alkyl derived from 80/20 mixture of tallow and coconut oil fatty acids
Sodium carboxylate nonionic surfactant: c13-C15Mixed ethoxylated/propoxylated fatty alcohols, average ethoxylation range
Degree 3.8, average degree of propoxylation 4.5Neodol 45-13: c14-C15Linear primary alcohol ethoxylates, STS marketed by Shell Chemical CO: sodium toluenesulfonate CFAA: c12-C14Alkyl N-methylglucamide TFAA: c16-C18Alkyl N-methylglucamide TPKFA: c12-C14Topping full-distillate fatty acid silicates: amorphous sodium Silicate (SiO)2∶Na2O ratio 1.6-3.2) metasilicate: sodium metasilicate (SiO)2∶Na2O ratio 1.0) zeolite a: formula Na12(AlO2SiO2)12.27H2Hydrated sodium aluminosilicate of O, primary particle size
0.1-10 microns (weight expressed on an anhydrous basis) NaSKS-6: of the formula delta-Na2Si2O5The crystalline layered silicate citrate of (4): trisodium citrate dihydrate with 86.4% activity, particle size distribution 425-
Micron citric acid: anhydrous citric acid borate salt: sodium borate carbonate: anhydrous sodium carbonate, particle size 200-: anhydrous sodium bicarbonate, particle size distribution 400-: anhydrous sodium sulfate magnesium sulfate: anhydrous magnesium sulfate STPP: sodium tripolyphosphate TSPP: tetrasodium pyrophosphate MA/AA: 4: 1 acrylate/maleate random copolymer having an average molecular weight of about 70000-
80000 MA/AAl: 6: 4 acrylate/maleate random copolymer having an average molecular weight of about 10000 AA: sodium polyacrylate polymer PA30 with average molecular weight of 4500: polyacrylic acid 480N having an average molecular weight of about 4500-: 7: 3 acrylate/methacrylate random copolymer having an average molecular weight of about
3500 Polygel/carbopol: high molecular weight crosslinked polyacrylatesPB 1: anhydrous sodium perborate monohydrate, nominal formula: NaBO2.H2O2PB 4: sodium perborate tetrahydrate, nominal formula: NaBO2.3H2O.H2O2Percarbonate salts: anhydrous sodium percarbonate, nominal formula: 2Na2CO3.3H2O2NaDCC: sodium dichloroisocyanurate TAED: tetraacetylethylenediamine NOBS: nonanoyloxybenzene sulfonate, sodium salt form NACA-OBS: (6-nonanoylaminocaproyl) oxybenzenesulfonate DTPA: HEDP of diethylene triamine pentaacetic acid: 1, 1-hydroxyethane diphosphonic acid DETPMP: diethyltriaminepenta (methylene phosphonate) available from Monsanto under the trade name Dequest
2060 marketing EDDS: ethylenediamine-N, N' -disuccinic acid, (S, S) isomer, sodium salt form MnTACN: 1, 4, 7-trimethyl-1, 4, 7-triazacyclononane manganese photoactivated bleaching agent: photoactivation of bleach 1 with sulfonated zinc phthalocyanine encapsulated with dextrin-soluble polymer: sulfonated aluminum phthalocyanine PAAC encapsulated with dextrin-soluble polymer: pentamine cobalt (III) acetate salt paraffin wax: paraffin oil NaBz sold by Wintershall under the trade mark Winog 70: sodium benzoate BzP: benzoyl peroxide mannanase: mannanase protease from Bacillus agaradherens, NCIMB 40482: under the trade name Savinase, Alcalase, Durazym (Novo Nordisk)
A/S), Maxacal, Maxapem (Gist-Brocades) sold as proteolytic enzyme
Enzymes and the enzymes described in patents WO91/06637 and/or WO95/10591 and/or EP251446
The protease amylase described in (1): commercially available from Genencor as described in WO94/18314, WO96/05295
Amylolytic enzyme sold under the name Purafact Oxam @, Novo Nordisk
Termamyl, Fungamyl and Duramyl A/S and Duramyl-
Those amylolytic enzymes lipase described in WO 95/26397: under the trade names Lipolase, Lipolase Ultra from Novo Nordisk A/S
And the lipolytic enzyme cellulase sold by Gist Brocades as Lipomax: by Novo Nordisk A/S under the trade names Carezyme, Celluzyme and-
Or cellulolytic enzyme clay sold by endosase: smectite or bentonite CMC: sodium carboxymethylcellulose (PVP): polyvinyl polymer having an average molecular weight of 60000 PVNO: polyvinylpyridine-N-oxide with an average molecular weight of 50000 PVPVI: copolymer of alkenyl imidazole and vinyl pyrrolidone, having an average molecular weight of 20000 brightener 1: disodium 4, 4' -bis (2-sulfostyryl) biphenyl brightener 2: 4, 4' -bis (4-anilino-6-morpholino-1, 3, 5-triazine 2-yl) stilbene-2: 2' -
Disodium disulfonate polysiloxane defoamer: polydimethylsiloxane foams containing siloxane oxyalkylene copolymers as dispersants
A foam control agent, the ratio of the foam control agent to the dispersant is 10: 1-
100: 1 suds suppressor: 12% polysiloxane/silica, 18% stearyl alcohol, 70% starch, in granular form
A sunscreen of the formula: aqueous based mixture of monostyrene latexes from BASF Aktiengesellschaft
SRP1 sold under the trade name Lytron 621: anionic end-capped polyester SRP 2: diethoxylated poly (1, 2-trimethylene terephthalate) short block polymer QEA: bis ((C)2H5O)(C2H4O)n)(CH3)-N+-C6H12-N+-(CH3) Bis ((C)2H5O)-(C2H4O))nWherein n-20-30 PEI: polyethyleneimine, average molecular weight 1800, average degree of ethoxylation 7 SCS: sodium cumene sulfonate HMWPEO: high molecular weight polyethylene oxide PEGx: polyethylene glycol, molecular weight xPEO: polyethylene oxide, average molecular weight 5000 TEPAE: tetraethylenepentamine ethoxylateExample 1
The following detergent compositions of the invention were prepared:
III blown powder
Zeolite A13.013.015.0
Sulfate-3.0-
LAS 3.0 3.0 3.0
QAS - 1.5 1.5
DETPMP 0.4 0.2 0.4
EDDS - 0.4 0.2
CMC 0.4 0.4 0.4
MA/AA 4.02.02.0 agglomerates
LAS 5.0 5.0 5.0
TAS 2.0 1.0 1.0
Silicate 3.02.04.0
Zeolite A8.08.08.0
Carbonate 7.04.04.0 spray liquid
Fragrance 0.30.30.3
C45E7 2.0 2.0 2.0
C25E32.0 Dry additive
Citrate 3.0-2.0
Bicarbonate-3.0-
Carbonate 8.015.010.0
TAED 6.0 2.0 5.0
PB1 9.0 7.0 10.0
PEO - - 0.2
Bentonite 10.010.010.0
Mannanase 0.0010.0010.02
Protease 0.030.030.03
Lipase 0.0080.0080.008
Cellulase 0.0010.0010.001
Amylase 0.010.010.01 Silicone antifoam 5.05.05.0
sulfate-3.0-Density (g/l) 850850850 Trace and minor ingredients Up to 100% example 2
The following liquid detergent compositions according to the invention were prepared (the contents are given in parts by weight and the enzymes are expressed as pure enzymes):
i II III IV LAS 25.0.0- - -C25 AS-13.016.013.0C 25E 3S-2.02.04.0C 25E 7- -4.04.0 TFAA-6.06.06.0 APA 3.01.02.0-TPKFA-14.011.011.0 citric acid 1.01.01.01.0 dodecenyl/tetradecyl 15.0- - -alkenyl succinic rapeseed fatty acid 1.0-3.5-ethanol 7.02.03.02.01, 2 propylene glycol 6.08.010.013.0 monoethanolamine- -9.09.0 TEPAE- -0.40.3 DETPPMP 2.01.21.0-mannanase 0.0010.0020.020.001 protease 0.080.020.010.02 lipase- -0.0030.003 amylase 0.0040.010.010.01 cellulase- -0.0040.003 SRP 2- -0.20.1 boric acid 1.01.52.52.5 bentonite 4.05.04.04.0 brightener 10.10.20.3-foam suppressor 0.4- - -
Opacifier 0.80.7-
Sodium hydroxide Up to pH 8.07.58.08.2
Micro-ingredients and moisture example 3
The following granular fabric detergent compositions of the invention are prepared which provide a "softening in the wash" effect:
I II
C45AS - 10.0
LAS 7.6 -
C68AS 1.3 -
C45E7 4.0 -
C25E3 - 5.0
cocosanyl-dimethyl-hydroxyethylammonium chloride 1.41.0
Citrate 5.03.0
NaSKS-6 - 11.0
Zeolite A15.015.0
MA/AA 4.0 4.0
DETPMP 0.4 0.4
PB1 15.0 -
Percarbonate-15.0
TAED 5.0 5.0
Smectite clay 10.010.0
HMWPEO - 0.1
Mannanase 0.0010.02
Protease 0.020.01
Lipase 0.020.01
Amylase 0.030.005
Cellulase 0.001-
Silicate 3.05.0
Carbonate 10.010.0
Suds suppressor 1.04.0
CMC 0.2 0.1
Minor and minor Components Up to 100% example 4
The following laundry bar detergent compositions according to the invention were prepared (contents are given in parts by weight, enzymes are expressed as pure enzymes):
i II III IV V VI VII VIIILAS-19.015.021.06.758.8-C28 AS 26.013.5-15.7511.222.5 sodium laurate 2.59.0-zeolite A2.01.25-1.251.251.25 carbonate 20.03.013.08.010.015.013.08.0 calcium carbonate 27.539.031.0-36.0-36.0 sulfate 5.05.03.05.03.0-5.0 TSPP 5.0-5.02.5-STPP 5.015.010.0-7.08.010.0 bentonite 4.010.04.04.05.04.04.04.0 DETPP-0.70.6-0.60.70.70.7 CMC-1.01.01.01.0-1.0 slide-10.011.010.0-silicate-4.05.03.0-PVNO 0.020.03-0.01-0.02-MA/AA 0.41.0-0.20.40.50.4 SRP10.30.30.30.30.30.30.30.3 mannanase 0.0010.0010.020.0010.020.030.010.001 amylase-0.01-0.002-0.004-0.0030.003-0.003-0.002-0.002-cellulase-0003-0003.0002- - PEO-0.2-0.20.3-0.3 spice 1.00.50.30.20.4-0.4 magnesium sulfate-3.03.03.0-brightener 0.150.10.15-0.1 photoactivated bleach-15.015.015.015.0-15.0 agent (ppm)
Sequence listing (1) general information: the applicant: name: the Procter & Gamble Company street: one Procter & Gamble Plaza City: sincinatide, OHIO country: USA zip code: 45202 invention name: detergent composition containing mannanase and clay numbered: 6 computer-readable form: type of medium: a floppy disk computer: compatible with IBM PC operating system: PC-DOS/MS-DOS software: patentln Release #1.0Version 1.25(EPO) SEQ ID NO: 1 sequence characteristics: length: 1407 base pair type: nucleic acid strand type: single topology: linear molecular type: original source characteristics of genomic DNA: name/keyword: CDS location: 1-1482 sequence description: SEQ ID NO: 1ATGAAAAAAAAGTTATCACAGATTTATCATTTAATTATTTGCACACTTATAATAAGTGTGGGAATAATGGGGATTACAACGTCCCCATCAGCAGCAAGTACAGGCTTTTATGTTGATGGCAATACGTTATATGACGCAAATGGGCAGCCATTTGTCATGAGAGGTATTAACCATGGACATGCTTGGTATAAAGACACCGCTTCAACAGCTATTCCTGCCATTGCAGAGCAAGGCGCCAACACGATTCGTATTGTTTTATCAGATGGCGGTCAATGGGAAAAAGACGACATTGACACCATTCGTGAAGTCATTGAGCTTGCGGAGCAAAATAAAATGGTGGCTGTCGTTGAAGTTCATGATGCCACGGGTCGCGATTCGCGCAGTGATTTAAATCGAGCCGTTGATTATTGGATAGAAATGAAAGATGCGCTTATCGGTAAAGAAGATACGGTTATTATTAACATTGCAAACGAGTGGTATGGGAGTTGGGATGGCTCAGCTTGGGCCGATGGCTATATTGATGTCATTCCGAAGCTTCGCGATGCCGGCTTAACACACACCTTAATGGTTGATGCAGCAGGATGGGGGCAATATCCGCAATCTATTCATGATTACGGACAAGATGTGTTTAATGCAGATCCGTTAAAAAATACGATGTTCTCCATCCATATGTATGAGTATGCTGGTGGTGATGCTAACACTGTTAGATCAAATATTGATAGAGTCATAGATCAAGACCTTGCTCTCGTAATAGGTGAATTCGGTCATAGACATACTGATGGTGATGTTGATGAAGATACAATCCTTAGTTATTCTGAAGAAACTGGCACAGGGTGGCTCGCTTGGTCTTGGAAAGGCAACAGTACCGAATGGGACTATTTAGACCTTTCAGAAGACTGGGCTGGTCAACATTTAACTGATTGGGGGAATAGAATTGTCCACGGGGCCGATGGCTTACAGGAAACCTCCAAACCATCCACCGTATTTACAGATGATAACGGTGGTCACCCTGAACCGCCAACTGCTACTACCTTGTATGACTTTGAAGGAAGCACACAAGGGTGGCATGGAAGCAACGTGACCGGTGGCCCTTGGTCCGTAACAGAATGGGGTGCTTCAGGTAACTACTCTTTAAAAGCCGATGTAAATTTAACCTCAAATTCTTCACATGAACTGTATAGTGAACAAAGTCGTAATCTACACGGATACTCTCAGCTCAACGCAACCGTTCGCCATGCCAATTGGGGAAATCCCGGTAATGGCATGAATGCAAGACTTTACGTGAAAACGGGCTCTGATTATACATGGCATAGCGGTCCTTTTACACGTATCAATAGCTCCAACTCAGGAACAACGTTATCTTTTGATTTAAACAACATCGAAAATAGTCATCATGTTAGGGAAATAGGCGTGCAATTTTCAGCGGCAGATAATAGCAGTGGTCAAACTGCTCTATACGTTGATAACGTTACTTTAAGATAGSEQ ID NO: 2, sequence characteristics: length: 493 amino acid types: amino acid topology: linear molecular type: description of the protein sequence: SEQ ID NO: 2MKKKLSQIYHLIICTLIISVGIMGITTSPSAASTGFYVDGNTLYDANGQPFVMRGINHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAEQNKMVAWEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYGSWDGSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFNADPLKNTMFSIHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDVDEDTILSYSEETGTGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIVHGADGLQETSKPSTVFTDDNGGHPEPPTATTLYDFEGSTQGWHGSNVTGGPWSVTEWGASGNYSLKADVNLTSNSSHELYSEQSRNLHGYSQLNATVRHANWGNPGNGMNARLYVKTGSDYTWHSGPFTRINSSNSGTTLSFDLNNIENSHHVREIGVQFSAADNSSGQTALYVDNVTLRSEQ ID NO: 3, sequence characteristics: length: 1407 base pair type: nucleic acid strand type: single topology: linear molecular type: description of genomic DNA sequence: SEQ ID NO: 3ATGAAAAAAAAGTTATCACAGATTTATCATTTAATTATTTGCACACTTATAATAAGTGTGGGAATAATGGGGATTACAACGTCCCCATCAGCAGCAAGTACAGGCTTTTATGTTGATGGCAATACGTTATATGACGCAAATGGGCAGCCATTTGTCATGAGAGGTATTAACCATGGACATGCTTGGTATAAAGACACCGCTTCAACAGCTATTCCTGCCATTGCAGAGCAAGGCGCCAACACGATTCGTATTGTTTTATCAGATGGCGGTCAATGGGAAAAAGACGACATTGACACCATTCGTGAAGTCATTGAGCTTGCGGAGCAAAATAAAATGGTGGCTGTCGTTGAAGTTCATGATGCCACGGGTCGCGATTCGCGCAGTGATTTAAATCGAGCCGTTGATTATTGGATAGAAATGAAAGATGCGCTTATCGGTAAAGAAGATACGGTTATTATTAACATTGCAAACGAGTGGTATGGGAGTTGGGATGGCTCAGCTTGGGCCGATGGCTATATTGATGTCATTCCGAAGCTTCGCGATGCCGGCTTAACACACACCTTAATGGTTGATGCAGCAGGATGGGGGCAATATCCGCAATCTATTCATGATTACGGACAAGATGTGTTTAATGCAGATCCGTTAAAAAATACGATGTTCTCCATCCATATGTATGAGTATGCTGGTGGTGATGCTAACACTGTTAGATCAAATATTGATAGAGTCATAGATCAAGACCTTGCTCTCGTAATAGGTGAATTCGGTCATAGACATACTGATGGTGATGTTGATGAAGATACAATCCTTAGTTATTCTGAAGAAACTGGCACAGGGTGGCTCGCTTGGTCTTGGAAAGGCAACAGTACCGAATGGGACTATTTAGACCTTTCAGAAGACTGGGCTGGTCAACATTTAACTGATTGGGGGAATAGAATTGTCCACGGGGCCGATGGCTTACAGGAAACCTCCAAACCATCCACCGTATTTACAGATGATAACGGTGGTCACCCTGAACCGCCAACTGCTACTACCTTGTATGACTTTGAAGGAAGCACACAAGGGTGGCATGGAAGCAACGTGACCGGTGGCCCTTGGTCCGTAACAGAATGGGGTGCTTCAGGTAACTACTCTTTAAAAGCCGATGTAAATTTAACCTCAAATTCTTCACATGAACTGTATAGTGAACAAAGTCGTAATCTACACGGATACTCTCAGCTCAACGCAACCGTTCGCCATGCCAATTGGGGAAATCCCGGTAATGGCATGAATGCAAGACTTTACGTGAAAACGGGCTCTGATTATACATGGCATAGCGGTCCTTTTACACGTATCAATAGCTCCAACTCAGGAACAACGTTATCTTTTGATTTAAACAACATCGAAAATATCATCATGTTAGGGAAATAGSEQ ID NO: 4, sequence characteristics: length: 468 amino acid types: amino acid topology: linear molecular type: description of the protein sequence: SEQ ID NO: 4MKKKLSQIYHLIICTLIISVGIMGITTSPSAASTGFYVDGNTLYDANGQPFVMRGINHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAEQNKMVAWEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYGSWDGSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFNADPLKNTMFSIHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDVDEDTILSYSEETGTGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIVHGADGLQETSKPSTVFTDDNGGHPEPPTATTLYDFEGSTQGWHGSNVTGGPWSVTEWGASGNYSLKADVNLTSNSSHELYSEQSRNLHGYSQLNATVRHANWGNPGNGMNARLYVKTGSDYTWHSGPFTRINSSNSGTTLSFDLNNIENIIMLGKSEQ ID NO: 5, sequence characteristics: length: 1029 base pair type: nucleic acid strand type: single topology: linear molecular type: description of genomic DNA sequence: SEQ ID NO: 55' AAT TGG CGC ATA CTG TGT CGC CTG TGA ATC CTA ATG CCC AGCAGA CAA CAA AAA CAG TGA TGA ACT GGC TTG CGC ACC TGC CGA ACCGAA CGG AAA ACA GAG TCC TTT CCG GAG CGT TCG GAG GTT ACA GCCATG ACA CAT TTT CTA TGG CTG AGG CTG ATA GAA TCC GAA GCG CCACCG GGC AAT CGC CTG CTA TTT ATG GCT GCG ATT ATG CCA GAG GATGGC TTG AAA CAG CAA ATA TTG AAG ATT CAA TAG ATG TAA GCT GCAACG GCG ATT TAA TGT CGT ATT GGA AAA ATG GCG GAA TTC CGC AAATCA GTT TGC ACC TGG CGA ACC CTG CTT TTC AGT CAG GGC ATT TTAAAA CAC CGA TTA CAA ATG ATC AGT ATA AAA ACA TAT TAG ATT CAGCAA CAG CGG AAG GGA AGC GGC TAA ATG CCA TGC TCA GCA AAA TTGCTG ACG GAC TTC AAG AGT TGG AGA ACC AAG GTG TGC CTG TTC TGTTCA GGC CGC TGC ATG AAA TGA ACG GCG AAT GGT TTT GGT GGG GACTCA CAT CAT ATA ACC AAA AGG ATA ATG AAA GAA TCT CTC TAT ATAAAC AGC TCT ACA AGA AAA TCT ATC ATT ATA TGA CCG ACA CAA GAGGAC TTG ATC ATT TGA TTT GGG TTT ACT CTC CCG ACG CCA ACC GAGATT TTA AAA CTG ATT TTT ACC CGG GCG CGT CTT ACG TGG ATA TTGTCG GAT TAG ATG CGT ATT TTC AAG ATG CCT ACT CGA TCA ATG GATACG ATC AGC TAA CAG CGC TTA ATA AAC CAT TTG CTT TTA CAG AAGTCG GCC CGC AAA CAG CAA ACG GCA GCT TCG ATT ACA GCC TGT TCATCA ATG CAA TAA AAC AAA AAT ATC CTA AAA CCA TTT ACT TTC TGGCAT GGA ATG ATG AAT GGA GCG CAG CAG TAA ACA AGG GTG CTT CAGCTT TAT ATC ATG ACA GCT GGA CAC TCA ACA AGG GAG AAA TAT GGAATG GTG ATT CTT TAA CGC CAA TCG TTG AGT GAA TCC GGG ATC 3' SEQ ID NO: 6, sequence characteristics: length: 363 amino acid types: amino acid topology: linear molecular type: description of the protein sequence: SEQ ID NO: 6ydhT T1 LFKKHTISLLIIFLLASAVLAKPIEAHTVSPVNPNAQQTTKTVMNWLAHL 50ydhT T51 PNRTENRVLSGAFGGYSHDTFSMAEADRIRSATGQSPAIYGCDYARGWLE 100ydhT T101 TANIEDSIDVSCNGDLMSYWKNGGIPQISLHLANPAFQSGHFKTPITNDQ 150ydhT T151 YKNILDSATAEGKRLNAMLSKIADGLQELENQGVPVLFRPLHEMNGEWFW 200ydhT T201 WGLTSYNQKDNERISLYKQLYKKIYHYMTDTRGLDHLIWVYSPDANRDFK 250ydhT T251 TDFYPGASYVDIVGLDAYFQDAYSINGYDQLTALNKPFAFTEVGPQTANG 300ydhT T301 SFDYSLFINAIKQKYPKTIYFLAWNDEWSAAVNKGASALYHDSVVTLNKGE 350ydhT T351 IWNGDSLTPIVE 363

Claims (8)

1. A laundry detergent and/or fabric care composition comprising a laundry detergent and/or fabric care ingredient, a mannanase enzyme and a clay.
2. A laundry detergent and/or fabric care composition according to claim 1 wherein said mannanase is present at a level of from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferably from 0.001% to 0.02% pure enzyme by weight of total composition.
3. A laundry detergent and/or fabric care composition according to claims 1-2 wherein the clay is present at a level of from 0.1% to 50%, preferably from 3% to 25%, more preferably from 4% to 15% by weight of the total composition.
4. A laundry detergent and/or fabric care composition according to claims 1-3 wherein the clay is a smectite, preferably a montmorillonite or hectorite clay having a cation exchange capacity of at least 50meq/100 g.
5. Laundry detergent and/or fabric care compositions according to claims 1-4, further comprising a builder selected from zeolites, sodium tripolyphosphate, layered silicates and/or mixtures thereof.
6. A laundry detergent and/or fabric care composition according to any preceding claim further comprising a cellulase.
7. A laundry detergent and/or fabric care composition according to any preceding claim further comprising a cationic surfactant, preferably a surfactant comprising two long alkyl chains.
8. A method of laundering fabrics with the laundry detergent and/or fabric care composition of any preceding claim.
CN98810218A 1997-08-14 1998-06-10 Detergent compositions comprising mannase and clay Pending CN1276005A (en)

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Application Number Priority Date Filing Date Title
EP97870120A EP0896998A1 (en) 1997-08-14 1997-08-14 Laundry detergent compositions comprising a saccharide gum degrading enzyme
EP97870120.9 1997-08-14

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CN1276005A true CN1276005A (en) 2000-12-06

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CN98810047A Pending CN1336953A (en) 1997-08-14 1998-06-10 Enzymatic cleaning compositions
CN98810231A Pending CN1276824A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannanase and cationic surfactant
CN98810237A Pending CN1276826A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannanase and hydrophobic bleach activator
CN98810049A Pending CN1301294A (en) 1997-08-14 1998-06-10 Laundry detergent compositions comprising a saccharide gum degrading enzyme
CNA988100487A Pending CN1469919A (en) 1997-08-14 1998-06-10 Laundry detergent compositions comprising mannosan enzyme and proteinase
CN98810046A Pending CN1306566A (en) 1997-08-14 1998-06-10 Detergent compsns. comprising mannanase and percarbonate
CN98810236A Pending CN1276825A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannanase and soil release polymer
CN98810218A Pending CN1276005A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannase and clay

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Application Number Title Priority Date Filing Date
CN98810047A Pending CN1336953A (en) 1997-08-14 1998-06-10 Enzymatic cleaning compositions
CN98810231A Pending CN1276824A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannanase and cationic surfactant
CN98810237A Pending CN1276826A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannanase and hydrophobic bleach activator
CN98810049A Pending CN1301294A (en) 1997-08-14 1998-06-10 Laundry detergent compositions comprising a saccharide gum degrading enzyme
CNA988100487A Pending CN1469919A (en) 1997-08-14 1998-06-10 Laundry detergent compositions comprising mannosan enzyme and proteinase
CN98810046A Pending CN1306566A (en) 1997-08-14 1998-06-10 Detergent compsns. comprising mannanase and percarbonate
CN98810236A Pending CN1276825A (en) 1997-08-14 1998-06-10 Detergent compositions comprising mannanase and soil release polymer

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BR (8) BR9811191A (en)
CA (8) CA2301404A1 (en)
CZ (2) CZ2000506A3 (en)
DE (4) DE69826294T2 (en)
DK (1) DK1009795T3 (en)
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HU (1) HUP0003670A3 (en)
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CN107735487A (en) * 2015-06-11 2018-02-23 荷兰联合利华有限公司 Laundry detergent composition
US10941372B2 (en) 2015-06-11 2021-03-09 Conopco, Inc. Laundry detergent composition
CN109477042A (en) * 2016-05-26 2019-03-15 诺维信公司 Purposes, cleaning compositions and the method for washing of enzyme

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