MXPA00001617A - Enzymatic cleaning compositions - Google Patents

Abstract

The present invention relates to laundry detergent compositions comprising a mannanase, and a cleaning and soil release soil release polymer.

Description

DETERGENT COMPOSITIONS CONTAINING A MANANASA AND A CLEARANCE POLYMER OF DIRT FIELD OF THE INVENTION The present invention relates to laundry detergent compositions containing a mannanase and a soil release polymer in cotton. This soil release polymer is a water soluble and / or dispersible modified polyamine having functionalized base portions of the structure and improved stability to the bleach.

BACKGROUND OF THE INVENTION A wide variety of soil release agents are known in the art for use in domestic and industrial fabric treatment processes such as laundry, fabric drying in hot air clothes dryers and the like. Various agents have been marketed to release dirt and are currently used in detergent compositions and in articles and fabric softening / antistatic compositions. Such soil release polymers typically contain a "base structure" of oligomeric or polymeric ester. So far, the development of a cotton-based soil release agent for use in a laundry detergent has been elusive. Attempts made by others to apply the paradigm of combining the structure of a soil-releasing polymer with the structure of the fabric, a useful method in the field of polyester-free soil polymer, have nevertheless yielded marginal results when applies to soil release agents in cotton fabrics. The use of methylcellulose, a cotton polysaccharide with modified oligomer units, proved to be more effective on polyesters than on cotton. For example, document U.K.1, 314,897, published on April 26, 1973, teaches a material based on 10 hydroxypropyl cellulose that prevents the redeposition of wet dirt and improves the release of stains on washed fabrics. The patent E.U.A. No. 3,897,026 issued to Kearney, discloses cellulosic textiles having improved soil release and stain resistance properties obtained by reaction of an ethylene-anhydride copolymer 15 maleic with the hydroxyl portions of the cotton polymers. The patent E.U.A. No. 3,912,681, issued to Dickson shows a composition for applying a non-permanent dirt release finish comprising a polycarboxylate-based polymer to a cotton cloth, at a pH of less than 3. The U.S.A. No. 3,948,838, issued to Hinton et al., Describes 20 polyacrylic polymers of high molecular weight (500,000 to 1, 500,000) to release dirt, preferably used with other cloth treatments. The patent E.U.A. No. 4,559,056, issued to Leigh et al., Discloses a process for treating cotton or synthetic fabrics with a composition ^ - y! t "? -, S > &. ^^^^^ l í ^^^^ -, ^^^^ á ^. ^^ containing an elastomer based on polysiloxane, an agent organosiloxanoxyalkylene-based copolymer interlayer and a catalyst for curing siloxane Other non-terephthalate-containing soil release agents and polyoxyethylene / propylene mixtures are vinylcaprolactam resins as described by Rupert et al in US Patent Nos. 4,579,681 and 4,614,519 Examples of alkoxylated polyamines and quaternized alkoxylated polyamines are described in European Patent Application 206,513 as being suitable for use as dirt dispersants WO97 / 42288 discloses effective soil release agents for cotton articles which can be prepared from certain modified polyamines available for all cotton articles whether they are washed in the presence or absence of a bleaching agent In addition to the aforementioned technique, the following describes various polymers. modified polyamines or dirt releasers: patent E.U.A. No. 5,565,145, Watson et al., Issued October 15, 1996; patent E.U.A. No. 4,548,744, Connor, issued October 22, 1985; patent E.U.A. No. 4,597,898, Van der Meer, issued July 1, 1986; patent E.U.A. No. 4,877,896, Maldonado et al., Issued October 31, 1989; patent E.U.A. No.4,891, 160, Vander Meer, issued on January 2, 1990; patent E.U.A. No. 4,976,879, Maldonado et al., Issued December 11, 1990; patent E.U.A. No. 5,415,807, Gosselink, issued May 16, 1995; patent E.U.A. No. 4,235,735, Marco et al., Issued November 25, 1980; WO95 / 32272, published November 30, 1995; U.K. Patent 1, 537,288 * published on December 29, 1978; U.K. patent 1, 498,520, published on January 18, 1978; German patent DE 28 29 022, issued on January 10, 1980; Japanese document Kokai JP 06313271, published on April 27, 1994. However, the use of such dirt-releasing polymers is not effective enough to protect clothing from the incrustation of stains, in particular from cosmetic and food stains. Indeed, modern cosmetic and food compositions contain more and more additives such as hydrocolloid gums used as thickeners. Mannans, guar gum and carob tree are used in various cosmetic and food compositions (see Industrial Gum, 2nd ed., RL Whistler p.308, Academic Press, 1973, ISBN, 0-12-74-6252-x) . It is known that these hydrocolloid gums have a very high affinity towards cellulose materials and are difficult to remove. Currently, the use of cotton-releasing polymer is not sufficient to try to solve this encrustation of cosmetic / food stains. Food stains and stains and cosmetics represent the majority of stains and soils relevant to the consumer and frequently include food additives such as thickening and stabilizing agents. Actually, hydrocolloid gums and emulsifiers are food additives that are commonly used. The term "gum" denotes a group of industrially useful polysaccharides (long chain polymers) or their derivatives, which are hydrated in hot or cold water = jgj¡¡§? Bf ai a .. ff fltfil-W * - faith »* & HÜ to form viscous solutions, dispersions or gels. The gums are classified as natural or modified. Natural gums include marine plant extracts, plant exudates, seed and root gums and gums obtained by microbial fermentation. Modified (semi-synthetic) gums include cellulose and starch derivatives and certain synthetic gums such as low methoxyl pectin, propylene glycol alginate and carboxymethyl and hydroxypropyl guar gum (Gums in Encvclopedia Chemical Technology 4th edition, vol 12 pages 842-862 , J. Baird, Kelco, Merck division). See also "Carbohydrate Chemistry for Food Scientists" (Eagan Press-1977) by R.L. Whistier and J.N. BeMiller, Chapter 4, pages 63-89 and Direct Food Additives in Fruit Processing of P. Laslo, "Bioprinciples and Applications", Vol. 1, chapter II, pages 313-325 (1996), Technomie publishing. Some of these gums such as guar gum (E412), carob (E410) are widely used alone or in combination in many food applications (Gums in ECT 4th edition, vol 12, pages 842-862, J. Baird, Kelco , division of Merck). The guar gum present in these food stains and cosmetics is obtained from the endosperm of the seed of the legume plant Cyamopsis tetragonoloba. Guar gum (also called guarana) extracted from the dicotyledonous seed is composed of a base structure of 1-4-β-D-mannopyranosyl units and is used as a thickening agent in dressings, frozen products and cosmetics (HD Belitz, "Food Chemistry "page 243, English version of the second edition, Springer-Verlag, 1987, ISBN 0-387-15043-9 (EUA)) and (Carbohydrate Chemistry for Food Scientists", RL Whistier Eagan Press, 1997 ISBN 0-913250- 92-9) and (Industrial Gum ", second edition, RL Whistier, page 308, Academic Press, 1973, ISBN 0-12-74-6252-x). Locust bean gum (also called carob gum or "San Juan bread") is also used in the food industry and is extracted from the seed of a perennial plant grown in the Mediterranean area. Carob bean gum probably differs from the structure of guar gum alone in the smaller number of D-galactosyl side chains and has the same 1,4-b-D-mannopyranosyl skeleton. In legume seeds, water-soluble galactomannan is the main storage carbohydrate, in some cases comprising up to 20% of the total dry weight. Galactomannan has an α-galactose bound to O-6 from mannose residues and may also be acetylated to a variable degree on O-2 and O-3 residues of mannose. As described above, there is a continuing need to formulate laundry detergent compositions that provide superior cleaning performance, especially of cosmetic and food stains and that provide soil release benefits. This objective has been met by formulating laundry detergent compositions comprising a mannanase enzyme and a cotton soil release polymer. It has further been found that the performance of the laundry detergent compositions of the present invention can be increased by the addition of another detergent ingredient selected from a builder, especially a zeolite, a sodium tripolyphosphate and / or layered silicate, a surfactant, preferably a nonionic surfactant such as alkylethoxylate or 5-alkylmethylglucamide, a conventional soil release polymer and / or mixtures thereof. Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol. 56 No. 11, pages 3505-3510 (1990) describe a β-mannanase derived from Bacillus 10 stearothermophilus in dimeric form with a MW of 162 kDa and an optimum pH of 5-5 - 7.5. Mendoza and others, World J. Microbio. Biotech., Vol. 10, No.5, pages 551-555 (1994) describe a β-mannanase derived from Bacillus subtilis having a MW of 38 kDa, an optimal activity at pH 5.0 at 55 ° C and a pl of 4.8. Document J0304706 describes a mannanase derived from 15 Bacillus sp. which has a MW of 37 ± 3 kDa measured by gel filtration, an optimum pH of 8-10 and a pl of 5.3 - 5.4. J63056289 discloses the production of a thermostable alkaline β-mannanase that hydrolyzes β-1,4-D-mannopyranoside bonds for example from mannans and produces hand: oligosaccharides. Document J63036774 refers to a 20 microorganism Bacillus FERM P-8856, which produces β-mannanase and β-mannosidase at an alkaline pH. In WO 07/11164 a purified mannanase from Bacillus amyloliquefaciens and its method of preparation is described, which is useful in the bleaching of pulp and paper. The document '* GÉii £ - && éB htiiBiaák, ±, ..,., ^ -L. ^ .. ^ SÉ ^ S ^, ^. ^^^^^^. ^ ^.

WO 91/18974 discloses a hemiacerase such as a glucanase, xylanase or mannanase, active at extreme pH and temperature, and the production thereof. WO 94/25576 describes an enzyme exhibiting mannanase activity, derived from Aspergillus aculeatus CBS 101.43, which could be used for various purposes in which degradation or modification of cell wall material from plants or algae is sought. WO 93/24622 describes an isolated mannanase from Trichoderma reesie for bleaching lignocellulosic pulps. However, the synergistic combination of a mannanase and soil release polymer in cotton has not been previously recognized to obtain superior cleaning and dirt release performance in a laundry detergent composition.

BRIEF DESCRIPTION OF THE INVENTION The present invention relates to laundry detergent compositions comprising a mannanase and a cotton soil release polymer to provide superior cleaning and dirt release performance. iSsmki &Eaá DETAILED DESCRIPTION OF THE INVENTION An essential element of the laundry detergent composition of the present invention is a mannanase enzyme.

The mannanase enzyme An essential element of the detergent compositions of the present invention is a mannanase enzyme. In the present invention, the following three mannan degrading enzymes are encompassed: EC 3.2.1.25: β-mannosidase, EC 3.2.1.78: Endo-1, 4-β-mannosidase, hereinafter referred to as "mannanase", and EC 3.2.1.100:1, 4-ß-manobiosidase (Enzyme nomenclature of IUPAC Classification, 1992, ISBN 0-12-227165-3 Academic Press). Most preferably, the detergent compositions of the present invention comprise a β-1,4-mannosidase (E.C. 3.2.1.78) referred to as mannanase. The term "mannanase" or "galactomannanase" denotes a mannanase enzyme defined according to the technique as officially called endo-1, 4-beta-mannosidase mannan and having the alternative names beta-mannanase and endo-1,4-mannanase and which catalyzes the reaction: random hydrolysis of 1, 4-beta-D-mannosidic bonds in mannans, galactomannans, glucomannans and galactoglucomannans. The mannans are polysaccharides that have a base structure composed of ß-1, 4-linked mañosa; glucomannans are polysaccharides that have a structure of to base or hands and glucose ß-1, 4- linked more or less alternating; the galactomannans and galactoglucomannans are mannans and glucomannans with attached side branches of galactose a-1,6. These compounds can be acetylated. The degradation of galactomannans and galactoglucomannans is facilitated by the complete or partial removal of the galactose side branches. In addition, the degradation of mannans, glucomannans, galactomannans and acetylated galactoglucomannans is facilitated by complete or partial deacylation. Acetyl groups can be removed by alkali or by mannitol acetylesterases. The oligomers that are released from the mannanases or by means of a combination of mannanases and α-galactosidase and / or mannitol acetylesterases can be degraded further to release free maltose by means of 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, pp. 3505-3510 (1990) describes a β-mannanase derived from Bacillus stearothermophilus in the form of a dimer having a MW of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J. Microbiol. Boitech., Vol. 10, No. 5, pp. 551-555 (1994) describes a β-mannanase derived from Bacillus subtilisis which has a MW of 38 kDa, an optimal activity at pH 5.0 / 55 ° C and a pl of 4.8. J0304706 describes a β-mannanase derived from Bacillus sp., Which has a molecular weight of 373 kDa, measured by gel filtration, an optimum pH of 8-10 and a pl of 5.3-5.4. J63056289 describes the production of an alkaline β-mannanase and thermoset, which hydrolyzes β-1,4-D-mannopyranoside bonds of, for example, mannans and produces hand-oligosaccharides. J63036774 refers to a Bacillus FERM P-8856 microorganism that produces β-mannanase and β-mannosidase at an alkaline pH. JP-08051975 describes beta-mannanases from Bacillus sp. Alcalophilic AM-001. A purified mannanase from Bacillus amyloliquefaciens useful in pulp and paper bleaching and a method of preparing it are described in WO97 / 11164. WO91 / 18974 describes a hemicellulase such as a glucanase, xylanase or mannanase, active at extreme pH and temperature. WO94 / 25576 describes an enzyme that exhibits a mannanase activity derived from Aspergillus aculeatus CBS 101.43, which could be used for various purposes for which the degradation or modification of plant or algal cell wall material is desired. WO93 / 24622 describes an isolated mannanase from Trichoderma reesie for bleaching lignocellulosic pulps. A hemicellulase capable of degrading hemicellulose containing mannan is described in WO91 / 18974, and a purified mannanase of Bacillus amyloliquefaciens is described in WO97 / 11164. In particular, this mannanase enzyme will be an alkaline mannanase as defined below, most preferably, a mannanase originating from a bacterial source. Especially, the laundry detergent composition of the present invention will comprise an alkaline mannanase selected from the mannanase of the Bacillus agaradherens strain and / or Bacillus subtilisis strain 168, yght gene.

The term "mannanase alkaline enzyme" is intended to encompass an enzyme having an enzymatic activity of at least 10%, preferably at least 25%, most preferably at least 40% of its maximum activity at a certain pH ranging from 7 to 12, preferably 7.5 to 10.5. Most preferably, the detergent compositions of the present invention will comprise the alkanal mannanase of Bacillus agaradherens. Said mannanase is i) a polypeptide produced by Bacillus agaradherens, NCIMB 40482, or ii) a polypeptide comprising an amino acid sequence as shown in positions 32-343 of SEQ ID NO: 2 or iii) a defined polypeptide analogue in i) or ii), which is at least 70% homologous with said polypeptide, or is derived from said polypeptide by substitution, deletion or addition of one or more 15 amino acids, or is immunologically reactive with a polyclonal antibody developed against said polypeptide in purified form. The present invention also encompasses an isolated polypeptide having mannanase activity selected from the group consisting of a) polynucleotide molecules that encode a polypeptide having mannanase activity and comprising a nucleotide sequence as shown in SEQ ID NO: 1 of the invention. nucleotide 97 to nucleotide 1029; b) homologous species of a); c) polynucleotide molecules that code for a polypeptide it * »*** ***: * ** í? Á * having mannanase activity that is at least 70% identical to the amino acid sequence of SEQ ID NO: 2 from amino acid residue 32 to amino acid residue 343; d) molecules complementary to a), b) or c); and e) degenerate nucleotide sequences of a), b), c) or d). Plasmid pSJ1678 comprising the polynucleotide molecule (the DNA sequence) encoding a mannanase of the present invention has been transformed into a strain of Escherichia coli which was deposited by the inventors in accordance with the Budapest Treaty on Recognition International Deposit of Microorganisms for the Purposes of Patent Procedures in the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH, Mascheroder Weg 1 b, D-38124, Braunschweig, Federal Republic of Germany, on May 18, 1998 with the deposit number DSM 12180. A second enzyme that is most preferred is the mannanase of Bacillus subtilisis strain 168, which: i) is encoded by the coding part of the DNA sequence shown in SEQ ID NO: 5 or an analogue of said sequence and / or i) a polypeptide comprising an amino acid sequence as shown in SEQ ID NO: 6 or iii) an analogue of the polypeptide 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 more '**** "* *" - - * "** ftfi - ^ | j-jfejj a-; 4 amino acids, or is immunologically reactive with a polyclonal antibody developed against said polypeptide in purified form. The present invention also encompasses an isolated polypeptide having mananase activity selected from the group consisting of: a) polynucleotide molecules that encode a polypeptide having mannanase activity and comprising a nucleotide sequence as shown in SEQ ID NO: 5; b) homologous species of a); c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 70% identical to the amino acid sequence of SEQ ID NO: 6; d) molecules complementary to a), b) or c); and e) degenerate nucleotide sequences of a), b), c) or d).

Definitions Before describing this invention in more detail, the following terms will first be defined: The term "ortholog" (or "species homolog") denotes a polypeptide or protein obtained from a species having homology to a polypeptide or protein analogous to a different species. The term "paralog" denotes a polypeptide or protein obtained from a certain species having a polypeptide or protein other than that same species.

The term "expression vector" denotes a DNA molecule, linear or circular, comprising a segment encoding a polypeptide of interest operably linked to additional segments that provide its transcription. Said additional segments may include promoter and terminator sequences, and may optionally contain one or more origins of replication, one or more selectable markers, an enhancer, a polyadenylation signal, and the like. Expression vectors are generally derived from plasmid or viral DNA, or may contain elements of both. The expression vector of the invention can be any expression vector that is conveniently subjected to procedures with recombinant DNA, and the choice of vector will commonly depend on the host cell into which the vector will be introduced. In this way, the vector can be a replication vector in an autonomous form, that is, a vector that exists as an extra chromosomal entity, whose replication is independent of chromosomal replication, for example, a plasmid. Alternatively, the vector may be one which, when introduced into a host cell, is integrated into the genome of the host cell and replicated together with the chromosome (s) into which it has been integrated. The term "recombinant expressed" or "recombinantly expressed" used herein in relation to the expression of a polypeptide or protein is defined according to the standard definition in the art. The expression in recombinant form of a protein is generally carried out using an expression vector as described above. The term "isolated", when applied to a polynucleotide molecule, denotes that the polynucleotide has been removed from its natural genetic environment and is thus free of any other foreign or unwanted coding sequence, and is in a form suitable for use within genetically engineered protein production systems. Said isolated molecules are those that are separated from their natural environment and include cDNA and genomic clones. The isolated DNA molecules of the present invention are free of other genes with which 10 are normally associated, but may include naturally occurring 5 'and 3' untranslated regions such as promoters and terminators. The identification of associated regions will be apparent to one skilled in the art (see, for example, Dynan and Tijan, Nature 316: 774-78, 1985). The term "an isolated polynucleotide" may be referred to Alternatively, "a cloned polynucleotide". When applied to a protein / polypeptide, the term "isolated" indicates that the protein is in a condition that is not that of its native environment. In a preferred form, the isolated protein is substantially free of other proteins, particularly other homologous proteins (ie, "impurities"). 20 homologues "(see below)) It is preferred to provide the protein in a more than 40% pure form, most preferably more than 60% pure form.More more preferably it is preferred to provide the protein in a highly purified form, it is say, more than 80% pure, most preferably more than 95% pure, more preferably more than 99% pure, as determined by SDS-PAGE. The term "isolated protein / polypeptide" can alternatively be referred to as "purified protein / polypeptide". The term "homologous impurities" means any impurity (for example, another polypeptide than the polypeptide of the invention) that originates from the homologous cell from which the polypeptide of the invention is originally obtained. The term "obtains from" as used herein in relation to a specific microbial source means the polynucleotide and / or polypeptide produced by the specific source, or by a cell into which a gene from the source has been inserted. The term "operably linked", when referring to DNA segments, denotes that the segments are arranged in such a way that they work in concert for their desired purposes, for example, the transcription starts at the promoter and proceeds through the coding segment towards the terminator. The term "polynucleotide" denotes a single or double chain polymer of deoxyribonucleotide or ribonucleotide bases read from the 5 'to the 3' end. The polynucleotides include RNA and DNA, and can be isolated from natural sources, synthesized in vitro, or prepared from a combination of natural and synthetic molecules.

The term "polynucleotide molecule complements" denotes polynucleotide molecules having a complementary base sequence and inverted orientation as compared to a reference sequence. For example, the 5 'sequence ATGCACGGG 3' is complementary to 5 'CCCGTGCAT 3'. The term "degenerate nucleotide sequence" denotes a nucleotide sequence that includes one or more degenerate codons (as compared to a reference polynucleotide molecule that encodes a polypeptide). Degenerate codons contain different triplets of nucleotides, but code for the same amino acid residue (ie, the triplets GAU and GAC encode each for Asp). The term "promoter" denotes a portion of a gene that contains DNA sequences that provide for the binding of RNA polymerase and the initiation of transcription. Promoter sequences are commonly, but not always, found in the 5 'non-coding regions of the genes. The term "secretory signal sequence" denotes a DNA sequence that encodes a polypeptide (a "secretory peptide") that, as a component of a larger polypeptide, directs the larger polypeptide through a secretory pathway of a cell in which it is synthesized. The larger peptide is commonly cut to remove the secretory peptide during its transit through the secretory pathway. ^ -x? How to use a sequence of the invention to obtain other related sequences The sequence information described herein which refers to a polynucleotide sequence encoding a mannanase of the invention can be used as a tool to identify other homologous mannanases. For example, the polymerase chain reaction (PCR) can be used to amplify sequences encoding other homologous mannanases from a variety of microbial sources, in particular from different Bacillus species.

Assay for activity test A polypeptide of the invention having mannanase activity can be tested to verify its mannanase activity according to standard test procedures known in the art, such as by applying a solution that will be tested to 4 mm holes of perforated diameters on agar plates containing 0.2% of AZCL galactomannan (carob), that is, substrate for the endo-1, 4-beta-D-mananase test available as CatNo.l-AZGMA from the company Megazyme by US $ 110.00 for 3 grams (Megazyme's Internet address: http://www.meqazyme.com/Purchase/index.html).

Polynucleotides An isolated polynucleotide of the invention will hybridize to regions of similar size of SEQ ID NO: 1, or a sequence complementary thereto, under conditions of at least half astringency. In particular, the polynucleotides of the invention will hybridize to a denatured double-stranded DNA probe which already comprises the entire sequence shown at positions 97-1029 of SEQ ID NO: 1 or any probe comprising a subsequence of SEQ ID NO. : 1 having a length of at least 100 base pairs under conditions of 10 at least half astringency, but preferably in conditions of high stringency as described in detail below. Suitable experimental conditions for determining hybridization in medium or high astringency between a nucleotide probe and a homologous DNA or RNA sequence include pre-blotting the filter containing the DNA fragments or RNA to hybridize in 5 x SSC (sodium chloride / sodium citrate, Sambrook et al., 1989) for 10 minutes, and prehybridization of the filter in a solution of 5 x SCC, 5 x Denhardt's solution (Sambrook et al. 1989), 0.5% SDS and 100 μg / ml sonicated and denatured salmon sperm DNA (Sambrook et al., 1989), followed by hybridization in the same solution as 20 contains a concentration of 10 ng / ml of a randomly initiated probe (Feinberg, AP and Vogelstein, B. (1983) Anal. Biochem. 132: 6-13), 32P dCTP-labeled (specific activity of more than 1 x 109 cpm / μg) for 12 hours at about 45 ° C. The filter is then washed twice for 30 minutes in 2 x SSC, 0.5% SDS at least at 60 ° C (medium astringency), still more preferably at least 65 ° C (medium / high astringency), even very preferably at least 70 ° C (high astringency) , and even more preferably at least 75 ° C (very high astringency). 5 The molecules to which the oligonucleotide probe hybridizes under these conditions are detected using an x-ray film. As previously mentioned, the isolated polynucleotides of the present invention include DNA and RNA. Methods for isolating DNA and RNA are well known in the art. The genes that code for DNA and RNA 10 of interest can be cloned into gene libraries or DNA libraries by methods well known in the art. Polynucleotides encoding mannanase-active polypeptides of the invention are then identified and isolated by, for example, hybridization or PCR. The present invention provides 15 also polypeptides and counterpart polynucleotides of different bacterial strains (orthologs or paralogs). Of particular interest are the mannanase polypeptides of Gram-positive alkalophilic strains, including Bacillus species. The homologous species of a polypeptide with activity Mannanase of the invention can be cloned using information and compositions provided by the present invention in combination with conventional cloning techniques. For example, a DNA sequence of the present invention can be cloned using chromosomal DNA obtained from a type of cell that expresses the protein. Suitable sources of DNA can be identified by probing Northern blots with probes designed from the sequences described herein. A chromosomal DNA library of a positive cell line is then prepared. A DNA sequence of the invention encoding a polypeptide having mannanase activity can then be isolated by a variety of methods, such as probing with probes designed from the sequences described in the present description and claims, or with one or more sets of probes degenerate based on the sequences described. A DNA sequence of the invention can also be cloned using the polymerase chain reaction, or PCR (Mullis, U.S. Patent No. 4,683,202), using primers designed from the sequences described herein. In a further method, the DNA library can be used to transform or transfect host cells, and the expression of the DNA of interest can be detected with an antibody (monoclonal or polyclonal) developed against the cloned mannase of β. Agaradherens, NCIMB 40482, expressed and purified as described in the Materials and Methods section and example 1, or by an activity test that relates to a polypeptide having mannanase activity. The mannanase coding part of the DNA sequence cloned in the plasmid pSJ1678 present in Escherichia coli DSM 12180 and / or an analogous DNA sequence of the invention can be cloned from a strain of the bacterial species Bacillus agaradherens, preferably the strain NCIMB 40482, producing the enzyme with mamanic degrading activity, or another different or related organism as described herein. Alternatively, the analogous sequence can be constructed on the basis of the DNA sequence obtainable from the plasmid present in Escherichia coli DSM 12180 (which is believed to be identical to the attached SEQ ID NO: 1), for example being a subsequence thereof. , and / or by introducing nucleotide substitutions that do not give rise to another amino acid sequence of the mannanase encoded by the DNA sequence, but corresponding to the use of codons of the host organism designed for the production of the enzyme, or by the introduction of nucleotide substitutions that can give rise to a different amino acid sequence (i.e., a variant of the morning-meal degrading enzyme of the invention).

Polypeptides The amino acid sequences Nos. 32-343 of SEQ ID NO: 2 constitute a mature mannanase sequence. The present invention provides mannanase polypeptides that are substantially homologous to the polypeptide of SEQ ID NO: 2 and homologous species thereof (paralogs or orthologs). The term "substantially homologous" is used herein to denote polypeptides having 70%, preferably at least 80%, preferably at least 85%, and most preferably at least 90% sequence identity with the sequence shown in US Pat. amino acids Nos. 32-343 of SEQ ID NO: 2 or their orthologs or paralogs. Said polypeptides will preferably be at least 95% identical, preferably 98% or more identical, to the sequence shown in amino acids Nos. 32-343 of SEQ ID NO: 2 or their orthologs or paralogs. The percentage of sequence identity is determined by conventional means, by means of computer programs known in the art such as the GAP, provided in the GCG program package (Program Manual for the Wisconsin Package, version 8, August 1994, Genetics Computer Group, 575 Science Drive, Madison, Wisconsin, USA 53711) as described by Needleman SB and Wunsch C.D. (1970), Journal of Molecular Bioloqy, 48, 443-453, which is incorporated herein by reference in its entirety. GAP is used with the following polypeptide sequence comparison parameters: GAP creation penalty of 3.0 and GAP extension penalty of 0.1. The sequence identity of polynucleotide molecules is determined by similar means using GAP with the following parameters for comparison of DNA sequences: GAP creation penalty of 5.0 and GAP extension penalty of 0.3 The enzyme preparation of the invention is preferably derived from a microorganism, preferably a bacterium, archeae or a fungus, especially a bacterium such as, for example, one belonging to the genus Bacillus, preferably an alkalophilic strain of Bacillus, which may be selected from the group consisting of Bacillus species agaradherens and closely related Bacillus species, wherein all species are preferably at least 95%, most preferably at least 98% homologous with Bacillus agaradherens based on the aligned 16S rDNA sequences. Substantially homologous proteins and polypeptides are characterized by having substitutions, deletions or additions of one or more amino acids. Preferably these changes are minor in nature, ie, conservative amino acid substitutions (see Table 2) and other substitutions that do not significantly affect the fold or activity 10 of the protein or polypeptide; small deletions, typically from 1 to about 30 amino acids; and small extensions of the amino or carboxyl terminus, such as an amino terminal residue of methionine, a small linker peptide of up to about 20-25 residues, or a small extension that facilitates purification (and affinity tag), such as 15 a tract of polyhistidine, 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 2: 95 -107, 1991, which are incorporated herein by reference DNAs that encode affinity tags of commercial suppliers are available (e.g., Pharmacia Biotech. 20 Piscataway, New Jersey; New England Biolabs, Beverly, Massachisetts). However, even though the changes described above are preferably of a minor nature, said changes may also be of a larger nature such as the fusion of larger polypeptides of M, j.ta * L ^, »& a ^^ to 300 amino acids or more both as extensions at the amino terminus or as extensions at the carboxyl terminus to a mannanase polypeptide of the invention.

TABLE 1 Conservative amino acid substitutions Basic arginine, lysine, histidine Acid glutamic acid, aspartic acid Polar glutamine, asparagine Hydrophobic leucine, isoleucine, valine Aromatic phenylalanine, tryptophan, tyrosine Small glycine, alanine, serine, threonine, methionine According to the invention, the amino acid residues of a polypeptide can be substituted with non-normal amino acids (such as 4-hydroxyproline, 6-N-methyl-lysine, 2-aminoisobutyric acid, isovaline and alpha-methyl-serine), in addition of the 20 normal amino acids. A limited number of non-conservative amino acids, amino acids that are not encoded by the genetic code and non-natural amino acids, can replace the amino acid residues. "Unnatural amino acids" have been modified after protein synthesis, and / or have a chemical structure in their side chain (or chains) different from that of normal amino acids. The non-natural amino acids can be chemically synthesized or, preferably, are commercially available and include pipecolic acid, thiazolidinecarboxylic acid, dehydroproline, 3- and 4-methylproline and 3,3-dimethylproline. The essential amino acids in the mannanase polypeptides of the present invention can be identified according to methods known in the art, such as site-directed mutagenesis or alanine scanning mutagenesis (Cunningham and Wells, Science, 1081-1085, 1989). . In the latter technique, simple mutations of alanine are introduced into each residue in the molecule, and the resulting mutant molecules are analyzed to determine their biological activity (ie, their mannanase activity) to identify 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 can also be determined by physical analysis of the structure, determined by techniques such as nuclear magnetic resonance, crystallography, electronic diffraction or photoaffinity marking, in conjunction with the mutation of putative amino acids from the contact site. See for example of 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 identities of the essential amino acids can also be inferred from an analysis of homologies with polypeptides that are related to the polypeptide according to the invention. Multiple substitutions of amino acids can be made and tested using known methods of mutagenesis, recombination and / or displacement, followed by a relevant selection procedure such as that described by Reidhaar-Olson and Sauer (Science, 241, 53-57, 1988), Bowie and Sauer (Proc. Nati, Acad. Sci. USA, 86 2152-2156, 1989), or WO 95/17413, or WO 95/22625. Briefly, these authors describe methods for simultaneously randomizing two or more positions in a polypeptide, or recombination / recombination of different mutations (WO 95/17413, WO 95/22625), followed by selection of a functional polypeptide, and then sequencing the polypeptides mutated to determine the spectrum of allowable substitutions in each position. Other methods that can be used include phage display (e.g., Lowman et al., Biochem 30, 10832-10837, 1991, Ladner et al., U.S. Patent No. 5,223,409, Huse, WIPO publication WO 92/06204) and site-directed mutagenesis (Cerbyshire et al., Gene 46, 145, 1986, Ner et al., DNA 7, 127, 1988). To detect the activity of mutated polypeptides cloned in host cells, the mutagenesis / displacement methods described above can be combined with high throughput automated selection methods. The mutated DNA molecules that encode active polypeptides can be rapidly sequenced using modern equipment. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide of interest, and can be applied for polypeptides of unknown structure. Using the methods mentioned above, a person of ordinary skill in the art can identify and / or prepare a variety of polypeptides that are substantially homologous to residues 32 to 343 of SEQ ID NO: 2 and retain mannanase activity of the protein of wild type. 5 Production of protein The proteins and polypeptides of the present invention, including full-length proteins, fragments thereof and fusion proteins, can be produced in genetically engineered host cells 10 according to conventional techniques. Suitable host cells are those cell types that can be transformed or transfected with exogenous DNA and grown in culture, and include bacteria and fungi and cultured higher eukaryotic cells. Bacterial cells are preferred, particularly cultured cells of Gram-positive organisms. Especially preferred are Gram-positive cells of the Bacillus genus, such as for example from the group consisting of Bacillus subtilis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillius coagulans, Bacillus circulans, Bacillus lautus, Bacillus thuringiensis. , Bacillus licheniformis and 20 Bacillus agaradherens, in particular Bacillus agaradherens. Techniques for manipulating cloned DNA molecules and introducing exogenous DNA into a variety of host cells are described by Sambrook and others in "Molecular Cloning: A Laboratory Manual", 2nd edition, JK ^ JL x * ** ** ^. ^ ^ ~ * »M ** r- ~ .- Ü« -~~ - ^ ~~ * - * ^ -a - ¿XX * ^ > ^ Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1989; Ausebel et al. (Editors), "Current Protocols in Molecular Biology", John Wiley and Sons, New York, 1987 and "Bacillus subtilis and other Gram-positive bacteria", Sonensheim et al., 1993, American Society for Microbiology, Washington DC, which are incorporated here as a reference. In general, a DNA sequence encoding a mannanase of the present invention is operably linked to other genetic elements required for its expression, generally including a transcription promoter and a terminator within an expression vector. The vector will also commonly contain one or more selectable markers and one or more origins of replication, although those skilled in the art will recognize that within certain systems selectable markers can be provided on separate vectors and replication of the exogenous DNA can be provided by its integration into the genome of the host cell. The selection of promoters, terminators, selectable markers, vectors and other elements is a matter of routine design within the scope of a person with average knowledge in the field. Many such elements are described in the literature and are available from commercial suppliers. To direct a polypeptide in the secretory pathway of a host cell, a secretory signal sequence (also known as a leader sequence, prepro-sequence or pre-sequence) is provided in the expression vector. The secretory signal sequence may be that of the polypeptide or it may be derived from another protein secreted or synthesized ofe novo. They know each other , ~? * ~ 3 in the art many suitable secretory signal sequences and are referred to "Bacillus subtilis and other Gram-positive bacteria", Sonensheim et al., 1993, American Society for Microbiology, Washington DC, and Cutting SM (editors ) "Molecular Biological Methods for Bacillus", John Wiley and Sons, 1990, for further description of suitable secretory signal sequences, especially for secretion in a Bacillus host cell. The secretory signal sequence is linked to the DNA sequence in the correct reading frame. The secretory signal sequences are commonly placed at the 5 'end of the DNA sequence encoding the polypeptide of interest, although certain signal sequences can be placed anywhere in the DNA sequence of interest (see for example, Welch et al. others, U.S. Patent No. 5,037,743; Holland et al., U.S. Patent No. 5,143,830). The transformed or transfected host cells are cultured according to conventional procedures in a culture medium containing nutrients and other components required for the growth of the chosen host cells. A variety of suitable media are known in the art, including defined media and complex media, and generally include a carbon source, a nitrogen source, essential amino acids, vitamins and minerals. The media may also contain components such as growth factors or serum as needed. The growth medium will generally select cells containing the added DNA exogenously by, for example, drug selection or deficiency of an essential nutrient, which is complemented by the selectable marker carrying the expression vector or that was cotransfected in the host cell. 5 Isolation of the protein When the expressed recombinant polypeptide is secreted, it can be purified from the growth medium. Preferably, the expression host cells are removed from the medium before the polypeptide is purified (eg, by centrifugation). When the expressed recombinant polypeptide is not secreted from the host cell, the host cell is preferably lysed and the released peptide is extracted into an aqueous "extract", which is the first step of said purification techniques. Preferably, expression host cells are harvested from the medium prior to cell lysis (e.g., by centrifugation). Cell lysis can be effected by conventional techniques such as by lysozyme digestion or by forcing the cells by high pressure. See Robert K. Scobes, "Protein Purification", second edition, Springer-Verlag, for an additional description of such lysis techniques 20 cellular Whether the expressed recombinant polypeptides (or chimeric polypeptides) are secreted or not, they can be purified using fractionation and / or purification methods and conventional means. - ^^^ é u ^ tß 3? Precipitation with ammonium sulfate and acid extraction or chaotrope can be used for fractionation of samples. Exemplary purification steps may include hydroxyapatite, size exclusion, FPLC and reverse phase high performance liquid chromatography. Suitable anion exchange media include dextrans derivatives, agarose, cellulose, polyacrylamide, specialty silicas and the like. Preferred are PEl, DEAE, QAE and Q derivatives, DEAE Flow-Fast Sepharose (Pharmacia, Piscataway, New Jersey) being particularly preferred. Exemplary chromatographic media include media derived with phenyl, butyl or octyl groups, such as Phenyl-Sepharose FF (Pharmacia), Toyopearl butyl 650 (Toso Haas, Montgomeryville, PA), Octyl-Sepharose (Pharmacia) and the like; or polyacrylic resins such as Amberchrom CG 71 (Toso Haas) and the like. Suitable solid supports include glass beads, silica-based resins, cellulosic resins, agarose beads, interlaced agarose beads, polystyrene beads, crosslinked polyacrylamide resins and the like, which are insoluble under the conditions in which they are used. These supports can be modified with reactive groups that allow the binding between the proteins and amino groups, carboxyl groups, sulfhydryl groups, hydroxyl groups and / or carbohydrate moieties. Examples of coupling chemistries include activation with cyanogen bromide, activation with N-hydroxysuccinimide, activation with epoxide, activation with sulfhydryl, activation with hydrazide, and carboxyl and amino derivatives for carbodiimide coupling chemistries. These and other solid media are well known and widely used in the art, and are available from commercial suppliers. The selection of a particular method is a matter of routine design and is determined in part by the properties of the chosen medium. See for example "Affinity Chromatography: Principles &Methods", Pharmacia LKB Biotechnology, Uppsala, Sweden, 1988. Polypeptides of the invention or fragments thereof can also be prepared by chemical synthesis. The polypeptides of the invention can be monomers or multimers; glycosylated or non-glycosylated; pegylated or non-pegylated; and may or may not include an initial residue of the amino acid methionine. Based on the sequence information described herein, a full-length DNA sequence encoding a mannanase of the invention can be cloned and comprises the sequence of DNA shown in SEQ ID NO: 1, at least the DNA sequence from position 97 to position 1029. The cloning is carried out by standard procedures known in the art, such as for example: preparing a library of a strain of Bacillus, especially the strain of S. agaradherens NCIMB 40482; • plating said library on suitable substrate plates; • identifying a clone comprising a polynucleotide sequence of the invention by standard hybridization techniques using a probe based on SEQ ID NO: 1; or • identifying a clone of said B. agaradherens NCIMB 40482 library by means of an inverse PCR strategy using primers based on sequence information of SEQ ID NO: 1. Reference is made to M.J. McPherson and others "PCR, A practical approach", Information Press Ltd., Oxford, England) for additional details regarding inverse PCR. Based on the sequence information described here (SEQ ID NO: 1, SEQ ID NO: 2), it is routine work for the expert in the The invention relates to isolating homologous polynucleotide sequences encoding homologous mannanase of the invention by means of a similar strategy using libraries of related microbial organisms., in particular libraries of other strains of the genus Bacillus, such as the alkaliphilic Bacillus species. Alternatively, DNA encoding the maman or galactomannan degrading enzyme of the invention can be conveniently cloned, according to well known procedures, from a suitable source, such as any of the aforementioned organisms, using synthetic oligonucleotide probes prepared by taking as base 20 the DNA sequence obtained from the plasmid present in Escherichia coli DSM 12180. Accordingly, the polynucleotide molecule of the invention can be isolated from Escherichia coli DSM 12180 in which it has been deposited. plasmid obtained by cloning as described above. Also, the present invention relates to a substantially pure isolated biological culture of strain DSM 12180 of Escherichia coli. In the present context, the term "enzyme preparation" refers to any conventional enzymatic fermentation product, possibly isolated and purified, from a single species of microorganism; said preparation usually comprises several different enzymatic activities; or a mixture of monocomponent enzymes, preferably enzymes derived from bacterial or fungal species using techniques 10 conventional recombinants; said enzymes have been fermented and possibly isolated and purified separately and may originate from different species, preferably from fungal or bacterial species; or the fermentation product of a microorganism that acts as a host cell for the expression of a recombinant mannanase, but said The microorganism simultaneously produces other enzymes, for example pectin-degrading enzymes, proteases or cellulases, being natural products of fermentation of the microorganism, that is, the enzyme complex conventionally produced by the corresponding natural microorganism. A production method of the enzyme preparation of the invention comprises culturing a microorganism, for example a wild-type strain, capable of producing the mannanase under conditions that allow the production of the enzyme and recover the enzyme from the culture. The crop is It can be carried out using conventional fermentation techniques, for example, cultivating in stirred flasks or stirred fermentors to ensure sufficient aeration on a growth medium that induces the production of the mannanase enzyme. The culture medium may contain a conventional N source such as peptone, yeast extract or casein amino acids, a reduced amount of a conventional C source such as dextrose or sucrose, and an inducer such as guar gum or locust bean gum. Recovery can be carried out using conventional techniques, for example separation of biomass and supernatant by means of centrifugation or filtration, recovery of the supernatant, or cell lysis if the enzyme of interest is intracellular, followed perhaps by additional purification, as described in EP 0 406 314 or by crystallization as described in WO 97/15660.

Cross-immunogenic reactivity Polyclonal antibodies to be used in the determination of immunological cross-reactivity can be prepared using a purified mannanase enzyme. More specifically, antisera against the mannanase of the invention can be developed by immunizing rabbits (or other rodents) according to the procedure described by N. Axelsen et al. In "A Manual of Quantitative Immunoelectrophoresis", Blackwell Scientific Publications, 1973, Chapter 23, or A. Johnstone and R. Thorpe "Immunochemistry in Practice", Blackwell Scientific Publications, 1982 (more specifically, page 27-31). essa Purified immunoglobulins can be obtained from the antiserum, for example by salt precipitation ((NH4) 2S0), followed by dialysis and ion exchange chromatography, for example on DEAE-Sephadex. The immunochemical characterization of proteins can be done by double-spread analysis of 5 Outcherlony (O. Ouchterlony in "Handbook of Experimental Immunology" DM Weir (editor), Blackwell Scientific Publications, 1967, pages 655-706; by cross-immunoelectrophoresis (N. Axelsen and others, cited above, chapters 3 and 4) or rocket immunoelectrophoresis (N. Exelsen et al., chapter 2). Examples of useful bacteria that produce the enzyme or enzyme preparation of the invention are Gram-positive bacteria, preferably from the Bacillus / Lactobacillus subdivision, preferably a strain of the genus Bacillus, preferably a strain of Bacillus agaradherens, especially the NCIMB strain. 40482 of Bacillus agaradherens. The present invention includes an isolated mannanase having the above described properties and which is free of homologous impurities and is produced using conventional recombinant techniques.

Determination of the catalytic activity of mannanase (ManU) 20 Coyometric test: Substrate: AZCL 2% -Galactomannan (Megazyme, Australia) of locust bean in 0.1 M glycine buffer, pH 10.0. The test is carried out in a 1.5 ml Eppendorf Micro tube with a thermomixer with ^ ^^^^^ É ^ -, ^^, ^^^^^^^. ^ Control of agitation and temperature at 40 ° C. Incubation of 0.750 ml of substrate with 0.05 ml of enzyme for 20 minutes, stopping by centrifugation for 4 minutes at 15000 rpm. The color of the supernatant is measured at 600 nm in a 1 cm cuvette. A ManU (mannanase unit) gives a 5 absorption of 0.24 in 1 cm.

Obtaining mannase from Bacillus aqaradherens NCIMB 40482 Bacillus agaradherens strains NCIMB 40482 contains the DNA sequence encoding the mannanase enzyme. Strain of £. coli: E. coli SJ2 cells were prepared (Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, BR, Sjfholm, C. (1990) "Cloning of aldB, which encodes alpha-acetolactate decarboxylase, an exoenzyme from Bacillus brevis "J. Bacteriol., 172, 4315-4321), and transformed by electroporation using a Gene Pulser ™ electroporator from BIO-RAD as described by the supplier. H.H. subtilis PL2306. This strain is B. subtilis DN1885 with the interrupted apr and npr genes (Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, BR, Sjfholm, C. (1990) "Cloning of aldB, which encodes alpha - 20 acetolactate decarboxylase, an exoenzyme from Bacillus brevis "J. Bacteriol., 172, 4315-4321) interrupted in the transcription unit of the known gene for β-cellulase. subtilis, which results in cellulase-negative cells. The interruption was carried out essentially as described ^^ M ^^,. ^^^^^ - ^^^^^^ in (Eds. AL Sonenshein, JA Hoch and Richard Losick (1993) Bacillus subtilis and other Gram-Positive Bacteria, American Society for Microbiology, p. 618). Competent cells were prepared and transformed as described by Yasbin, R.E., Wilson, G.A. and Young, F.E. (1975) Transformation and transfection in lysogenic strains of Bacillus subtilis: evidence for selective induction of prophage in competent cells. J. Bacteriol, 121: 296-304.

Plasmids PSJ1678 (as described in detail in WO 94/19454 which is incorporated herein by reference in its entirety). PMOL944: This plasmid is a pUB110 derivative that essentially contains elements that make the plasmid capable of propagating in Bacillus subtilis, the kanamycin resistance gene and having a strong promoter and a signal peptide cloned from the amyL gene of β. licheniformes atcc 14580. The signal peptide contains a Sacll site which makes it convenient to clone the DNA encoding the mature part of a protein in fusion with the signal peptide. This results in the expression of a Pre-protein that is directed towards the outside of the cell. The plasmid was constructed by conventional genetic engineering techniques which are briefly described below.

Construction of pMOL944 Plasmid pUB110 (McKenzie, T. et al., 1986, Plasmid 15: 93-103) was digested with the unique restriction enzyme Ncyl. A PCR fragment amplified from the amyL promoter encoded in the plasmid pDN1981 (PL Jfrgensen et al., 1990, Gene, 96, p37-41) was digested with Ncil and inserted into the pcil110 digested with Ncil to give the plasmid pSJ2624 . The two initiators of PCR used have the following sequences: # LWN5494 5'-GTCGCCGGGGCGGCCGCTATCAATTGGTAACTGTATCTCAGC-3 '# LWN54955'-GTCGCCCGGGAGCTCTGATCAGGTACCAAGCTTGTCGACCTGCAGAA TGAGGCAGCAAGAAGAT-3' The primer # LWN5494 inserts a NotI site in the plasmid. The plasmid pSJ2624 was then digested with Sacl and NotI and a new PCR fragment amplified in the amyL promoter encoded in the plasmid pDN1981 was digested with Sacl and NotI and this DNA fragment was inserted into the plasmid pSJ2624 to give the plasmid pSJ2670. This cloning replaces the first promoter that is cloned with the same promoter but in the opposite direction. The two primers used for PCR amplification have the following sequences: # LWN5938 5'-GTCGGCGGCCGCTGATCACGTACCAAGCTTGTCGACCTGCAGAATG 4t-AGGCAGCAAGAAGAT-3 '# LWN5939 5'-GTCGGAGCTCTATCAATTGGTAACTGTATCTCAGC-3' Plasmid pSJ2670 was digested with restriction enzymes Pstl and Bell and a PCR fragment amplified from a cloned DNA sequence encoding the alkaline SP722 amylase enzyme (described in the international patent application as W095 / 26397 which is incorporated herein by reference in its entirety) was digested with Pstl and Bell and inserted to give the plasmid pMOL944. The two primers used for PCR amplification have the following sequences: # LWN7864 5'-AACAGCTGATCACGACTGATCTTTTAGCTTGGCAC-3 ' # LWN7901 5'- AACTGCAGCCGCGGCACATCATAATGGGACAAATGGG-3 'The primer # LWN7901 inserts a Sacll site into the plasmid.

Cloning of the gene for mannanase from Bacillus aqaradherens Preparation of genomic DNA: The strain NCIMB 40482 from Bacillus agaradherens was prpopaged in liquid medium as described in WO94 / 01532. After 16 hours of incubation at 30 ° C and 300 rpm, the cells were harvested and the 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 guanidium thiocyanate, Lett.Appl Microbiol., 8, 151-156).

Construction of the genomic library Genomic DNA was partially digested with the restriction enzyme Sau3A, and fractionated by size by electrophoresis on 0.7% agarose gel. The fragments with size between 2 and 7 kb were isolated by electrophoresis in DEAE-cellulose paper (Dretzen, G., Bellard, M., Sassone -Corsi, P., Chambón, P. (1981) A reliable method for the recovery of DNA fragments from agarose and acrylamide gels, Anal. Biochem., 112, 295-298). The isolated DNA fragments were ligated to the plasmid DNA pSJ1678 digested with BamHI, and the ligation mixture was used to transform E. coli SJ2.

Identification of positive clones A DNA library in E. coli, constructed as described above, was selected on LB agar plates containing 0.2% AZCL-galactomannan (Megazyme) and 9 μg / ml chloramphenicol and incubated overnight at 37 ° C. Clones expressing mannanase activity appeared with blue diffusion halos. The plasmid DNA from one of these clones was isolated by Qiagen plasmid spin preparations in 1 ml of the culture broth used at night (cells incubated at 37 ° C in TY with 9 μg / ml chloramphenicol and shaking at 250 rpm). This clone (MB525) was further characterized by determination of the DNA sequence of the Sau3A DNA fragment. The 1 S8. ?? "WÉÉ ft * 1 **** - 1 determination of the DNA sequence was performed by primerwalking, using the Taq deoxyric-terminal cycle sequence determination equipment (Perkin-Elmer, USA), fluorescently labeled terminators and the appropriate oligonucleotides as primers Sequence data analysis was performed in accordance with Devereux et al (1984) Nucleic Acids Res. 12, 387-395.The sequence encoding 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 β. subtilis The DNA sequence encoding mannanase of the invention was amplified by PCR using the set of PCR primers consisting of these two oligonucleotides: Mannanase.upper.Sacll 5'-CAT TCT GCA GCC GCG GCA GCA AGT ACA GGC TTT TAT GTT GAT GG-3 'Mannanase.lower.Notl 5'-GAC GAC GTA CAG GCG GCC GCG CTA TTT CCC TAA CAT GAT GAT ATT TTC G-3' The restriction sites Sacll and Notll are underlined. Chromosomal DNA isolated from B. agaradherens NCIMB 40482 as described above was used as template in a PCR reaction using Amplitaq DNA Polymerase (Perkin-Elmer) in accordance with yes ^ ^^ j ^^^ the manufacturer's instructions. The PCR reaction was done in buffer for PCR (10 mM Tris-HCl, pH 8.3, 50 mM KCl, 1.5 mM MgCl2, 0.01% (w / v) gelatin) containing 200 μM of each dNTP, 2.5 units of AmpliTaq polymerase (Perkin-Elmer, Cetus, USA) and 100 pmoles of each primer. The PCR reaction was performed using a thermal cycler for DNA (Landgraf, Germany). An incubation at 94 ° C for 1 minute followed by 30 cycles of PCR using a denaturing cyclic profile at 94 ° C for 30 seconds, annealing at 60 ° C for 1 minute and extension at 72 ° C for 2 minutes. Aliquots of 5 μl of the amplification product were analyzed by electrophoresis in 0.7% agarose gels (NuSieve), FMC). The appearance of a DNA fragment with a size of 1.4 kb indicated appropriate amplification of the gene segment.

Subcloning the PCR fragment Forty-five μl aliquots of the PCR products generated as described above were purified using the QIAquick PCR purification kit (Qiagen, USA) in accordance with the manufacturer's instructions. The purified DNA was eluted in 50 μl of 10 mM Tris-HCl, pH 8.5. 5 μg of pMOL944 and twenty-five μl of the PCR fragment purified with Sacll and Notl were digested, electrophoresed on 0.8% agarose gels (SeaPlaque GTG, FMC) at low gelation temperature, The relevant fragments were from the gels and were purified using the QIAquick Gel extraction equipment (Qiagen, USA) in accordance with the manufacturer's instructions. The isolated PCR DNA fragment was then ligated to pMOL944 digested with Sacll-Notl and purified. The ligation was carried out overnight at 16 ° C using 0.5 μg of each DNA fragment, 1 U of T4 DNA ligase and regulatory solution for T4 ligase (Boehringer Mannheim, Germany). The ligation mixture was used to transform β. Subtilis PL2306 competent. The transformed cells were seeded on LBPG-10 μg / ml kanamycin plates. Colonies were observed on the plates after 18 hours of incubation at 37 ° C. Several colonies were analyzed by plasmid DNA isolation from the culture broths used at night. One of said positive clones was re-streaked several times on agar plates as previously used, this clone was designated MB594. Clone MB594 was grown overnight in TY-10 μg / ml kanamycin at 37 ° C, and the next day 1 ml of cells was used to isolate the plasmid from the cells using the Qiaprep Spin Plasmid Minippre # 27106 equipment in accordance with the manufacturer's recommendations for plasmid preparations of B. subtilis. This DNA was DNA sequenced and revealed the DNA sequence corresponding to the mature part of mannanase, ie positions 94-1404 of SEQ ID NO: 3 appended. The derived mature protein is shown in SEQ ID NO: 4. It will be seen that the The 3 'end of the mannanase encoded by SEQ ID NO: 1 was changed to one shown in SEQ ID NO: 3 due to the design of the lower primer used in the PCR. The resulting amino acid sequence is shown in SEQ ID NO: 4 and it is apparent that the C-terminal end of SEQ ID NO: 2 (SHHVREIGVQFSAADNSSGQTALYVDNVTLR) is changed to the C-terminal end of SEQ ID NO: 4 (IIMLGK).

TY means (as described in Ausubel, F.M. et al. (Eds) "Current 10 protocols in Molecular Biology." John Wiley and Sons, 1995). Agar LB (as described in Ausubel, F.M. et al. (Eds) "Current protocols in Molecular Biology." John Wiley and Sons, 1995). LBPG is LB agar (see above) supplemented with 0.5% glucose and 0.05 M potassium phosphate, pH 7.0. 15 BPX medium is described in EP 0 506 780 (WO 91/09129).

Expression, purification and characterization of mannanase from Bacillus agaradherens 20 Clone MB 594 obtained as described above in the Materials and Methods section was developed in 25 x 250 ml BPX medium with 10 μg / ml kanamycin in two shake flasks with 500 ml deflectors for 5 days at 37 ° C at 300 rpm. 4d 6,500 ml #flyido were collected from the shake flask culture of clone MB 594 (lot # 9813) and adjusted to pH 5.5. 146 ml of cationic agent (C521) and 292 ml of anionic agent (A130) were added during agitation for flocculation. The flocculated material was separated by centrifugation using a Sorval RC 3B centrifuge at 9000 rpm for 20 minutes at 6 ° C. The supernatant was clarified using Whatman GF / D and C glass filters and finally concentrated in a filter with a cut-off of 10 kDa. 750 ml of this concentrate was adjusted to pH 7.5 using sodium hydroxide. The clear solution was applied to anion exchange chromatography using a 900 ml Q-Sepharose column equilibrated with 50 mM Tris, pH 7.5. The bound mannanase activity was eluted using a gradient of sodium chloride. The pure enzyme gave an individual band on SDS-PAGE with a molecular weight of 38 kDa. The amino acid sequence of the mannanase enzyme, ie the translated DNA sequence, is shown in SEQ ID NO: 2.

Determination of kinetic constants Substrate: Locust bean gum (buffalo) and reducing sugar analysis (PHBAH). Carob bean gum from Sigma (G-0753). Determination of the kinetics using different concentrations of locust bean gum and incubation for 20 minutes at 40 ° C at pH 10 gave Kcat: 467 per second. Km: 0.08 grams per liter. Mol weight: 38 kDa. pl (isoelectric point): 4.2. 5 It was found that the optimum temperature of mannanase is 60 ° C. The pH-activity profile showed maximum activity between pH 8 and 10. DSC analysis with differential scanning calorimetry gives 77 ° C as the melting point at pH 7.5 in Tris buffer, indicating that this enzyme is thermostable. 10 Detergent compatibility analysis using 0.2% of AZCL-locust bean galactomannan as substrate and incubation as described above at 40 ° C demonstrates excellent compatibility with conventional liquid detergents and good compatibility with conventional powder detergents. Obtaining mannase 168 from Bacillus subtilis The β-mannanase from Bacillus subtilis was characterized and purified as follows: The Bacillus subtilis genome was investigated for 20 homology with a known sequence of the gene for β-Mananase from Bacillus spp (Mendoza et al., Biochemistry et Biophysica Acta 1243: 552-554, 1995). The coding region of ydhT, whose product is unknown, showed a 58% similarity to the known Bacillus β-Mananase. The M following oligonucleotides to amplify the sequences encoding the mature portion of the putative β-Mannanase: 5'-GCT CAA TTG GCG CAT ACT GTG TCG CCT GTG-3 'and 5'-GAC GGA TCC CGG ATT CAC TCA ACG ATT GGC G-3 '. The total genomic DNA from Bacillus subtilis strain 1A95 was used as a template to amplify the mature region and dhT using the aforementioned primers. PCR was performed using the GENE-AMP PCR kit with AMPLITAQ DNA Polymerase (Perkin-Elmer, Applied Biosystems, Foster City, CA). An initial melting period at 95 ° C for 5 minutes was followed by 25 cycles of the following program: melting at 95 ° C for 1 minute, tempering at 55 ° C for 2 minutes and extension at 72 ° C for 2 minutes. After the last cycle, the reaction was maintained at 72 ° C for 10 minutes to complete the extension. The PCR products were purified using the QIAquick PCR purification kit (Qiagen, Chatsworth, CA). The mature region and dhT amplified from Bacillus subtilis strain 1A95 was inserted into the expression vector pPG1524 (previously described) as follows: The 1028 bp amplified fragment was digested with Mfe I and BamH I. The expression vector pPg1527 was digested with EcoR I and BamH I. The restriction products were purified using the QIAquick PCR purification kit (Qiagen, Chatsworth, CA). The two fragments were ligated using T4 DNA ligase (13 hours, 16 ° C) and used to transform competent E. coli strain DH5-a. The ampicillin resistant colonies were cultured for the DNA preparations. The DNA was then characterized by restriction analysis. Plasmid pPG3200 contains the mature region of the gene for ydhT. The phasmid pPG3200 was then used to transform the competent PG 632 strain of Bacillus subtilis (Saunders et al., 1992). Seven clones of Bacillus subtilis resistant to kanamycin and one PG 632 control clone were chosen and grown in 20 ml of 20/20/5 medium (20 g / ll of tryptone, 20 g / l of yeast extract, 5 g / l. l of NaCl) supplemented with 1 ml of 25% maltrin, 120 μl of 10 mM MnCl 2 and 20 μl of kanamycin at 50 mg / ml. The clones were grown overnight in 250 ml flasks with baffles shaken at 250 rpm at 37 ° C for protein expression. The cells were centrifuged at 14,000 rpm for 15 minutes. One μl of each supernatant was diluted in 99 μl of 50mM sodium acetate (pH 6.0). One μl of this dilution was tested using the Beta-Mannazyme tablets of endo-1, 4-β-mannanase (Megazyme, Ireland) in accordance with the manufacturer's instructions. The absorbance was read at 590 nm on a Beckman DU640 spectrophotometer. Clone 7 showed high absorbance of 1.67. The PG632 control showed no absorbance at 590 nm. The supernatant was analyzed by SDS-PAGE on 10-20% Tris-Glycine gel (Novex, San Diego, Cal.) To confirm the expected size of the 38kDa protein. The samples were prepared as follows. A 500 μl sample of clone 7 of ydhT and supernatants of PG 632 were precipitated with 55.5 μl of 100% trichloroacetic acid (Sigma), washed with 100 μl of 5% trichloroacetic acid, resuspended in 50 μl of regulatory solution for sample Tris-Glycine SDS (Novex) and boiled for five minutes. One μl of each sample was subjected to gel electrophoresis at 30 mA for 90 minutes. A large protein band was observed that ran at 38 kDa for clone 7 of ydhT. A fermentation of clone 7 of Bacillus subtilis ydhT was carried out in a 10 liter Biostat C fermenter from B. Braun. The fermentation conditions were as follows. The cells were grown for 18 hours in a rich medium similar to 20/20/5 at 37 ° C. At the end of the fermentation, the cells were removed and the supernatant was concentrated to one liter using a tangential flow filtration system. It was determined that the final yield of β-mannanase in the concentrated supernatant was 3 g / l. Purification of the β-mannanase from the supernatant of the fermentation was performed as follows: 500 ml of supernatant was centrifuged at 10,000 rpm for 10 minutes at 4 ° C. The centrifuged supernatant was dialyzed overnight at 4 ° C in two 4-liter exchanges of 10 mM sodium phosphate (pH 7.2) through a 12,000-14,000 cut-off Spectrapor membrane of molecular weight (Spectrum). The dialyzed supernatant was centrifuged at 10,000 rpm for 10 minutes at 4 ° C. A Q Sepharose column of 200 ml fast-flowing anion exchange was equilibrated with 1 liter of 10 mM potassium phosphate solution (pH7.2) at 20 ° C and 300 ml of supernatant was loaded onto the column. Two fractions of the flow of 210 ml (sample A) and 175 ml (sample B) were collected. The two fractions were tested as above, except that the samples were diluted with 199 μl of 50 mM sodium acetate solution (pH 6.0) and these showed absorbance. * ^? ^. ^^ - ^^^^^^ of 0.38 and 0.52 respectively. 2 μl of each sample was added to 8 μl of Tris-glycine SDS sample buffer (Novex, Cal.) And boiled for 5 minutes. The resulting samples were subjected to electrophoresis on a 10-20% Tris-glycine gel (Novex, Cal.) At 30mA for 90 minutes. 5 A major band corresponding to 38 kDa was presented in each sample and it constituted more than 95% of the total protein. A BCA protein test (Pierce) was performed on both samples according to the manufacturer's instructions, using bovine serum albumin as standard. Samples A and B contained 1.3 mg / ml and 1.6 mg / ml of β-mannanase 10 respectively. The identity of the protein was confirmed by ion spraying mass spectrometry and amino-terminal amino acid sequence determination analysis. Purified samples of β-mannanase were used to characterize the activity of the enzymes as follows. All the tests 15 used Beta-Mannazyme tablets with endo-1, 4-β-mannanase (Megazyme, Ireland) as described above. The activity in a range of pH 3.0-9.0 was carried out in 50 mM citrate-based buffer, to determine activity at pH 9.5, in 50 mM CAPSO (Sigma) and for the pH range 10.0-11.0 CAPS buffer was used 50mM. It was found that The optimum pH for Bacillus subtilis β-mannanase is 6.0-6.5. The temperature-activity profiles were made in a 50mM citrate-based buffer solution (pH 6.5). The enzyme showed optimal activity at 40-45 ° C. Bacillus subtilis β-mannanase maintained significant activity less than ? km? **, ~ ka * ~~,. ^? m * aUU? *. ** 15 ° C and more than 80 ° C. The specific activity against β-galactomannan is determined to be 160,000 μmol / min * mg of β-mannanase using Beta-Mannazyme tablets with endo-1,4-β-mannanase (Megazyme, Ireland) in accordance with the manufacturer's instructions . The 5 amino acid and nucleotide sequences of the β-mannanase from Bacillus subtilis are shown in SEQ ID No. 5 and 6. The mannanase is incorporated in the compositions of the invention preferably at a level from 0.0001% to 2%, more preferred from 0.0005% to 0.1%, even more preferred from 0.001% to 0.02% of 10 pure enzyme by weight of the composition. The enzyme of the invention, in addition to the enzymatic core comprising the catalytic domain, further comprises a cellulose binding domain (CBD), the cellulose-binding domain and the enzyme core (the catalytically active domain) of the enzyme being linked together functional way.

The cellulose binding domain (CBD) can exist as an integral part of the encoded enzyme, or a CBD from another source can be introduced to the enzyme, thereby creating an enzymatic hybrid. In this context, the term "cellulose binding domain is designed to be understood as defined by Peter Tomme et al.," Cellulose-Binding Domains: 20 Classification and Properties "in" Enzymatic Degradation of Insoluble Carbohydrates ", John N. Saddier and Michael H. Penner (Eds), ACS Symposium Series, No. 618, 1996. This definition classifies more than 120 cellulose-binding domains in 10 families (lX), and shows that the CBDs are present in various enzymes such as cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. CBDs have also been found in algae, for example the red alga Porfhyra purpurea as a non-hydrolytic protein that binds polysaccharide, see Tomme et al., Op cit. However, the majority of CBD comes from cellulases and xylanases, CBDs are found at the N- and C-terminal ends of proteins or are internal. Enzyme hybrids are known in the art, see for example WO 90/00609 and WO 95/16782, and can be prepared by transforming a DNA construct containing at least one fragment of the DNA encoding a host cell into a host cell. the bound cellulose binding domain, with or without a linker, to a DNA sequence encoding the mannanase enzyme and developing the host cell to express the fused gene. The enzyme hybrids can be described by the following formula: CBD-MR-X in which CBD is the N-terminal region or the C-terminal region of an amino acid sequence corresponding to at least the cellulose binding domain; MR is the middle region (the linker), and may be a bond, or a short linking group of preferably from about 2 to about 100 carbon atoms, more preferably from 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 an N-terminal or C-terminal region of the enzyme of the invention.

The aforementioned enzymes can be of any suitable origin, such as of vegetable, animal, bacterial, fungal and yeast origin. The origin can also be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc). These enzymes can be used in pure or unpurified form. Currently, it is common practice to modify wild-type enzymes by protein / genetic engineering techniques in order to optimize their efficiency of performance in the cleaning compositions of the invention. For example, the variants can be designed in such a way as to increase the compatibility of the enzyme with the ingredients of such commonly encountered compositions. Alternatively, the variant can be designed in such a way that the optimum pH, the stability towards the bleach or the chelator, the catalytic activity and the like of the enzymatic variant are made to measure to suit the cleaning application in particular. In particular, attention must be focused on amino acids sensitive to oxidation in the case of stability to the bleach and surface loads in the case of compatibility with the surfactant. The isoelectric point of such enzymes can be modified by substitution of some charged amino acids, for example, an increase in the isoelectric point can help improve compatibility with anionic surfactants. The stability of the enzymes can be further increased by creating for example additional salt bridges and reinforcing the metal binding sites to increase the stability towards the chelating agent.

The soil release polymer The laundry detergent compositions of the present invention generally contain from 0.0001% to 20%, preferably from 0.001% to 15%, more preferred from 0.01 to 10% by weight of a polyethyleneimine soil release polymer. cotton. The preferred cotton polyethyleneimine soil release polymer is the water soluble or dispersible modified polyamine based cotton soil release agents having a polyamine base structure corresponding to the formula as described in W097 / 42288, filed on April 25, 1997 by Procter & Gamble: H I I [H2N-R] n + 1- [N-R] m- [N-R] n-NH2 having a modified polyamine formula V (n + i) WmYnZ or a polyamine base structure corresponding to the formula: H R [H2N-R] n.k + 1- [N-R] m- [N-R] n- [N-R] k-NH2 having a modified polyamine formula V (n_k + < |) WmY'kZ, where k is less than or equal to n, the base structure of the polyamine prior to m modification has a molecular weight approximately greater than 200 daltons, where i) the units V are terminal units that have the formula: OR E- N-R- or E-N X-R'- or E- N t- R- I I E E E ii) the units W are the base structure units that have the formula: iii) Y units are branching units that have the formula: iv) Z units are terminal units that have the formula: wherein the linking units R of the base structure are selected from the group consisting of C2-C alkylene < 2, alkenylene of C4-C-2, hydroxyalkylene of C3-C- | , C4-C-2 dihydroxyalkylene, dialkylarylene C8-C12, - (R10) XR1-, - (R10) XR5 (0R1) X-, (CH2CH (OR2) CH2O) z (R1?) And RI (OCH2CH (OR2) CH2) w-, -C (Q) (R4) rC (O) -, - e-J CH2CH (OR2) CH2-, and mixtures thereof; where R ^ is alkylene of C2-C6 and mixtures thereof; R2 is hydrogen, - (R10) xB, and mixtures of same; R ^ is C- | -C-8 alkyl. C7-C2 arylalkyl, substituted aryl of C7-C? 2 alkyl, C? -C? 2 aryl, and mixtures thereof; R 4 is alkylene of C- | -C- | 2, alkenylene of C4-C- | 2, arylalkylene of C8-C- | , arylene of C - C-io and mixtures thereof; R5 is C- | -C- | 2 alkylene, C3-C- | 2-dihydroxy-C4-C-2 alkylene hydroxyalkylene, C8-C-2-dialkylarylene, -C (O) -, -C (0) NHR6NHC (0) -, -R1 (0R1) -, -C (0) (R4) rC (0) -, -CH2CH (OH) CH2-, -CH- 2CH (OH) CH20 (R10) and R1? CH2CH (OH) CH2-, and mixtures thereof, R6 is C2-C- | 2 alkylene or C6-C- arylene;; the E units are selected from the group consisting of hydrogen, C- | -C22 alkyl, C3-C22 alkenyl, C7-C2 arylalkyl, C2-C22 hydroxyalkyl, - (CH2) pC02M, - (CH2) qS03M, -CH (CH2C02M) C02M, - (CH2) pP03M, - (R1?) XB, -C (0) R3, and mixtures thereof, with the proviso that when any unit E of a nitrogen is a hydrogen, said Nitrogen is also not an N-oxide; B is hydrogen, Ci-Cß alkyl, - (CH) qS03M, - (CH2) pC02M, (CH2) q (CHS? 3M) CH2S? 3M, - (CH2) q- (CHS02M) CH2S03M, - (CH2) pP03M, -PO3M, and mixtures thereof; M is hydrogen or a cation soluble in water in an amount sufficient to satisfy the charge balance; X is a water soluble anion; k and k 'have a value from 1 to approximately 15; m has the value of 4 to about 400; n has the value from 0 to approximately ttlÉHhr ^ * hM * £ Í * JL 200; p has the value of 1 to 6, q has the value of 0 to 6; r has the value of 0 or 1; w has the value 0 or 1; x has the value of 1 to 100; and has the value from 0 to 100; z has the value of 0 or 1. These polyamines comprise base structures which can be linear or cyclic. The polyamine base structures can also comprise polyamine branching chains to a greater or lesser degree. The polyamine base structures described herein are modified in such a way that at least one, preferably each nitrogen of the polyamine chain is subsequently described in terms 10 of a unit that is replaced, quaternized or combinations thereof. For the purposes of the present invention, the term "modification" which refers to the chemical structure of the polyamines, is defined as replacing a hydrogen atom of the base structure -NH by 15 a unit E (substitution), quatemize a nitrogen of the base structure (quaternized) or oxidize a nitrogen of the base structure to the N-oxide (oxidized). The terms "modification" and "substitution" are used interchangeably when referring to the procedure of replacing a hydrogen atom attached to a base structure nitrogen with an E unit.

The quaternization or oxidation may take place in certain circumstances without substitution, but the substitution is preferably accompanied by the oxidation or quaternization of at least one nitrogen of the base structure. The non-cyclic or linear polyamine base structures that ^ a, "*:? - and ^ -m ^^ r ^^^^^^^^^^^ comprises the amino-functional polymer. They have the general formula: H I I [H2N-R] n + 1- [N-R] m- [N-R] n-NH2 said base structures prior to the subsequent modification comprise primary, secondary and tertiary amine nitrogens connected by the "bonding" units R. The cyclic base polyamine structures comprising the soil release agents in cotton of the present invention have the formula general: I H | R [H2N-R] n-k + l- [N-R] m- [N-R] n- [N-R] k-NH2 said base structures, prior to the subsequent modification, comprise primary, secondary and tertiary amine nitrogens connected by "linker" units R. For the purpose of the present invention, the primary amine nitrogens comprising the base structure or branching chain, once modified, they are defined as "terminal" units V or Z. For example, when a portion of primary amine located at the end of the base structure of the main polyamine or branching chain having the structure H2N-R] - is modified from according to the present invention, it is defined after as a "terminal" unit V, or simply a unit V. However, for the purposes of the present invention, some or all of the primary amine portions may remain unmodified subject to the restrictions described in more detail hereinafter. These unmodified primary amine portions, by virtue of their position in the base structure chain, remain as "terminal" units. Likewise, when a portion of primary amine, located at the end of the main polyamine base structure having the structure -NH2 is modified in accordance with the present invention, is hereinafter defined as a "terminal" unit Z, or simply a unit Z. This unit may remain unmodified subject to the restrictions described in more detail hereinafter. Similarly, the secondary amine nitrogens comprising the base structure or branching chain, once modified, are defined as "base structure" units W. For example, when a secondary amine moiety, the principal constituent of the structures of base and the branching chains of the present invention, having the structure H _. { NR] - is modified in accordance with the present invention, is hereinafter defined as a "base structure" unit W, or simply a unit W. However, for the purposes of the present invention, some or all portions of secondary amine may remain unmodified. These unmodified secondary amine portions, by virtue of their position in the base structure chain, remain as "base structure" units. In another similar form, the tertiary amine nitrogens comprising the base structure or branching chain, once modified, are further defined as "branching" Y units. For example, when a tertiary amine moiety, which is a point of chain branch or of the base structure of polyamine or of other branching chains or rings, which have the structure I _ [NR} - is modified according to the present invention, is defined hereinafter as a "branching" unit Y, or simply a unit Y. However, For the purposes of the present invention, some or all of the tertiary amine moieties may remain unmodified. These unmodified tertiary amine portions, by virtue of their position in the base structure chain, remain as "branching" units. The R units associated with the nitrogens of unit V, W, and Y will be described below. 20 are used to connect polyamine nitrogens. The modified final structure of the polaminas of the present invention can then be represented by the general formula: V (n + 1) WmYnZ for linear polymers of cotton-releasing polyamine, and by the general formula V (n-k + 1) mYnY'kZ for cyclic cotton-based polyamine-releasing polymers. 5 For the case of the polyamines comprising rings, a unit Y 'of the formula: I R -IN-R] - 10 serves as a branch point for a base structure or a branch ring. For each unit Y 'there exists a unit Y having the formula: I _ [N-R] - which will form the connection point of the ring to the polymer chain or branch 15 main. In the single case in which the base structure is a complete ring, the base structure of polyamine has the formula: H I I [H2N-R] n- [N-R] m- [N-R] n- therefore does not comprise any terminal unit Z and has the formula 20 Vn.kWmYnY'k where k is the number of ring forming branching units. Preferably, the polyamine base structures of the present invention do not comprise rings.

In the case of non-cyclic polyamines, the ratio of index n to index m refers to the relative degree of branching. A linear modified polyamine completely unbranched according to the present invention has the formula: 5 VWmZ that is, n is equal to 0. The higher the value of n (the lower the ratio of man), the greater the degree of branch in the molecule. Typically, the value of m varies from a minimum value of 2 to 700, preferably 4 to 400, however, values are also preferred. 10 greater than m, especially when the value of the index n is very low or almost 0. Each polyamine nitrogen, whether primary, secondary or tertiary, once modified according to the present invention, is further defined as being a member of one of two general classes; 15 simple replaced, quaternized or oxidized. Those unmodified polyamine nitrogen units are classified into units V, W, Y, or Z depending on whether they are primary, secondary or tertiary nitrogens. That is, the nitrogens of the unmodified primary amine are units V or Z, the nitrogens of the unmodified secondary amine are units W and the The nitrogens of the unmodified tertiary amine are Y units for the purposes of the present invention. Modified primary amine moieties are defined as "terminal" V units that have one of three forms: J # 6 a) simple substituted units that have the structure: E- - R_ b) quaternized units that have the structure: E I x- E- N + - R- where X is an adequate counter-ion that provides load balance; and c) oxidized units that have the structure: 10 O t E- N-- R- The modified secondary amine portions are defined as "base structure" units W having one of three forms: 15 a) simple substituted units having the structure: - N- -R- b) quaternized units that have the structure: I x- 20 - N + - R- where X is an adequate counter-ion that provides load balance; and c) oxidized units having the structure: you? & ií O t - N- R- The modified tertiary amine moieties are defined as "branching" units and they have one of three forms: a) unmodified units that have the structure: - N-R- c) quaternized units that have the structure: E l x- - N + - R- I where X is an adequate counter ion that provides load balance; and d) oxidized units having the structure: O t - N - R - Certain portions of modified primary amine are defined as "terminal" Z units that have one of three forms: a) simple substituted units that have the structure: -N- E b) quaternized units that have the structure: E l x- - N + - E E where X is an adequate counter-ion that provides load balance; Y d) Oxidized units that have the structure: O t - N - E E When any position on a nitrogen is substituted or unmodified, it is understood that hydrogen will replace E. For example, a primary amine unit comprising an E unit in the form of a hydroxyethyl portion is a terminal unit V having the formula (HOCH2CH2) HN-.

For the purposes of the present invention, there are two types of chain terminator units, units V and Z. The "terminal" unit Z is derived from a terminal primary amino portion of the -NH2 structure. The non-cyclic polyamine based structures according to the present invention, they comprise only one unit Z, while the cyclic polyamines can comprise no unit Z. The "terminal" unit Z can be substituted with any of the units E described in more detail later, except when the unit Z is modified to form an N -oxide. In case the unit Z is oxidized to an N-oxide, the nitrogen must be modified and therefore E can not be a hydrogen. The polyamines of the present invention comprise units "linkers" R of base structure that serve to connect the nitrogen atoms of the base structure. R units comprise units that 5 for the purpose of the present invention are called "hydrocarbyl" units R "and units" oxy R. "The" hydrocarbyl "R units are C 2 -C 2 alkylene, C 4 -C 2 alkylene and C 3 -C 2 hydroxyalkylene in which the hydroxyl portion can take any position on the R unit, except the carbon atoms directly connected to the nitrogens of the structure 10 polyamine base; C4-C- | 2 dihydroxyalkylene wherein the hydroxyl portions can occupy any two of the carbon atoms of the chain of the R unit, except those carbon atoms directly connected to the nitrogens of the polyamine base structure; C8-C- | 2 dialkylarylene which for the purpose of the present invention are 15 arylene portions having two alkyl substituent groups as part of the linker chain. For example, a dialkylarylene unit has the formula: Although the unit does not need to be 1, 4-substituted, it can also be 1, 2 or 1, 3-substituted with C 2 -C 2 alkylene, preferably ethylene, 1,2-propylene and mixtures thereof , most preferably ethylene. The St ^ kSS ^ & ^ i ^ &a ^ S1 units R "oxy" comprise - (R1O) xR5 (OR) x-, CH2CH (OR2) CH20) z (R10) and R1 - (OC ^ CHIOR2) ^) ^, CH2CH (OR2) CH2-, - (Rl?) XRl- and mixtures thereof. Preferred R units are C2-C alkylene < | 2, C3-C- | 2 hydroxyalkylene, C4-C12 dihydroxyalkylene, C8-C12 dialkylarylene, - (R1?) XR1-, -CH2CH (OR2) CH2-, - (CH2CH (OH) CH20) z- (R10) and R1 (OCH2CH-, (OH) CH2) w-, - (R10) XR5 (OR1) X-, most preferred R units are C2-C2 alkylene, C3- C2 hydroxyalkylene, C4-C dihydroxyalkylene < | 2, (R 0) xR1-, - (R 0) xR5 (OR) x-, (CH2CH (OH) CH20) z (R10) and RI (OCH2CH- (OH) CH2) w- and mixtures thereof, even more preferred R units are C2-C2 alkylene, C3 hydroxyalkylene and mixtures of the same, much more preferred are C2-C6 alkylene. The most preferred base structures of the present invention comprise at least 50% R units which are ethylene. The R1 units are C2-C2 alkylene and mixtures thereof, preferably ethylene, R2 is hydrogen and - (R1?) XB, preferably hydrogen. R3 is C- | -C- | 8 alkyl, C7-C2 arylalkylene, substituted aryl C7-C- | 2 alkyl, C6-C? 2 aryl, and mixtures thereof, preferably alkyl C- | -C? 2, C7-C-2 alkylarylene, most preferably C- | -C- | 2 alkyl, more preferably methyl. The R3 units serve as part of the E units described below. R4 is alkylene of C- | -C- | 2, alkenylene of C4-C < 2, C 8 -C 2 arylalkylene, CS-CI Q arylene, preferably C 1 -C 6 alkylene, C 8 -C arylalkylene, most preferably C 2 -C 8 alkylene, more preferably ethylene or butylene. R5 is C -) - C - 2 alkylene, C3 - C - 2 hydroxyalkylene, C4 - C - 2 - dihydroxyalkylene, C8 - C - 2 - dialkylarylene, - C (O) -, - C (0) NHR6NHC (0) -, -C (0) (R4) rC (0) -, R1 (0R1) -, (CH2CH (OH) CH20 (R0) and R1 OCH2CH (OH) CH2-, -C (0) (R4) rC (0) -, 10 (CH2CH (OH) CH2-, R5 is preferably ethylene, -C (O) -, C (0) NHR6NHC (0) -, R1 (0R1) -, -CH2CH (OH) CH2-, (CH2CH (OH) CH20 (R10) and R1? CH2CH- (OH) CH2-, most preferably - (CH2CH (OH) CH2-.

R6 is C2-C-j2 alkylene or C6-C2 | arylene. The preferred R "oxy" units are further defined in terms of the units R ^, R2 and R5. The preferred R "oxy" units comprise the preferred R1, R2 and R5. The preferred polyamine soil release agents of the present invention comprise at least 50% Rl units which are ethylene. The preferred R1, R and R5 units are 20 combine with the R "oxy" units to produce the preferred R "oxy" units in the following manner.

^^^^ X. ^ ^^ ^, ^^^^^^^ n i) substituting the most preferred R5 for (CH2CH20) xR5 (OCH2CH2) x- (CH2CH20) xCH2CHOHCH2- (OCH2CH2) - is produced. ii) substituting preferred R1 and R for (CH2CH (OR2) CH20) z- (R10) and R10 (CH2CH (OR2) CH2) w- occurs - (CH2CH (OH) CH20) z- (CH2CH20) and CH2CH20 (CH2CH (OH ) CH) w-. iii) substituting preferred R2 for -CH2CH (OR2) CH2- produces -CH2CH (OH) CH2-. The E units are selected from the group consisting of hydrogen, C- | -C alkyl, C3-C2 alkenyl, C7-C arylalkyl, C2-C22 hydroxyalkyl, - (CH2) pC02M, - (CH2) qS? 3M, CH (CH2C02M) C02M, - (CH2) nP03M, - (R0) mB, -C (0) R3, preferably hydrogen, C2-C22 hydroxyalkylene, benzyl, C- | -C2 alkylene, - (R10) mB, -C (0) R3, - (CH2) pC02M, - (CH2) qS? 3M, -CH (CH2C02M) C02M, most preferably alkylene of C- | -C2, - (R10) XB, -C (0) R3, - (CH2) pC02M, - (CH) qS? 3M, -CH (CH C0 M) C02M, more preferably alkylene from C < | - C22 > - (R ^ O) xB and -C (0) R3. When no modification or substitution is made on a nitrogen, then the hydrogen atom will remain as the portion representing E. The units E do not comprise a hydrogen atom when the units V, W or Z are oxidized, that is, the nitrogens are N-oxides. For example, the chain of the base structure or branching chains do not comprise units of the following structure: 0 0 t t t _N_R or H- N- R 0 - N-H 5 H H H Additionally, the units E do not comprise carbonyl moieties directly attached to a nitrogen atom when the units V, W and Z are oxidized, that is, the nitrogens are N-oxides. In accordance withthe present invention, the portion -C (0) R3 of the unit E is not bound to a nitrogen modified by N-oxide, that is, there are no N-oxide amides having the structure: OOO 0 0 t II tt II-N- R or R3- C- N- R or - N -C- R3 IIIC = 0 EEI 15 R3 or combinations thereof. B is hydrogen, C < \ -CQ, - (CH) qS? 3M, - (CH) pC02M, (CH2) q- (CHS03M) CH2S? 3M, (CH2) q (CHS02M) CH2S03M, - (CH2) pP03M, - PO3M, preferably hydrogen, - (CH) S? 3M, 20 (CH2) q (CHS? 3M) CH2S? 3M, (CH2) q- (CHS02M) CH2S03M, very preferably hydrogen or - (CH2) qS? 3M.

M is hydrogen or a cation soluble in water in an amount sufficient to satisfy the charge balance. For example, a sodium cation it also satisfies - (CH) pC02M and - (CH2) qS03M, resulting in portions (CH2) pC02Na and - (CH2) qS? 3Na. More than one monovalent cation (sodium, potassium, etc.) can be combined to satisfy the required chemical charge balance. However, the charge of more than one anionic group can be balanced by means of a divalent cation, or more than one monovalent cation may be necessary to satisfy the loading requirements of a polyanionic radical. For example, a - (CH2) pP? 3M portion substituted with sodium atoms has the formula - (CH2) pP? 3Na3. The divalent cations such as calcium (Ca2 +) or magnesium (Mg2 +) can be substituted by or 0 combined with other suitable water-soluble monovalent cations. The preferred cations are sodium and potassium, sodium is very preferred. X is a water-soluble anion such as chlorine (CI-), bromine (Br) and iodine (I "). (I-) or X can be any negatively charged radical such as sulfate (S? 42_) and methosulfate (CH3SO3) .). 5 The formula indices have the following values: p has the value of 1 to 6, q has the value of 0 to 6, r has the value of 0 or 1, w has the value of 0 or 1, x it has the value from 1 to 100, and has the value from 0 to 100, z has the value 0 or 1, m has the value from 2 to 700, preferably from 4 to 400, n has the value from 0 to 350, preferably from 0 to 200; m + n has the value of at least 5. Preferred cotton soil release agents of the present invention comprise polyamine base structures in which less than about 50% of the R units comprise R "oxy" units, preferably less than about 20%, most preferably less than 5%, more preferably the R units do not comprise R "oxy" units. The most preferred cotton soil release agents that do not comprise R "oxy" units comprise polyamine base structures in which less than 50% of the R groups comprise more than 3 carbon atoms. For example, ethylene, 1,2-propylene and 1,3-propylene comprise 3 or fewer carbon atoms and are the preferred R 10"hydrocarbyl" units. That is, when the R units of the base structure are C 2 -C 2 alkylene, C 2 -C 3 alkylene is preferred and more ethylene is preferred. Cotton soil release agents of the present invention comprise modified polyamine base structures 15 homogeneous and non-homogeneous, in which 100% or less of the NH units are modified. For the purpose of the present invention, the term "homogeneous polyamine base structure" is defined as a polyamine base structure having R units that are the same (ie, all are ethylene). However, this definition of equality does not exclude 20 polyamines comprising other foreign units comprising the base structure of the polymer, which are present due to an artifact of the chosen chemical synthesis method. For example, it is known to those skilled in the art that ethanolamine can be used as an "initiator" in * £ já & te, * eifrum ** ^ m í *? ¿. the synthesis of polyethyleneimines, so it would be considered that a polyethyleneimine sample comprising a hydroxyethyl portion resulting from the polymerization "primer" It comprises a homogeneous polyamine base structure for the purposes of the present invention. A base structure 5 of polyamine comprising all R units of ethylene in which no branching units Y are present is a homogeneous base structure. A polyamine base structure comprising all R units of ethylene is a homogeneous base structure regardless of the degree of branching or the number of cyclic branches present. 10 For the purposes of the present invention, the term "Base polymer inhomogeneous structure" refers to structures base polyamine is a mixture of several unit lengths and R unit types R. For example, a non-homogeneous base structure comprises R units that are a mixture of ethylene units and 1, 2-propylene. For the For purposes of the present invention, a mixture of "hydrocarbyl" and "oxy" R units is not necessary to provide a non-homogeneous base structure. Proper handling of these "chain lengths of the R unit" provides the formulator with the ability to modify the solubility and substantivity towards the fabric of the soil release agents in cotton. 20 of the present invention The cotton soil release polymers of the present invention comprise homogeneous polyamine base structures that are wholly or partially substituted by portions ^ •? S? ^^ p ^? M mt WHM ***** "*** polyethyleneoxy, amines wholly or partially quaternised, fully or partially oxidized to N-oxides nitrogens, and mixtures thereof. However, not all amine nitrogens of the base structure must be modified in the same way, leaving the choice of modification at 5 specific needs of the formulator. the degree of ethoxylation is also determined by the specific requirements of the formulator. preferred polyamines comprise the base structure of the compounds of the present invention are generally polyalkylamines (PAA), polyalkyleneimines (PAI), preferably polyethyleneamines (PEA), 10 polyethyleneimines (PEl) or PEA or PEl connected by portions that have longer R units than the PAA, PAI, PEA or PEl of origin. A polyalkyleneamine (PAA) is tetrabutylenepentamine. PEAs are obtained by reactions involving ammonia and ethylene dichloride, followed by fractional distillation. The common AEPs obtained are 15 triethylenetetramine (TETA) and tetreetilenpentamine (TEPA). Above the pentamines, the hexamines ie, heptamines, octaminas and possibly nonaminas, the mixture obtained cogenerically seems not separated by distillation and can include other materials such as cyclic amines and particularly piperazines. Amines may also be present 20 cyclicals with side chains in which the nitrogen atom is present. See patent E.U.A. No. 2,792,372, Dickinson, issued May 14, 1957, which describes the preparation of PEA. The base structures of the preferred amine polymer . * include R units that are C2 (ethylene) alkylene acrylates, also known as polyethylene imines (PEI's). The PEI's preferred have at least moderate branching, that is, the ratio of m to n is less than 4: 1, however, more preferred are PEI's having a ratio of m to n of 2: 1. The basic structures, before the modification, have the general formula: H I I [H2NCH2CH2] n- [NCH2CH2] m- [NCH2CH2] n-NH2 where m and n are the same as those defined above. Preferred PEI's, before modification, will have a molecular weight of more than about 200 daltons. The relative proportions of the amine, primary, secondary and tertiary units in the base structure of the polyamine, especially in the case of PEI's, will vary, depending on the form of preparation. Each hydrogen atom attached to each nitrogen atom of the base structure chain of the polyamine represents a potential site for subsequent substitution, quaternization or oxidation. These polyamines can be prepared, for example, by polymerizing ethyleneimine in the presence of a catalyst such as carbon dioxide, sodium bisulfite, sulfuric acid, hydrogen peroxide, hydrochloric acid, acetic acid, etc. The specific methods for preparing these polyamine base structures are described in the U.S. patent. No. 2,182,306, Ulrich et al., Issued December 5, 1939. ; the patent of E.U. No. 3,033,746, Mayle et al., Issued May 8, 1962; the patent of E.U. No. 2,208,095, Esselman et al., Issued July 16, 1940; the patent of E.U. No. 2,806,839, Crowther, issued September 17, 1957; and the U.S. patent. No. 2,553,696, Wilson, issued May 21, 1951, all incorporated herein by reference. Examples of modified cotton soil release polymers of the present invention comprising PEI's are illustrated in the formulas I-V: Formula I illustrates a preferred cotton soil release polymer comprising a PEI base structure in which all substitutable nitrogens are modified by replacing hydrogen with a polyoxyalkylenoxy unit, - (CH2CH20) 2rjH, which have the formula: Formula I Formula II illustrates a cotton soil release polymer comprising a PEI base structure in which all substitutable nitrogens are modified by hydrogen replacement j ^ ii ^ l ^ a ^ ^ i ü with a polyoxyalkylenoxy unit, - (GH2CH O) 7H having the formula: Formula II This is an example of a cotton blotting polymer that is completely modified with a portion type. Formula III illustrates a cotton soil release polymer comprising a PEI base structure in which all substitutable primary amine nitrogens are modified by replacement of the hydrogen with a polyoxyalkylenoxy unit, - (CH2CH2O) 7H, the The molecule is then modified by subsequent oxidation of all oxidizable primary and secondary nitrogens to the N-oxides, said cotton-releasing polymer having the formula: Formula III Formula IV illustrates a soil-releasing polymer in 10 cotton comprising a PEl base structure in which all the hydrogen atoms of the base structure are substituted and some amine units of the base structure are quaternized. The substituents are polyoxyalkylenoxy units, - (CH 2 CH 20) 7 H or methyl groups. The PEl-modified cotton soil release polymer has the 15 formula: Formula IV Formula V shows a cotton-releasing polymer comprising a PEI base structure in which the nitrogens of the base structure are modified by substitution (ie by - (CH2CH20) 7H or methyl), quaternized, oxidized to N -oxides or combinations thereof. The resultant cotton soil release polymer has the formula: Formula V In the previous examples, not all the nitrogens of a unit class comprise the same modification. The present invention allows the formulator to have ethoxylated a portion of the nitrogens of the secondary amine while having the other nitrogens of the secondary amine oxidized to N-oxides. This also applies to the nitrogens of the primary amine, since the formulator may choose to modify all or a portion of the nitrogens of the primary amine with one or more substituents before oxidation or quaternization. Any possible combination of E groups can be substituted on the nitrogens of the primary or secondary amine, except for the restrictions described hereinabove. The formulator can take advantage of the possibility of modifying the polyamine base structures of the present invention in a manner that allows only the minimum amount of oxidation of the base structures of the substrate. For example, "tempering" with bleach can be achieved before or after formulating. For the purposes of the present invention, the term "bleaching with bleach" is defined as the treatment of the modified polyamine with sufficient bleaching agent to oxidize the base structure 10 against the formulation conditions. By way of example, a polyamine base structure does not necessarily require complete modification by quaternization or N-oxidation to be stable to the bleach. When a sample of modified polyamine base structure is exposed to a suitable bleaching system (eg 15 nonanoyloxybenzenesulfonate / perborate) any nitrogen of the oxidizable base structure under these conditions will be oxidized. However, due to the exact structural properties of the base structure, all or some of the nitrogens in the previous bleach treatment will remain unchanged. Once this tempering has been carried out, the formulator can 20 combine the modified polyamine with the bleaching system and be sure that the polyamine will not consume the total amount of the bleaching agent. Those skilled in the art of bleach formulation will recognize that bleaching with bleach will have its limitations and that it will not ¡Jjgg «a bleach should be used for weaker tempering instead of the bleach of the formulation. In another case, the formulator may wish to add an excess of bleaching agent to the washing detergent composition < During the formulation for the purpose of conducting the "tempering" with bleach in situ during the storage and handling of the formulation. A preferred embodiment of the present invention involves the use of surfactants based on polyhydroxy fatty acid amides in combination with the modified polyamines described herein. The The combination of nonionic surfactant and modified polyamine is especially useful in formulations with low pH, ie at a pH of less than about 10. The polyhydroxy fatty acid amides suitable for use in the low pH embodiments of the present invention are can combine with other appropriate detersive surfactants 15 such as anionic, ampholytic, zwitterionic surfactants and mixtures thereof. Cotton polyethylenimine soil release polymers selected from polyethylene imine 1800E7 and its amine oxide derivatives are preferred for the purpose of the present invention. 20 polyethyleneimine 1200E7 and its oxidized or quaternized derivatives, polyethyleneimine 600E20 and / or mixtures thereof as described in examples 1 to 4 of W097 / 42288. j | i | The detergent compositions for laundry detergents of the invention must contain at least one additional detergent component.The precise nature of this additional component and the levels of incorporation thereof will depend on the physical form of the composition and the nature of the cleaning operation for which it will be used The laundry detergent compositions of the present invention preferably contain further detergent ingredients selected from the group consisting of builder, especially a zeolite, a sodium tripolyphosphate and / layered silicate, a surface active agent, preferably a nonionic surfactant such as alkylethoxylate or alkylmethylglucamide, a conventional soil release polymer and / mixtures thereof Laundry detergent compositions according to the invention may be liquid, in the form of paste, gels , bars, tablet s, spray, foam, powder or granulates. The granulated compositions may also be in "compact" form and the liquid compositions may be in "concentrated" form. The compositions of the invention can be formulated, for example, as hand-wash and machine-wash detergent compositions, including laundry additive compositions and compositions suitable for use in soaking and / or pretreatment of soiled fabrics, by fabric softening compositions added. during rinsing.

When formulated as suitable compositions for use in a washing machine laundry method, the compositions of the invention preferably contain a surfactant and a builder compound, and additionally one or more detergent components preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime soap dispersants, suspending and anti redeposition agents, and corrosion inhibitors. The laundry compositions may also contain softening agents as additional detergent components. Compositions such as those containing a mannanase and a soil release polymer in cotton can provide fabric cleaning performance, stain removal, maintenance of whiteness and appearance of color when formulated as laundry detergent compositions. The compositions of the invention can also be used as detergent additive products in solid or liquid form. Said additive products are designed to complement or enhance the performance of conventional detergent compositions and can be added at any stage of the cleaning process. If required, the density of laundry detergent compositions herein ranges from 400 to 1200 g / liter, preferably from 500 to 950 g / liter of the composition, measured at 20 ° C. The "compact" form of laundry detergent compositions herein is best reflected by the density and, in terms of composition, by the amount of inorganic filler salt; the inorganic filler salts are conventional ingredients of the powder detergent compositions; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition. In compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, and most preferably not exceeding 5% by weight of the composition. The inorganic filler salts such as those referred to in the present compositions are selected from alkali metal and alkali metal salts of sulfates and chlorides. A preferred filler salt is sodium sulfate. The liquid detergent compositions according to the present invention may also be in "concentrated form", in which case, the liquid detergent compositions according to the present invention will have a lower amount of water, compared to conventional liquid detergents. Typically, the water content of the concentrated liquid detergent is preferably less than 40%, more preferred less than 30%, more preferred still less than 20% by weight of the detergent composition. The detergent compounds suitable for use herein are selected from the group consisting of the compounds described | Next.

Surface-active agent system Preferably, laundry detergent compositions 5 in accordance with the present invention may further comprise a surfactant system in which the surfactant may be selected from nonionic and / or anionic and / or cationic and / or ampholytic and / or zwitterionic surfactants and / or semipolar Especially, laundry detergent compositions of the present invention In addition to the enzyme mannanase and the cotton-releasing polymer, they will have a nonionic surfactant, preferably alkyl ethoxylated with a chain length of C8 to C20, more preferred of C? 2 to C16 and a degree of ethoxylation of 2 to 9, preferably 3 to 7 or an alkylmethyl glucamine based surfactant with an alkyl chain length of C8 to 15 C2o, preferably from C? 2 to C18. It has been surprisingly discovered that such compositions provide better cleaning performance, especially in cosmetics and food stains, and better soil release benefits. The other surfactant is typically present at a level of 0.1% to 60% by weight. The preferred levels of incorporation are from 1 to 35% by weight, most preferably from 1 to 30% by weight of the laundry detergent compositions according to the invention. The surfactant is preferably formulated to be ^ tttí fó | compatible with the enzyme components present in the composition. In liquid or gel compositions, the surfactant is most preferably formulated in a manner that promotes, or at least does not degrade, the stability of any enzyme in these compositions. The polyethylene oxide, polypropylene and polybutylene oxide condensates of alkylphenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being more preferred. These compounds include the condensation products of alkylphenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, either in a straight chain or branched chain configuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount from about 2 to about 25 moles, most preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkylphenol. Commercially available nonionic surfactants of this type include Igepaf CO-630, marketed by GAF Corporation; and Triton ™ X-45, X-114, X-100 and X-102, all sold by Rohm & Haas Company. These surfactants are commonly known as alkylphenol alkoxylates (alkylphenol ethoxylates). The condensation products of the primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant system of the present invention. The alkyl chain of the aliphatic alcohol may be either straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. The condensation products of alcohols having an alkyl group containing from about 8 to about 20 carbon atoms, most preferably from about 10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene oxide are preferred. mol of alcohol. Approximately 2 to about 7 moles of ethylene oxide, and most preferably 2 to 5 moles of ethylene oxide per mole of alcohol are present in said condensation products. Examples of commercially available nonionic surfactants of this type include TergitoP "M 15-S-9 (the linear alcohol condensation product of C11-C15 with 9 moles of ethylene oxide), Tergitol ™ 24-L-6 NMW (the primary alcohol condensation product of C- | 2-C- | 4 with 6 moles of ethylene oxide with a limited molecular weight distribution), both marketed by Union Carbide Corporation; NeodolTM 45.9 (e | linear C14-C15 alcohol condensation product with 9 moles of ethylene oxide), Neodol ™ 23_3 (e | C- | 2-C- | 3 linear alcohol condensation product with 3.0 moles of t '- < rii ^ jSw < fi8 ^ S! JfaMd ----- fc? -Ife &, «^ ethylene), NeodolTM 45.7 (the linear condensation product of C-14-C15 with 7 moles of ethylene oxide), NeodolTM 45.5 (e | C14-C15 linear alcohol condensation product with 5 moles of ethylene oxide) commercialized by Shell Chemical Company, Kyro ™ EOB (the condensation product of C13-C-15 alcohol with 9 moles of ethylene oxide), marketed by The Procter & Gamble Company, and Genapol LA 030 or 050 (the condensation product of C- | -C- | 4 alcohol with 3 or 5 moles of ethylene oxide) marketed by Hoechst. The preferred range of HLB in these products is 8-11 and most preferred is 8-10. Also useful as the nonionic surfactant of the surfactant systems of the present invention are the alkylpolysaccharides described in the U.S. patent. No. 4,565,647, Filling, issued January 21, 1986, having a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms, and a polysaccharide, for example, a polyglucoside, a hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 units of saccharide. Any reducing saccharide containing 5 or 6 carbon atoms can be used, for example, glucose, the galactose and galactosyl portions can be substituted for the glucosyl portions (optionally the hydrophobic group is fixed in the 2-, 3- positions , 4-, etc., thus giving a glucose or galactose unlike a glucoside or galactoside). The linkages between saccharides can be, for example, between position one of the additional saccharide units and positions 2-, 3-, 4- and / or 6- of the above saccharide units. Preferred alkyl polyglycosides have the formula R2? (CnH2nO) t (glucosyl) x wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl groups and mixtures thereof, in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14 carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x is from about 1.3 to about 10, preferably about 1.3 to about 3, most preferably from about 1.3 to about 2.7. The glucosyl is preferably derived from glucose. To prepare these compounds, the alkylpolyethoxylated alcohol or alcohol is first formed, and then reacted with glucose or a source of glucose to form the glucoside (attachment at position 1). The additional glucosyl units can then be fixed between their position 1 and the preceding glucosyl units in the 2-, 3-, 4- and / or 6- position, preferably e predominantly in the 2-position. The condensation products of ethylene with one This hydrophobic base formed by the condensation of propylene oxide with propylene glycol is also suitable for use as the additional nonionic surfactant system of the present invention. The hydrophobic portion of these compounds will preferably have a molecular weight of from about 1500 to about 1800, and will exhibit insolubility in water. The addition of polyoxethylene portions to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained to the point where the polyoxethylene content is about 50% of the total weight of the product of 10 condensation, which corresponds to the condensation with up to about 40 moles of ethylene oxide. Examples of compounds of this type include certain commercially available Plurafac ™ LF404 and Pluronic ™ surfactants, marketed by BASF. Also suitable for use as the surfactant is not Ionic of the nonionic surfactant system of the present invention are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine. The hydrophobic portion of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a weight Molecular from about 2500 to about 3000. This hydrophobic portion is condensed with ethylene oxide to the extent that the condensation product contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight faA * ih *** h ^^^ í ^. - ^^^^ ri ^^ r - "fT-Bllltfl ^^ ifeL -'- ^? ll-ÍM '&' T ** • from about 5,000 to about 11,000 Examples of this type of nonionic surfactant include certain of the compounds commercially available TetronicTM? marketed by BASF.

Preferred for use as the nonionic surfactant of the surfactant systems of the present invention are the polyethylene oxide condensates of alkylphenols, the condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene, alkyl polysaccharides and mixtures thereof. The most preferred are ethoxylates of C8-C14 alkylphenol having 3 to 15 ethoxy groups and the ethoxylates of C8-C18 alcohol (preferably from C <| rj average) that they have from 2 to 10 ethoxy groups, and mixtures thereof. The highly preferred nonionic surfactants are the polyhydroxy fatty acid amide surfactants of the formula R2-C-N-Z II I OR R-, wherein R1 is H, or R1 is C1-C4 hydrocarbyl, 2-hydroxyethyl, 2-hydroxy propyl or a mixture thereof, R2 is hydrocarbon of C5-31 and z s polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or a derivative alkoxylated thereof. Preferably, R1 is methyl, R2 is a C11-C15 alkyl chain or straight C16-C18 alkyl or alkenyl such as coconut alkyl or mixtures thereof, and 2 is derived from a reducing sugar such as glucose, fructose, maltose and lactose, in a reductive amination reaction. Suitable anionic surfactants to be used 5 are the alkyl ester sulfonate surfactants which include linear esters of C8-C carboxylic acids rj (ie, fatty acids) which are sulfonated with gaseous SO3 in accordance with "The Journal of the American Oil Chemists Society, "52 (1975), pp. 323-329. Suitable starting materials could include natural fatty substances such as those derived from tallow, palm oil, etc. The preferred alkyl ester sulfonate surfactant, especially for laundry applications, it comprises alkyl ester sulfonate surfactants of the structural formula: O 3 ll 4 -15 R - Chr- - C-OR SO 3M wherein R3 is a hydrocarbyl of C8-C2rj, preferably an alkyl or combination thereof, R4 is a C1-C5 hydrocarbyl, preferably an alkyl or a combination thereof, and M is a cation which forms a salt 20 soluble in water with the alkyl ester sulfonate. Suitable salt-forming cations include metals such as sodium, potassium and lithium, and substituted or unsubstituted ammonium cations such as monoethanolamine, diethanolamine and triethanolamine. Preferably, R3 is C ^ Q-C ^ Q alkyl and R4 is methyl, ethyl or isopropyl. Methyl ester sulfonates in which R3 is C- | o-C- | g alkyl are especially preferred. Other suitable anionic surfactants include 5 alkyl sulfate surfactants which are salts or water soluble acids of the formula ROSO3M, wherein R is preferably a hydrocarbyl of C- | or-C24, preferably an alkyl or hydroxyalkyl having an alkyl component of C- | rj -C2o, most preferably an alkyl or hydroxyalkyl of C- | 2-Ci8, and M is H or a cation, for example, a cation of Alkali metal (e.g., sodium, potassium, lithium), or ammonium or substituted ammonium (e.g., methyl-, dimethyl-, and trimethylammonium cations and quaternary ammonium cations such as tetramethylammonium and dimethylpiperidinium cations and ammonium cations quaternary derivatives of alkylamines such as ethylamine, diethylamine, triethylamine and mixtures thereof, and 15 similar). Typically, the C- | 2- C- | 6 alkyl chains are preferred for lower wash temperatures (e.g., below about 50 ° C) and the C- | 6-18 alkyl chains are preferred for wash temperatures. higher (for example, about 50 ° C). Other anionic surfactants useful for the purposes Detersives can also be included in the laundry detergent compositions of the present invention. These may include salts (including, for example, sodium, potassium, ammonium and substituted ammonium salts such t? aanrt? t? ^ Ai ^ L? or?? as salts of mono-, di- and triethanolamine) of soap, primary or secondary alkanesulfonates of C8-C22 C8-C24 olefinsulfonates, sulfonated polycarboxylic acids prepared by the sulfonation of the pyrolyzed product of alkali earth metal citrates, for example, as the 5 described in the description of British Patent No. 1, 082,179, C8-C24 alkyl polyglycol ether sulfates (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, oleylglycerol fatty sulphonates, ethylene oxide sulphates of alkylphenol, parafin sulfonates, alkyl phosphates, isethionates, such as acyl 10 isethionates, N-acyl taurates, alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates ( especially C- | 2-C- | 8 saturated and unsaturated monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated Cg-C? 2 diesters), acyl sarcosinates, alkylpolyacharide sulfates such as alkylpolyglucoside sulfates (the 15 non-sulphonated non-ionic compounds being described below), branched primary alkyl sulphates and alkyl polyethoxycarboxylates such as those of the formula RO (CH 2 CH 20) -CH COO-M + where R is a C 8 -C 22 alkyl, k is an integer of 1 at 10 and M is a soluble salt forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin and rosin acids, as well as hydrogenated rosin acids present in or derived from tallow oil. Additional examples are described in "Surface Active Agents" and Detergents "(Vol. I and II by Schwartz, Perry and Berch.) A variety of such surfactants are also generally described in U.S. Patent No. 3,929,678, issued December 30, 1975 to Laughiin, and others, in Column 23, line 58 to Column 29, line 23 (incorporated herein by reference) When included therein, the laundry detergent compositions of the present invention typically comprise about 1% to about 40%, preferably about from 3% to about 20% by weight of said anionic surfactants The highly preferred anionic surfactants include the alkoxylated alkyl sulfate surfactants which are water soluble salts or acids of the formula RO (A) mS03M wherein R is a alkyl or hydroxyalkyl group of unsubstituted C < 4C; having an alkyl component of C- | rj-C24, preferably an alkyl or hydroxyalkyl of C- | 2-C2rj, most preferred alkyl or hydroxyalkyl of C- | 2-C- (8, A is an ethoxy or propoxy unit, m is greater than zero, typically between about 0.5 and about 6, most preferably between about 0.5 and about 3, and M is H or a cation which may be, for example, a metal cation (for example, sodium, potassium, lithium, calcium, magnesium, etc.) or an ammonium or substituted ammonium cation. The ethoxylated alkyl sulphates as well as the propoxylated alkyl sulphates are also contemplated herein. Specific examples of substituted ammonium cations include methyl-, dimethyl-, and trimethyl ammonium cations and quaternary ammonium cations such as tetramethylammonium and dimethylpiperidinium cations and those derivatives of aquilamines such as ethylamine, diethylamine, triethylamine, mixtures thereof and the like . Exemplary surfactants are polyethoxylated alkyl sulphate of C? -C- | 8 (1.0) 5 (C- | 2-Ci8E (1.0) M), polyethoxylated alkyl sulfate of C? 2-C < | 8 (2.25) (C < | 2- C- | 8E (2.25) M), polyethoxylated alkyl sulfate of C-] 2-C- | 8 (3-0) (C-j2- C < | 8E (3.0) M), and polyethoxylated alkyl sulphate of C- | -C < | 8 (4-0) C < | -C < | 8E (4.0) M), in which M is conveniently selected from sodium and potassium. The cationic detersive surfactants which are suitable for use in the laundry detergent compositions of the present invention are those having a long chain hydrocarbyl group. Examples of such cationic surfactants include ammonium surfactants such as alkyltrimethyl ammonium halides and those surfactants having the formula: [R2 (OR3) and] [R4 (OR) and] 2RdN + X- wherein R2 is an alkyl or alkylbenzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R3 is selected from the group consisting of -CH2CH2-, -CH2CH (CH3) -, -CH2CH (CH2OH) -, -CH2CH2CH2 -, and mixtures thereof; Each R 4 is selected from the group consisting of C 1 -C 4 alkyl, C 1 -C 4 hydroxyalkyl, benzyl ring structures formed by joining the two groups R 4, -CH 2 CHOH-, -CHOHCOR 6 CHOHCH 2 OH, wherein R 6 is any hexose or hexose polymer having a molecular weight of less than about 1000, and hydrogen when and not being 0; R5 is the same as R4 or is an alkyl chain in which the total number of carbon atoms of R2 plus R ^ is not greater than about 18; each y is from 0 to approximately 10 and the sum of the values and ranges from 0 to approximately 15; and X is any compatible anion. The quaternary ammonium surfactant suitable for the present invention has the formula (I): wherein R1 is a short chain alkyl (C6-C10) or alkylamidoalkyl of the formula (II): Formula II and is 2-4, preferably 3, 20 wherein R2 is H or a C1-C3 alkyl, wherein x is 0-4, preferably 0-2, most preferably 0, wherein R3, R4 and R5 are each the same or different, and can be either a short chain alkyl (C1-C3) or alkoxylated alkyl of It is the formula (III), wherein X "is a counter ion, preferably a halide, for example, chloride or methylisulfate.

Formula III R6 is C- | -C4 and z is 1 or 2. The soluble quaternary ammonium surfactants are those as defined in formula I wherein R1 is Cs, C-io or mixtures thereof, x = o , R3, R4 = CH3 and R5 = CH2CH2OH. Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition, having the formula: RlR2R3R4N + X "(i) wherein R- | is CQ-C ^ Q alkyl, each of R , R3 and R4 is independently C1-C4 alkyl, C1-C4 hydroxyalkyl, benzyl and - (C2H4o) x ^, where x has a value of 2 to 5 and x is an anion. No more than one of R2, R3 or R4 must be benzyl. The preferred length of the alkyl chain for R1 is C < | 2-C < 5, particularly when the alkyl group is a mixture of -fl »¡JSb * t? t ?? chain derived from palm or coconut semíKa fat either synthetically derived by the olefin accumulation or the synthesis of OXO alcohols. The preferred groups for R2, R3 and R4 are methyl and hydroxyethyl groups, and the anion X can be selected from halide, methosulfate, acetate and phosphate ions. Examples of quaternary ammonium compounds of the formula (i) to be used herein are: coconut trimethyl ammonium chloride or bromide; coconut methyl dihydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; dimethyl hydroxyethyl ammonium chloride or bromide of C- | 2-C-); coconut dimethyl hydroxyethyl ammonium chloride or bromide; Methyl Trimethyl Ammonium Methyl Sulfate; chloride or bromide of lauryl dimethyl benzyl ammonium chloride or bromide of lauryl dimethyl (ethenoxy) 4 ammonium; choline esters (compounds of the formula i in which R- | is alkyl of CH-CH2-0-C-C < | 2_ < | 4 and R2R3R4 are methyl).

II O di-alkyl imidazolines [compounds of the formula (i)]. Other cationic surfactants useful herein are also disclosed in the U.S. patent. No. 4,228, 044, Cambre, issued October 14, 1980, and in the European patent application EP 000,224. The cationic fabric softening components include the water-insoluble quaternary ammonium fabric softening actives or their corresponding amine precursor, the di-long alkyl chain ammonium chloride or methylisulfate being most commonly used. Preferred cationic softeners include the following: 1) ditallow dimethyl ammonium chloride (DTDMAC); 2) ditallowhydrogenated dimethyl ammonium chloride; 10 3) diphoshydrogenated dimethyl ammonium methylisulfate; 4) distearyldimethylammonium chloride; 5) dioleyldimethylammonium chloride; 6) dipamitylhydroxyethylmethylammonium chloride; 7) stearylbenzyldimethylammonium chloride; 15 8) sebotrimethylammonium chloride; 9) sebohydrogenadotrimethylammonium chloride; 10) alkylhydroxyethyldimethylammonium chloride of C-J2-14 11) alkyldihydroxyethyldimethylammonium chloride of C-J2-18 »12) di (stearoyloxyethyl) dimethylammonium chloride (DSOEDMAC); 20 13) di (tallowoxyethyl) dimethylammonium chloride; 14) diseboimidazolinium methylisulfate; 15) 1- (2-tallowylamidoethyl) -2-tallowylimidazolinium methylisulfate. The biodegradable quaternary ammonium compounds have been - ^ CT ¿-JJe to jüi¡ fc í ^ s presented as alternatives to ios chlorides and ammonium metiisulfatos chain alkyl di-long used traditionally. Said quaternary ammonium compounds contain long chain alkyl (en) yl groups interrupted by functional groups such as carboxyl groups. Such materials and fabric softening compositions containing them are described in numerous publications such as EP-A-0,040,562 and EP-A-0,239,910. The quaternary ammonium compounds and amine precursors of the present have the formula (I) or (II), below: X " wherein Q is selected from -O-C (O) -, -C (0) -0-, -0-C (0) -0-, NR4-C (0) -, C (0) -NR4-; R1 is (CH2) n-Q-T2 or T3; R2 is (CH2) m-Q-T4 or T5 or T3; R 3 is C 1 -C 4 alkyl or C 1 -C 4 hydroxy alkyl or H; R 4 is H or C 1 -C 4 alkyl or C 1 -C 4 hydroxyalkyl; T "l, T2, T3, T4 and T5 are independently C- or C-) alkyl; n and m are integers from 1 to 4; and X "is a softener-compatible anion.Non-limiting examples of anions compatible with softener include chloride or methylisulfate The T1, T2, T3, T4 and T4 chain of the alkyl or alkenyl must contain at least 11 carbon atoms, preferably at least 16 carbon atoms. the chain may be straight or branched. tallow is a convenient source and inexpensive material alkyl and alkenyl long chain. the compounds are particularly preferred wherein T ^, T2, T3, T4 and T ^ represent the mixture of typical long chain materials for sebum Specific examples of quaternary ammonium compounds to be used in the aqueous fabric softening compositions herein include: 1) N, N-di (tallowyl) oxychloride ethyl) -N, N-dimethylammonium; 2) N, N-di (tallowyloxyethyl) -N-methyl, N- (2-hydroxyethyl) -ammonium methylisulfate; 3) N, N-di ( 2-Seboyl-oxy-2-oxo-ethyl) -N, N-dimethylammon; 4) N, N-di (2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl) -N, N- chloride dimethylammonium 5) N- (2-tallowyl-oxy-2-ethyl) -N- (2-tallowyl-oxy-2-oxo-ethyl) -N, N-dimethyl ammonium chloride; 6) N, N, N-tri (tallowyl-oxy-ethyl) -N-methylammonium chloride; 06 7) r- (2-tallowyl-oxy-2-oxo-etH) -N- (tallowyl-N, N-dimethylammonium chloride and 8) 1,2-disodium-oxy-3-trimethylammoniopropane chloride and mixtures of any of the above materials. When these are included in the laundry detergent compositions of the present invention typically comprise about 0.2% to about 25%, preferably about 1% to about 8% by weight of such cationic surfactants. the laundry detergent compositions of the present invention may also contain ampholytic surfactants, zwitterionic and semipolar, as well as the nonionic and / or anionic surfactants different from those already described hereinabove. The ampholytic surfactants are also suitable for use in the laundry detergent compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or as aliphatic derivatives of heterocyclic secondary or tertiary amines in which the aliphatic radical can be a straight or branched chain. One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic group solubilizable in water, for example, carboxy, sulfate, sulfonate. See the patent of E.U.A. No. 3,929,678 to Laughiin et al., Issued December 30, 1975, column 19, lines 18-35, for examples of ampholytic surfactants. When included therein, the laundry detergent compositions of the present invention typically comprise from about 0.2% to about 15%, preferably from about 1% to about 10% by weight of said ampholytic surfactants. Zwitterionic surfactants are also suitable for use in laundry detergent compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines or quaternary ammonium derivatives, quaternary phosphonium or tertiary sulfonium compounds. See the US patent. No. 3,929,678 to Laughiin et al., Issued December 30, 1975, in column 19, line 38 to column 22, line 48, for examples of zwitterionic surfactants. When included therein, the laundry detergent compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of said zwitterionic surfactants. Semi-polar nonionic surfactants are a special category of nonionic surfactants that include water-soluble amine oxides containing an alkyl portion of from about 10 to about 18 carbon atoms and 2 portions selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-soluble phosphine oxides containing an alkyl portion of about 10 to about 18 carbon atoms and two portions selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water soluble sulfoxides containing an alkyl portion of from about 10 to about 18 carbon atoms and a portion selected from the group consisting of alkyl and hydroxyalkyl portions of from about 1 to about 3 carbon atoms. Semi-polar nonionic surfactants include the amine oxide surfactants having the formula: ## STR3 ## wherein R3 is an alkyl, hydroxyalkyl or alkylphenyl group or mixtures thereof, which contains about 8 to about 22 carbon atoms; R 4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms, or mixtures thereof; x is from 0 to approximately 3; and each R ^ is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms, or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups. The R ^ groups may be attached to each other, for example, through an oxygen or nitrogen atom to form a ring structure. These amine oxide surfactants include, in particular, alkyl-dimethylamine oxides of C- | rj-Ci8 and C8-C- | 2 alkoxyethyldihydroxyethylamine oxides. When included in these, the cleaning compositions of the present invention typically comprise about 10 0.2% to about 15%, preferably from about 1% to about 10% by weight of said semi-polar nonionic surfactants. The laundry detergent composition of the present invention may further preferably comprise a co-agent 15 surfactant selected from the group of primary or tertiary amines. Primary amines suitable for use herein include amines according to the formula R- | NH2, in which R- | is an alkyl chain of 6-C-I8- preferably CQ-C ^ Q, O R4X (CH2) n, X is -0 -, - C (0) NH_ or -NH-, R4 is an alkyl chain of C6- C- | , n is between 1 to 5, preferably 3. The 20 alkyl chains of R < | they may be straight or branched and may be interrupted with up to 12, preferably less than 5, portions of ethylene oxide.

Preferred amines according to the above formula are the n-alkylamines. Amines suitable for use herein may be selected from 1-hexyl amine, 1-octyl amine, 1-decylamine and laurylamine. Other preferred primary amines include oxy-propylamine of Cs-C-io. octyloxypropylamine, 2-ethylexyl-oxypropylamine, lauryl amido propylamine and high propylamine. Tertiary amines suitable for use herein include tertiary amines having the formula R? R R3N, in which R- | and R are alkyl chains of C-j-Cs or R3 is an alkyl chain of C6-C- | 2, preferably C5-C10. or R3 is R4X (CH2) n, where X is -0 -, - C (0) NH_ or -NH-, R4 is a C4-C- | 2, n is between 1 to 5, preferably 2-3. R5 is H or C- | -C alkyl and x is between 1 to 6. R3 and R4 can be linear or branched; the alkyl chains of R3 can be interrupted with up to 12, preferably less than 5 portions of ethylene oxide. The preferred tertiary amines are R- | R2R3N, where R- | is an alkyl chain of C6-C- | 2, R2 and R3, are C6-C3 alkyl or wherein R5 is H or CH-3 and x = 1-2. Also preferred are amidoamines of the formula: O II R-, - C-NH- (CH2) n- N- (R2) 2 where R- | is C alquilo-C alkyl?; n is 2-4, preferably n is 3; R2 and R3 is C1-C4.

The highly preferred amines of the present invention include 1-octylamine, 1-exylamine, 1-decylamine, 1-dodecylamine, C 1 -C 6 oxypropylamine. N coconut 1-3-diaminopropane, cocoalkyldimethylamine, lauryldimethylamine, lauryl bis (hydroxyethyl) amine, coco bis (hydroxyethyl) amine, laurilamine propoxylated with 2 moles, propoxylated octyl amine of 2 moles, lauryl amidopropyldimethylamine, amidopropyldimethylamine of Cß-C-io and amidopropyldimethylamine of C10. The most preferred amines for use in the compositions herein are 1-hexyl amine, 1-octyl amine, 1-decylamine, 1-dodecylamine. Especially desirable are n-dodecyldimethylamine and bishydroxyethylcocoalkylamine and 7-fold ethoxylated oleylamine, lauryl amido propylamine and cocoamidopropylamine.

Bleaching agent The laundry detergent compositions of the present invention may further comprise a bleaching agent such as hydrogen peroxide, PB1, PB4 and percarbonate, with a particle size of 400 to 800 microns. These bleaching agent components may include one or more oxygen bleaching agents and, depending on the bleaching agent chosen, one or more bleach activators. When present, oxygen bleach compounds will typically be present at levels of from about 1% to about 25%. The bleaching agent component for use herein may be any of the bleaching agents useful for cleaning compositions, including oxygen bleaching, as well as other bleaching agents known in the art. The agent of Suitable bleaching in the present invention can be an activated or non-activated bleaching agent. One category of oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include 15 magnesium monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloro perbenzoic acid, 4-nonyllamido-4-oxoperoxybutyric acid and diperoxydecanedioic acid. Said bleaching agents are described in the patent of E.U.A. 4,483,781, patent application of E.U.A. 740,446, European patent application 0,133,354 and US patent. 4,412,934. The agents of The highly preferred bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid, as described in US Pat. 4,634,551. Another category of bleaching agents that can be used encompasses halogen bleaching agents. Examples of agents Hypohalide bleaching include, for example, trichloroisocyanuric acid and the sodium and potassium dichloroisocyanurates and N-chloro and N-bromoalkanesulphonamides. Said materials are usually added from 0.5 to 10% by weight of the finished product, preferably from 1 to 5% by weight. The hydrogen peroxide release agents can be used in combination with bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934), 3,5-trimethylhexanoyloxybenzenesulfonate (ISONOBS, described in EP 120,591 ) or pentaacetylglucose (PAG) or N-nonanoyl-6-aminocaproic acid phenolsulfonate ester (NACA-OBS, described in WO94 / 28106), which are perhydrolyzed to form a peracid as the active bleaching species, which leads to an improved bleaching effect. Also suitable activators are citrated citrate esters such as described in co-pending European patent application No. 91870207.7 and the asymmetric acyclic imide bleach activator of the following formula, as described in the co-pending patent applications of Procter & Gamble Serial No. US 60 / 022,786 (filed July 30, 1996) and No. 60 / 028,122 (filed October 15, 1996): ^ J? E ^^ ... ^ - -i &Js &u where Ri is a straight or branched chain saturated or unsaturated alkyl group of C-C3, R2 is a straight-chain saturated or unsaturated alkyl group or branched Ci-Cs and R3 is a straight or branched chain saturated or unsaturated alkyl group of C -? - C. Useful bleaching agents including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleach compounds for use in the detergent compositions according to the invention are described in the co-pending applications of the authors USSN 08 / 136,626, PCT / US95 / 07823, W095 / 27772, W095 / 27773, W095 / 27774 and W095 / 27775. Hydrogen peroxide may also be present by adding an enzyme system (i.e., an enzyme and a substrate therefor) which is capable of generating hydrogen peroxide at the start or during the washing and / or rinsing process. Such enzyme systems are described in patent application EP 91202655.6, filed on October 9, 1991. Metal-containing catalysts for use in bleaching compositions include cobalt-containing catalysts, such as cobalt (III) salts of pentaamine acetate and manganese-containing catalysts, such as those described in EPA 549 271; EPA 549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US 5,114,611. A bleaching composition comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent, is described in patent application No. 94870206.3. Bleaching agents other than oxygen bleaching agents are also known in the art and can be used herein. One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated phthalocyanines of zinc and / or aluminum. These materials can be deposited on the substrate during the washing process. After irradiation with light, in the presence of oxygen, such as hanging garments to dry in daylight, sulfonated zinc phthalocyanine is activated and, as a result, the substrate is bleached. The preferred zinc phthalocyanine and a photo-active bleaching process are described in the US patent. 4,033,718. Typically, laundry detergent compositions will contain from about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine.

Preferred detergency system Preferably, the laundry detergent compositions according to the present invention may further comprise a builder system, more preferably a zeolite, a sodium tripolyphosphate and / or a layered silicate. It has been discovered, surprisingly, that such compositions provide better cleaning performance, especially in cosmetics and food stains and better soil release benefits.

Mh ^ ^ ^^^ HhiltM - Any conventional builder system is suitable for use herein, including aluminosilicate materials, silicates, polycarboxylates and fatty acids, materials such as ethylenediamine tetraacetate, diethylenetriamine pentamethylene-acetate, metal ion sequestrants such as aminopolyphosphonates, particularly ethylenediaminetetra-methylenephosphonic acid and diethylenetriamine pentamethylene-phosphonic acid. Phosphate builders can also be used herein. Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, most particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP. Another suitable inorganic builder material is the layered silicate, for example, SKS-6 (Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na2Si? 5). Suitable polycarboxylates contain a carboxy group and include lactic acid, glycolic acid and ether derivatives thereof, such as those described in Belgian patents Nos. 831, 368, 821, 369 and 821, 370. Polycarboxylates containing two carboxy 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, as well as the ether carboxylates described in German Patent 2,446,686. and 2,446,687 and in the U.S. patent No. 3,935,257, and the sulfinyl carboxylates described in Belgian Patent No. 840,623. Polycarboxylates containing three carboxy groups include, in particular, the water-soluble citrates, aconitrates and citraconates, as well as the succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 5,379,241, the lactoxysuccinates described in the application. Dutch 7205873, and oxypolycarboxylate materials such as 2-oxa-1, 1-3-propane tricarboxylates described in British Patent No. 1, 387,447. Polycarboxylates containing four carboxy groups include the oxydisuccinates described in British Patent No. 1, 261, 829, 10 1, 1, 2,2-ethane tetracarboxylates, 1, 1, 3,3-propane tetracarboxylates and 1, 1, 2,3-propane tetracarboxylates. Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives described in British Patent Nos. 1, 398,421 and 1, 398,422, and in the US patent. No. 3,936,448, as well as the sulfonated pyrolysed citrates described in the British patent No. 1, 082,179, while polycarboxylates containing phosphon substituents are described in British Patent No. 1, 439,000. Alicyclic and heterocyclic polycarboxylates include cyclopentan-cis.cis.cis-tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydrofuran-cis, cis, cis-tetracarboxylates, 2,5-tetrahydrofuran-cis-20 dicarboxylates, 2, 2,5,5-tetrahydrofuran-tetracarboxylates, 1, 2,3,4,5,6-hexan-hexacarboxylates and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromatic polycarboxylates include melific acid, pyromellitic acid and the phthalic acid derivatives described in British Patent No. 1, 425,343. Of the above, the preferred polycarboxylates are hydroxycarboxylates containing up to three carboxy groups per molecule, very particularly citrates. Preferred builder systems for use in the present compositions include a mixture of a water insoluble aluminosilicate builder such as zeolite A, or a layered silicate (SKS-6) and a water soluble carboxylate chelating agent. such as citric acid, other preferred builder systems include a mixture of a water insoluble aluminosilicate builder such as zeolite A and a water soluble carboxylate chelating agent such as citric acid. The builder systems that are preferred to be used in the liquid detergent compositions of the present invention are soaps and polycarboxylates. Other detergency builders that may form part of the builder system for use in granular compositions include inorganic materials such as carbonates, bicarbonates, alkali metal silicates and organic materials such as organic phosphonates, amino polyalkylene phosphonates and amino polycarboxylates. Other suitable water-soluble organic salts are homo- or copolymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Polymers of this type are i * & - describe in GB-A-1, 596,756. Examples of such salts are the polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, said copolymers have a molecular weight of from 20,000 to 70,000, especially about 40,000. Builder salts are usually included in amounts of from 5% to 80% by weight of the composition, preferably from 10% to 70% and most commonly from 30% to 60% by weight.

Conventional Detergent Enzymes Laundry detergent compositions may contain, in addition to the mannanase enzyme, one or more enzymes that provide performance benefits of cleaning, fabric care and / or sanitation benefits. Said enzymes include selected enzymes of cellulases, hemicellulases, peroxidases, proteases, glucoamylases, amylases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tanases, pentosanas, malanases. , ß-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase or mixtures thereof. A preferred combination is a laundry detergent composition having a cocktail of conventional applicable enzymes such as protease, amylase, lipase, cutinase and / or cellulase, in conjunction with one or more plant cell wall degrading enzymes.

Suitable proteases are the subtilisins that are obtained from particular strains of B.subtilis and B.licheniformis (subtilisin BPN and BPN '). A suitable protease is obtained from a Bacillus strain, having a maximum activity throughout the pH range of 8 to 12, developed and sold as ESPERASE ^ by Novo Industries A / S of Denmark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1, 243,784, for Novo. Other suitable proteases include ALCALASE®, DURAZYM® and SAVINASE® from Novo and MAXATASE®, MAXACAL®, PROPERASE® and MAXAPEM® (Maxacal manipulated with proteins) from Gist-Brocades. Proteolytic enzymes also include modified bacterial serine proteases, such as those described in European Patent Application No. 87303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98) and which is referred to herein as "Protease. B ", and in the European patent application EP 199 404, Venegas, published on October 29, 1986, which refers to a modified bacterial serine protease that is called in the present" Protease A ". More preferred herein is the so-called "Protease C" which is a variant of a Bacillus alkaline serine protease in which lysine replaces arginine in position 27, tyrosine replaces valine in position 104, serine replaces asparagine in position 123 and alanine replaces threonine at position 274. Protease C is described in EP 90915958.4, which corresponds to WO 91/06637, published May 16, 1991. Genetically modified variants, particularly protease C, are also included herein. A preferred protease referred to as "protease D" is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for the amino acid residue in said carbonyl hydrolase equivalent to position +76, preferably also in combination with one or more amino acid residue positions equiv those selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, 10 +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and / or +274 compliance with the numeration of the subtilisin of Bacillus amyloliquefaciens as described in WO 95/10591 and in the patent application of C. Ghosh, et al, "Bleaching Compositions Comprising Protease Enzymes", which has the serial number of EU 08 / 322,677, submitted on 13 October 15, 1994. A carbonyl hydrolase variant of the protease described in WO95 / 10591, having an amino acid sequence obtained by replacing a plurality of amino acid residues replaced in the precursor enzyme, is also suitable for the present invention. corresponding to position +210 in combination with one or more 20 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 a subtilisin present in nature from Bacillus ^ ^ ^ * ^ .. J amM * ^? - amyloliquefaciens or equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin (US Patent Application Serial No. 60/048 550, filed 4 June 1997). Also suitable for the present invention are the proteases described in patent applications EP 251 446 and WO 91/06637, the BLAP® protease described in WO91 / 02792 and their variants described in WO 95/23221. See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO 93/18140 A for Novo. Enzymatic detergents comprising protease, one or more other different enzymes and a reversible protease inhibitor are described in WO 92/03529 A for Novo. When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 95/07791 to Procter & Gamble. A recombinant trypsin-like protease for detergents suitable herein is described in WO 94/25583 for Novo. Other suitable proteases are described in EP 516 200 by Unilever. The proteolytic enzymes are incorporated in the laundry detergent compositions of the present invention at a level of from 0.0001% to 2%, preferably from 0.001% to 0.2%, most preferably from 0.005% to 0.1% pure enzyme by weight of the composition. Cellulases useful in the present invention include both bacterial and fungal cellulases. Preferably, they will have an optimum pH between 5 and 12 and an activity greater than 50 CEVU (cellulose viscosity unit). Suitable cellulases are described in the U.S.A. No. 4,435,307, Barbesgoard et al, J61078384 and WO96 / 02653 which describe a fungal cellulase produced respectively from Humicola insolens, Trichoderma, Thievalia and Sporotrichum. EP 739 982 describes cellulases isolated from novel species of Bacillus. Suitable cellulases are also described in GB-A-2,075,028; GB-A-2,095,275; DE-OS-2,247,832 and WO 95/26398. Examples of said cellulases are cellulases produced by 10 a strain of Humicola insolens (Humicola grísea var thermoidea.), Particularly the Humicola strain DSM 1800. Other suitable cellulases are the cellulases originated from Humicola insolens that have a molecular weight of approximately 50 KDa, an isoelectric point of 5.5, and that contain 415 amino acids, and one 15 ~ 43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence described in PCT patent application No. WO 91/17243. Also suitable cellulases are the EGIII cellulases of Trichoderma longibrachiatum described in WO 94/21801, Genencor, 20 published September 29, 1994. Particularly suitable cellulases are cellulases that have color care benefits. Examples of said cellulases are the cellulases described in the European patent application No. 91202879.2, filed on November 6, 1991 (Novo) Carezyme and Gelluzyme (Novo Nordisk A / S) are especially useful. See also WO 91/17244 and WO 91/21801. Other cellulases suitable for fabric care and / or cleaning properties are described in WO 96/34092, W096 / 17994 and WO 95/24471. Said cellulases are normally incorporated in the laundry detergent composition at levels of 0.0001% to 2% pure enzyme by weight of the laundry detergent composition. Peroxidase enzymes are used in combination with oxygen sources, for example, percarbonate, perborate, persulfate, hydrogen peroxide, etc., and with a phenolic substrate as a bleach enhancing molecule. They are used for "bleaching in solution", that is, to avoid the transfer of dyes or pigments removed from substrates during washing operations, to other substrates in the washing solution. Peroxidase enzymes are known in the art and include, for example, horseradish peroxidase, ligninase, and haloperoxidase such as chloro- and bromo-peroxidase. Laundry detergent compositions containing peroxidase are described, for example, in the PCT International Application WO89 / 099813, WO 89/09813 and European Patent Application No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, filed on February 20, 1996. Also suitable is the laccase enzyme. The improvers are generally comprised at a level of 0.1% to 5% by weight of the total composition. Preferred improvers are substituted phenoxyzine and phenoxyzine, 10-phenothiazinopropionic acid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazinopropionic acid (POP) and 10-methylphenoxazine (described in WO 94/12621). and substituted syringates (substituted C3-C5 alkylsalicylates) and phenols. Sodium percarbonate or perborate are sources of hydrogen peroxide that are preferred. Said peroxidases are normally incorporated in the laundry detergent composition at levels of 0.0001% to 2% active enzyme by weight of the laundry detergent composition. Other preferred enzymes that can be included in the compositions Laundry detergents of the present invention include lipases. Suitable lipase enzymes for detergent use include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, such as those described in British Patent 1, 372, 034. Suitable lipases include those that show a 15 positive immunological cross-reaction with the lipase antibody, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano", hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, 20 lipases ex Chromobacter viscosum, for example Chromobacter viscosum var. lipoliticum NRRLB 3673, from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp, E.U.A. and Disoynth Co., Holland and lipases ex Pseudomonas gladioli. Lipasas especially jJi? e ** -. suitable are lipases such as M1 Lipase® and Lipomax® (Gist-Brocades) and Lipolase® and Lipolase Ultra® (Novo), which have been found to be very effective when used in combination with the compositions of the present invention. Also suitable are the lipolytic enzymes described in EP 258 068, WO 92/05249 and WO 95/22615 by Novo Nordisk, and in WO 94/03578, WO 95/35381 and WO 96/00292 by Unilever. Also suitable are cutinases [EC 3.1.1.50] that can be considered as a special type of lipase, namely lipases that do not require interfacial activation. The addition of cutinases to laundry detergent compositions has been described in for example, WO-A-88/09367 (Genencor); WO 90/09446 (Plant Genetic System), and WO 94/14963 and WO 94/14964 (Unilever). Lipases and / or cutinases are normally incorporated into the laundry detergent composition at levels of 0.0001% to 2% pure enzyme by weight of the laundry detergent composition. Amylases (a and / or ß) can be included for the removal of carbohydrate-based stains. WO94 / 02597, Novo Nordisk A / S, published on February 3, 1994, discloses detergent compositions that incorporate mutant amylases. See also WO / 95/10603, Novo Nordisk A / S, published April 20, 1995. Other amylases to be used in detergent compositions include and β-amylases. A-amylases are known in the art and include those described in the U.S. patent. Do not. 5,003,257; EP 252,666; WO / 91/00353; RF 2,676,456; EP 285,123; EP 525,610; EP 368,341; and in the description of British Patent No. 1, 296,839 (Novo). Other suitable amylases are the amylases of improved stability described in W094 / 18314, published August 18, 1994 and WO 96/05295, Genencor, published February 22, 1996, and the amylase variants having further modification in the immediate parent, available from Novo Nordisk A / S and described in WO95 / 10603, published April 1995. Also suitable are the amylases described in EP 277 216, WO 95/26397 and WO 96/23873 (all by Novo Nordisk). 10 Examples of commercial α-amylases products are Purafect Ox Am®, Termamyl®, Ban®, Fungamyl® and Duramyl®, all available from Novo Nordisk A / S Denmark. W095 / 26397 describes other suitable amylases: α-amylases characterized in that they have a specific activity at least 25% greater than the specific activity of Termamyl® in a 15 temperature range from 25 ° C to 55 ° C and at a pH value in the range of 8 to 10, as measured by the Phadebas test of a-amylase activity. The variants of the previous enzymes, described in the document, are appropriate W096 / 23873 (Novo Nordisk). Other amylolytic enzymes with improved properties with respect to the activity level and the combination of 20 thermostability and higher activity level are described in W095 / 35382. The amylolytic enzymes are incorporated in the laundry detergent compositions of the present invention at a level of from 0.0001% to 2%, preferably from 0.00018% to 0.06%, very preferably from 0.00024% to 0.048% pure enzyme by weight of the composition. The aforementioned enzymes may have any suitable origin, such as vegetable, animal, bacterial, fungal and yeast. 5 The origin can also be mesophilic or extremophile (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidic, halophilic, etc.). The purified or non-purified forms of these enzymes can be used. These days it is a common practice to modify wild-type enzymes by means of genetic manipulation or protein techniques to optimize their efficiency. 10 performance in laundry detergent compositions of the invention. For example, the variants can be designed in such a way that the compatibility of the enzyme with the ingredients of said commonly found compositions is increased. Alternatively, the variant can be designed in such a way that the optimum pH, the stability in bleach or The chelator, the catalytic activity and the like of the enzyme variant are designed to suit the particular cleaning application. In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface charges for compatibility with the surfactant. He The isoelectric point of said enzymes can be modified by replacing some charged amino acids, for example, an increase in the isoelectric point could help improve compatibility with anionic surfactants. The stability of the enzymes can increase ~ - - "*" "« n ***. more by creating additional salt bridges for example, and reinforcing the calcium binding sites to increase stability towards the chelator. Particular attention should be paid to cellulases, since most cellulases have separate binding domains (CBD). The properties of these enzymes can be altered by modifying these domains. Said enzymes are normally incorporated in the laundry detergent composition at levels of 0.0001% to 2% pure enzyme by weight of the laundry detergent composition. Enzymes can be added as separate individual ingredients (pellets, granules, stabilized liquids, etc. containing an enzyme) or as mixtures of two or more enzymes (eg cogranulates). Other suitable detergent ingredients that may be added are the enzyme oxidation scavengers which are described in co-pending European patent application 92970018.6, filed on January 31, 1992. Examples of such enzyme oxidation scavengers are the ethoxylated tetraethylenepolyamines. A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 and WO 9307260 for Genencor International, WO 8908694 A for Novo, and E.U. 3,553,139, January 5, 1971 to McCarty and others. Enzymes are also described in E.U.A. 4,101, 457, Place and others, July 18, 1978 and in E.U. 4,507,219, Hughes, March 26, 1985. The «- ttM ^^ p ,, .. n ^. ^ JMh. ^^^ t .. i Enzyme materials useful for liquid detergent formulations and their incorporation into such formulations are described in E.U. 4,261, 868, Hora et al., April 14, 1981. The enzymes that will be used in detergents can be stabilized by various techniques. Enzyme stabilization techniques are described and exemplified in E.U. 3,600,319, August 17, 1971, Gedge et al., EP 199,405 and EP 200,586, October 29, 1986, Venegas. Enzyme stabilization systems are also described, for example, in E.U. 3,519,570. A Bacillus sp. AC13 useful and which gives proteases, xylanases and cellulases is described in WO 9401532 A for Novo.

Benefits of color care Technologies that provide a type of color care benefit can also be included. Examples of these technologies are metallocatalysts for color maintenance. Said metallocatalysts are described in copending European patent application No. 92870181.2. Coloring agents, dispersion of polyolefin for anti-wrinkles and improved water absorbency, perfume and aminofunctional polymer (PCT / EUA97 / 16546) for the treatment of color care and perfume substantivity are additional examples of fabric care / color care technologies and are described in co-pending patent application No. 96870140.9, filed November 7, 1996. Fabric softening agents may also be incorporated into laundry detergent compositions in accordance with the present invention. These agents may be of inorganic or organic type. Inorganic softening agents are exemplified by the smectite clays described in GB-A-1 400 898 and in the US patent. No. 5 5,019,292. Organic fabric softening agents include water-insoluble tertiary amines such as those described in GB-A1 514 276 and EP-BO 011 340 and their combination with C12-C14 mono-saccharose ammonium salts are described in EP-BO 026 527 and EP -BO- 026 528 and the double long chain amides as described in EP-BO 242 919. Other ingredients Useful organic fabric softener systems include the high molecular weight polyethylene oxide mattes as described in EP-A-0 299 575 and 0 313 146. Smectite clay levels are usually in the range of 2% to 20%, most preferably from 5% to 15% by weight, 15 adding the material as a dry mixed component to the rest of the formulation. Organic fabric softening agents such as water-soluble tertiary amines or double long chain amide materials are incorporated at levels of 0.5% to 5% by weight, normally from 1% to 3% by weight, while the materials of heavyweight polyethylene oxide Molecular and water-soluble cationic materials are added at levels from 0.1% to 2%, usually from 0.15% to 1.5% by weight. These matepales are usually added to the spray-dried portion of the composition, although in some cases it may be more convenient to add them as a particulate material mixed in dry, or sprayed as a melted liquid over the other solid components of the composition.

Chelating Agents Laundry detergent compositions herein may also optionally contain one or more iron and / or manganese chelating agents. Such chelating agents can be selected from the group consisting of aminocarboxylates, aminophosphates, polyfunctionally substituted aromatic chelating agents and mixtures thereof, all as defined below. Without intending to be limited by theory, it is believed that the benefit of these materials is due in part to their exceptional ability to remove iron and manganese ions from the washing solutions through the formation of soluble chelates. Aminocarboxylates useful as optional chelating agents include ethylenediaminetetracetates, N-hydroxyethylenediamine triacetates, nitrilotriacetates, ethylenediaminetetraproprionates, triethylenetetra-aminohexacetates, diethylenetriaminepentaacetates and ethanoldiglicines, substituted alkali metal, ammonium and ammonium salts herein and mixtures herein. The aminophosphonates are also useful for use as chelating agents in the compositions of the invention when at least low levels of total phosphorus are allowed in the laundry detergent compositions and include ethylene diamine tetrakis (methylene phosphonates) as DEQUEST. Preferably, these aminophosphonates do not contain alkyl or alkenyl groups with more than about 6 carbon atoms. Polyfunctionally substituted aromatic chelating agents are also useful in the compositions herein. See the US patent. 3,812,044 issued May 21, 1974 to Connor et al. Preferred compounds of this type in acid form are dihydroxydisulfobenzenes such as 1,2-dihydroxy-3,5-disulfobenzene. A biodegradable chelator that is preferred to be used herein is ethylene diamine disuccinate ("EDDS"), especially the [S, S] isomer as described in the U.S. patent. 4,704,233, November 3, 1987 for Hartman and Perkins. The compositions herein may also contain water-soluble salts of methyl glycine diacetic acid (MGDA) (or acid form) as a useful chelator or co-builder with, for example, insoluble builders such as zeolites, layered silicates and the like. If used, these chelating agents should generally comprise from about 0.1% to about 15% by weight of the laundry detergent compositions herein. Most preferably, if used, the chelating agents should comprise from about 0.1% to about 3.0% by weight of said compositions. Í34 Foam suppressor Another optional ingredient is a foam suppressor exemplified by silicones and silica-silicone blends. The silicones can generally be represented by the alkylated polysiloxane materials while the silicas are normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. These materials can be incorporated as particles in which the suds suppressor is advantageously and releasably incorporated in a detergent impermeable vehicle substantially not active on surfaces, dispersabie or soluble in water. Alternatively, the foam suppressant can be dissolved or dispersed in a liquid vehicle and applied by spraying on one or more of the other components. A preferred silicone foam control agent is described in Bartollota et al., U.S. Pat. No. 3,933,672. Other particularly useful foam suppressors are the self-emulsifiable silicone foam suppressors described in the German patent application DTOS 2 646 126, published on April 28, 1977. An example of said compound is DC-544, commercially available from Dow Corning, which is a copolymer of syloxane-glycol. Especially preferred foam control agents are the foam suppressor system comprising a mixture of silicone oils and 2-alkyl-alkanols. Suitable 2-alkyl-alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R.

Said foam suppressor systems are described in co-pending European patent application No. 92870174.7, filed on November 10, 1992. Especially preferred silicone foam control agents are described in copending European patent application No. 92201649. 8. Said compositions may comprise a mixture of silica / silica in combination with nonporous fuming silica such as Aerosil.RTM. The foam suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1% by weight.

Other components Other components used in laundry detergent compositions, such as soil suspending agents, soil release agents, optical brighteners, abrasives, bactericides, stain inhibitors, color delivery agents and / or encapsulated perfumes can be employed and can not be used. encapsulated Especially suitable encapsulating materials are water-soluble capsules consisting of a matrix of polysaccharide and polyhydroxyl compounds such as those described in GB 1, 464,616. Other suitable water-soluble encapsulating materials comprise dextrins derived from non-gelatinized starch acid esters of substituted dicarboxylic acids such as those described in US 3,455,838. These 116 acid-ester dextrins are preferably prepared from starches such as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of such encapsulating materials include N-Lok, manufactured by National Starch. The N-Lok encapsulating material consists of a modified corn starch and glucose. The starch is modified by adding monofunctional substituted groups such as octenyl succinic acid anhydride. Suitable antiredeposition and slurry suspending agents herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or copolymeric polycarboxylic acids or their salts. Polymers of this type include the polyacrylates and the maleic anhydride-acrylic acid copolymers mentioned above as builders, as well as copolymers of maleic anhydride with ethylene, methyl vinyl ether or methacrylic acid, constituting maleic anhydride at least 20 mol% of the copolymer. These materials are normally used at levels of from 0.5% to 10% by weight, most preferably from 0.75% to 8%, more preferably from 1% to 6% by weight of the composition. Preferred optical brighteners are of an anionic character, examples of which are 4, 4-bis- (2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2: 2'-disulfonate dioxide, 4, -4 '-bis- (2-morpholino-4-anilino-s-triazin-6-ylamino-stilbene-2: 2-disulfonate disodium, 4,4'-bis- (2,4-dianilino-s-tr¡az) Disodium n-6-ylamino) stilben-2: 2'-d-sulphonate, 4 ', 4"-bis- (2,4-dianylin-s-triazin-6-ylamino) stilben-2-sulfonate monosodium, 4,4'-bis- (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylammon) stilbene-2,2'-disulfonate disodium, 4,4'-bis - (4-phenyl-2,1, 3-triazol-2-yl) -stilben-2,2'-disulfonate disodium, 4,4'bis (2-anilino-4- (1-methyl-2-hydroxyethylamino) -s-triazin-6-ylamide-no) stilben-2,2'-disulfonate disodium, 2 (stilbe-4"- (naphtho-1,, 2 ': 4.5) -1, 2,3-triazole-2" sodium-4-sulfonate-4,4-bis (2-sulfostyril) biphenyl The highly preferred brighteners are the specific brighteners described in EP 753 567. Other polymeric materials Useful are polyethyleneglucoles, particularly those with a molecular weight of 1000-10000, very 10 particularly 2000 to 8000 and most preferably approximately 4000. These are used at levels of from 0.20% to 5%, most preferably from 0.25% to 2.5% by weight. These polymers and the abovementioned homo- or copolymeric polycarboxylate salts are valuable because they improve the maintenance of whiteness, prevent the deposition of ashes in the fabric and 15 improve the cleaning performance on clay, proteinaceous and oxidizable soils in the presence of transition metal impurities.

Conventional dirt release polymers Preferably laundry detergent compositions 20 of the present invention will comprise another conventional soil release polymer. Such compositions provide better cleaning and dirt release performance. The appropriate soil release polymer is polyester with anionically blocked ends and conventionally t38 copolymers or terpolymers of terephthalic acid with ethylene glycol and propylene glycol units in various arrangements. Examples of such polymers are described in the patents of E.U.A. Nos. 4116885 and 4711730 commonly assigned, and in published European patent application No. 0 272 033. A particularly preferred polymer in accordance with EP-A-0 272 033 has the formula: (CH3 (PEG) 43) o.75 (POH) 0.25 [T-PO) 2.8 (T-PEG) o.4] - T (POH) o.25 ((PEG) 43CH3) o.75 where PEG is - (OCH2H4) 0-, PO is ( OC3H6O) and T is (pcOC6H4CO). Also very useful are modified polyesters such as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propanediol, the end groups consisting primarily of sulfobenzoate and secondarily of monoesters of ethylene glycol and / or propane diol. The objective is to obtain a polymer blocked at both ends by sulfobenzoate groups; "primarily", in the present context, means that the majority of said copolymers herein will be blocked at their ends by sulfobenzoate groups. However, some copolymers will be less than completely blocked and therefore their end groups may consist of monoester of ethylene glycol and / or propane 1-2 diol, thereof, consisting "secondarily" of said species. The polyesters selected herein contain about 46% by weight of dimethylterephthalic acid, about 16% by weight of propane-1,2-diol, about 10% by weight of ethylene glycol, about 13% by weight of methylsulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3,000. The polyesters and their method of preparation are described in detail in EPA 311 342. It is well known in the art that free chlorine in the tap water rapidly deactivates the enzymes comprised in the detergent compositions. Therefore, using a chlorine scrubber such as perborate, ammonium sulfate, sodium sulfite or polyethyleneimine at a level above 0.1% by weight of the composition. total, in the formulas will provide improved stability through the washing of detergent enzymes. Compositions comprising a chlorine scavenger are described in European Patent Application No. 29870018.6, filed on January 31, 1992. Alkoxylated polycarboxylates such as those prepared from polyacrylates are useful herein to provide additional removal performance of fat. Such materials are described in WO 91/08281 and PCT 90/01815 in p. 4 et seq, incorporated herein by way of reference. Chemically, these materials comprise polyacrylates having an ethoxy side chain for every 7-8 acrylate units. The side chains have the formula (CH2CH20) m (CH2) nCH3 where m is 2-3 and n is 6-12. The side chains are linked by ester to -, the "base structure" of the polyacrylate to provide a "comb" type polymer structure. The molecular weight may vary, but is typically in the range of about 2000 to about 50,000. Said alkoxylated polycarboxylates may comprise from about 0.05% to about 10% by weight of the compositions herein.

Dispersants The laundry detergent compositions of the present invention may also contain dispersants. Suitable organic water-soluble salts are homo- or copolymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. Polymers of that type are described in GB-A-1, 596,756. Examples of such salts are polysaccharides of MW 2000-5000 and their copolymers with maleic anhydride, said copolymers have a molecular weight of from 1,000 to 100,000. Especially, the acrylate-methacrylate copolymer such as 480N having a molecular weight of 4000, at a level of 0.5-20% by weight in the composition, can be added in the laundry detergent compositions of the present invention. The compositions of the invention may contain a lime soap peptizer compound, which preferably has a lime soap dispersion potency (LSDP), as defined below.

^ X sÉÍ ^ &X £? in the present, of not more than 8, preferably not more than 7, most preferably not more than 6. The lime soap peptizer compound is preferably present at a level of 0% to 20% by weight. A numerical measurement of the effectiveness of a lime soap peptizer is given by the lime soap dispersion power (LSDP), which is determined using the lime soap dispersant test as described in an article by H.C. Borghetty and C.A. Bergman, J. Am. Oil. Chem. Soc, volume 27, p. 88-90, (1950). This lime soap dispersion test method is widely used by practitioners in this technique referred to, for example, in the following articles; W.N. Linfield, Surfactant science Series, Volume 7, p. 3, W.N. Linfield, Tenside surf. det., volume 27, pgs. 159-163, (1990); and M.K. Nagarajan, W.F. Masler, Cosmetics and Toiletries, volume 104, p. 71-73, (1989). The LSDP is the ratio of the percentage by weight of dispersing agent to sodium oleate required to disperse the lime soap deposits formed by 0.025 g of sodium oleate in 30 ml of water with an equivalent hardness of 333 ppm CaC3 (Ca : Mg = 3.2). Surfactants having an adequate lime soap peptising capacity will include certain amine oxides, betaines, sulfobetaines, alkyl ethoxy sulfates and ethoxylated alcohols. Exemplary surfactants having an LSDP of not more than 8 to be used in accordance with the present invention include dimethylamine oxide of C ^ QC ^ Q, C- | 2-C- | 8 alkylethylsulfates with an average degree of ethoxylation of 1-5, particularly in C-2-C-5 alkylcytoisulfate surfactant with an ethoxylation degree of about 3 (LSDP = 4) and ethoxylated alcohols of C 14 -C 15 with an average degree of ethoxylation of 12 (LSDP = 6) or 30, sold under the trade names Lutensol A012 and Litensol A030 respectively, by BASF GmbH. Polymeric lime soap peptizers suitable for use herein are described in an article by M.K. Nagarajan, W.F. Masler, which is in Cosmetics and Toiletries, volume 104, pgs. 71-73, (1989). Lime soap peptizers such as 4- [N-octanoyl-6-aminohexanoyljbenzenesulfonate, 4- [N-nonanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-decanoyl-6-] can also be used as lime soap peptiser compounds. aminohexanoyl] benzenesulfonate and mixtures thereof; and nonanoyloxybenzenesulfonate together with hydrophobic / hydrophobic bleach formulations.

Inhibition of dye transfer The laundry detergent compositions of the present invention may also include compounds for inhibiting the transfer of dyes from one fabric to another, of solubilized and suspended dyes encountered during fabric washing operations including dyed fabrics. uz Dye transfer inhibiting polymeric agents Laundry detergent compositions according to the present invention also comprise from 0.001% to 10%, preferably 0.01% to 2%, most preferably from 0.05% to 1% by weight of inhibitory polymeric agents Such dye transfer inhibiting polymeric agents are normally incorporated into laundry detergent compositions to inhibit dye transfer from dyed fabrics onto fabrics washed therewith.These polymers have the ability to complex or adsorb dyes. fugitive dyes washed out of the dyed fabrics before the dyes have the opportunity to be fixed to other articles in the wash Polymeric agents inhibitors of dye transfer inhibitors are particularly polymers of polyamine N-oxides, copolymers of N-vinylpyrrolidone and N-vinylimidazole, po polymers of polyvinylpyrrolidone, polyvinyloxazolidones and polyvinylimidazoles and mixtures thereof. The addition of said polymers also increases the yield of the enzymes according to the invention. (a) Polyamine N-oxide polymers Polyamine N-oxide polymers suitable for use contain units having the following structural formula: P (I) x R where P is a polymerizable unit, to which the group R-N- Or it may be fixed or in which the group R-N-O forms part of the polymerizable unit, or a combination of both.

O O O II II II A is NC, CO, C, -0 -, "S -, - N-; xesOo 1 R are aliphatic, aliphatic, ethoxylated, aromatic, heterocyclic or alicyclic groups or any combination thereof to which the nitrogen of the N-O group may be attached or in which the nitrogen of the N-O group is part of these groups. The N-O group can be represented by the following general structures: O O I (R1) x-N- (R2) y = N- (R1) x I (R3) z wherein R1, R2, and R3 are aliphatic, aromatic, heterocyclic or alicyclic groups or combinations thereof, X and / oyo / yz is 0 or 1 and wherein the nitrogen of the NO group can be attached to, or wherein the NO group nitrogen is part of these groups. The N-O group can be part of the polymerizable unit (P) or It can be attached to the polymeric base structure or a combination of both. Suitable polyamine N-oxides in which the N-O group forms part of the polymerizable unit comprise the polyamine N-oxides in which R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups. A class of said polyamine N-oxides comprises the group of polyamine N-oxides in which the nitrogen of the group NO is part of the group R. The preferred N-oxides of polyamine are those in which R is a heterocyclic group such such as pyridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof. Another class of said polyamine N-oxides comprises the group of polyamine N-oxides in which the nitrogen of the NO group is attached to the R group. Other suitable N-oxides of polyamine are the polyamine oxides to which the NO group it is fixed to the polymerizable unit. Preferred classes of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) in which R are aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the functional group is NOT part of said group R Examples of these classes are the polyamine oxides in which 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 (!) Wherein R are heterocyclic or alicyclic aromatic groups in which the nitrogen of the functional group is NOT attached to said R groups. Examples of these The classes are the polyamine oxides in which the R groups can be aromatic, such as phenyl. Any polymer base structure can be used, so long as the amine oxide polymer formed is soluble in water and has dye transfer inhibiting properties. Examples of suitable polymeric base structures are polyvinyls, polyalkylenes, polyesters, polyethers, polyamines, polyamides, polyacrylates and mixtures thereof. The amine N-oxide polymers of the present invention typically have a ratio of amine to amine N-oxide from 10: 1 to 1: 1000000. However, the amount of amine oxide groups present in the polyamine oxide polymer can be varied by suitable copolymerization or by an appropriate degree of N-oxidation. Preferably, the ratio of amine to amine N-oxide is from 2: 3 to 1: 1000000, most preferably from 1: 4 to 1: 1000000, and more preferably from 1: 7 to 1: 1000000. The polymers of the present invention actually comprise random or block copolymers in which one type of monomer is an amine N-oxide and the other type of monomer is or is not an amine N-oxide. The amine oxide unit of the polyamine N-oxides has a Pka < 10, preferably Pka < 7, most preferably Pka < 6 Polyamine oxides can be obtained in almost any degree of polymerization. The degree of polymerization is not critical, as long as the material has the solubility in water and the suspension power of the desired dyes. Typically, the average molecular weight is within the range of 500 to 1,000,000; preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000 and still more preferably from 3,000 to 20,000. (b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole The polymers of N-vinyl limdazole and N-vinylpyrrolidone used in the present invention have an average molecular weight in the range of 5,000-1,000,000, preferably 5,000- 200,000. Highly preferred polymers for use in laundry detergent compositions in accordance with the present invention comprise a polymer selected from copolymers of N-vinylimidazole and N-vinylpyrrolidone wherein said polymer has an average molecular weight range of 5,000 to 50,000, very preferably from 8,000 to 30,000, more preferably from 10,000 to 20,000. The average molecular weight range was determined by light scattering as deciphered in Barth H.G. and Mays J.W. Chemical Analysis Vol 113, "Modern Methods of Polymer Characterization". The highly preferred N-vinylimidazole and N-vinylpyrrolidone copolymers have an average molecular weight range of 5,000 to 50,000; most preferably from 8,000 to 30,000; more preferably from 10,000 to 20,000. The copolymers of N-vinylimidazole and N-vinylpyrrolidone characterized in that they have said average molecular weight range provide excellent dye transfer inhibiting properties and do not adversely affect the cleaning performance of the detergent compositions formulated therewith. The copolymer of N-vinylimidazole and N-vinylpyrrolidone of the present invention has a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, most preferably from 0.8 to 0.3 and more preferably from 0.6 to 0.4. c) Polyvinylpyrrolidone The laundry detergent compositions of the present invention can also use polyvinylpyrrolidone ("PVP") having an average molecular weight from about 2500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000. and still more preferably from about 5,000 to about 15,000. Suitable polyvinyl pyrrolidones are commercially available from ISP Corporation, New York, NY and Montreal, Canada, under the product names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K-60 (average molecular weight of 160,000) and PVP K-90 (average molecular weight of 360,000). Other suitable polyvinyl pyrrolidones which are commercially available from BASF Corporation include Sokalan HP 165 and Sokalan HP 12; the polyvinylpyrrolidones known to those skilled in the detergent field (see, for example, EP-A-262,897 and EP-A-5 256,696). d) Polyvinyl oxazolidone: The laundry detergent compositions of the present invention can also use polyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Said polyvinyloxazolidones have an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, most preferably from about 5,000 to about 50,000 and still more preferably from about 5,000 to about 15,000. E) Polyvinylimidazole: The laundry detergent compositions of the present invention can also use polyvinylimidazole as a polymeric dye transfer inhibiting agent. Said polyvinylimidazoles have an average molecular weight of from 2,500 to about 400,000, preferably from about 5,000 to about 200,000, most preferably from about 5,000 to about 50,000 and more preferably from about 5,000 to about 15,000. . ^^^^ .. j ^^ tí l ütfrr - ff ía ÉT "- ^ tfcffiff ^ f) Interlaced polymers: Interlaced polymers are polymers whose base structures are interconnected to a certain degree, these bonds may be chemical or physical in nature. , possibly with active groups in the base structure or on the branches, the entangled polymers have been described in the Journal of Polymer Science, volume 22, pages 1035-1039 In one embodiment, the entangled polymers are made in such a way that they form a rigid three-dimensional structure that can catch «Dyes in the pores formed by the three-dimensional structure. In another embodiment, the entangled polymers trap the dyes by swelling. Said entangled polymers are described in co-pending patent application 94870213.9 Washing Method The compositions of the invention can be used essentially in any washing or cleaning method, including soaking methods, pretreatment methods and methods with rinsing steps for which a separate rinse aid composition can be added. The process described herein comprises making contact between the fabrics and a washing solution in the usual manner and exemplified hereinafter. The process of the invention is conveniently carried out in the course of the cleaning process. The cleaning method was preferably carried out between 5 ° C and 95 ° C, especially between 10 ° C and 60 ° C. The pH of the treatment solution is preferably from 7 to 12. The following examples are designed to exemplify compositions of the present invention, but are not necessarily designed to limit or otherwise define the scope of the invention. In laundry detergent compositions, the levels of the enzymes are expressed as pure enzyme by weight of the total composition, and unless otherwise specified, the detergent ingredients are expressed by weight of the total compositions. The identifications of the abbreviated components have the following meanings: LAS: Linear sodium alkylbenzene sulfonate of Cn.13 TAS: Sebum sodium alkylsulfate CxyAS: Sodium alkylsulfate of C? XC- | and CxySAS: (2,3) Sodium alkylsulfate secondary of C- | xC- | and CxyEz: A primary alcohol of C- | xC- | and predominantly linear condensed with an average of z moles of ethylene oxide CxyEzS: Sodium alkylsulfate of C- | xC- | and condensed with an average of z moles of oxide of ethylene. QAS: R2.N + (CH3) 2 (C2H4OH) with R2 = C12-C14 QAS 1: R2.N + (CH3) 2 (C2H4OH) with R2 = C8-Cn APA: C8- Amidopropyl dimethylamine or Soap: Sodium alkylcarboxylate linear derivative of an 80/20 mixture of 1S2 coconut and tallow fatty acids Nonionic: Mixed ethoxylated / propoxylated fatty alcohol of C13-C-15 with an average degree of ethoxylation of 3.8 and a degree of propoxylation of 4.5. Neodol 45-13 Primary C14-C15 primary ethoxylate alcohol, sold by Shell Chemical Co. STS: Sodium toluene sulphonate CFAA: N- methyl glucamide of C- | 2-C < | 4 TFAA: N-methyl alkyl glucamide of CJ Q-C Q TPKFA. Whole cut fatty acids of C? 2-C- | 4 Silicate: Amorphous sodium silicate (ratio Si02: Na20 = 1.6-3.2) Metasilicate Sodium metasilicate (ratio Si02: Na20 = 1.0) Zeolite A: Sodium aluminosilicate hydrated from the formula Na- | 2 (A102Si02)? 2 27H20, having a primary particle size in the range of 1 to 10 microns (weight expressed on an anhydrous basis) NaSKS-6: Crystalline layered silicate of the formula Ü-Na2Si? 5 Citrate: Trisodium citrate dihydrate of 86.4% activity with a particle size distribution of between 425 and 850 μm. Citrus: Anhydrous citric acid. Borate: Sodium borate. Carbonate: Anhydrous sodium carbonate with a particle size between 200 and 900 microns. Bicarbonate: Anhydrous sodium bicarbonate with a size distribution of * 53 particle between 400 and 1200 μm. Sulfate: Anhydrous sodium sulfate Mg sulfate: Anhydrous magnesium sulfate STPP: Sodium tripolyphosphate TSPP: Tetrasodium pyrophosphate MA / AA: Acrylate / maleate 4: 1 copolymer, average molecular weight of approximately 70,000-80,000 MA / AA 1: Copolymer Acrylate / Maleate 6: 4, average molecular weight of about 10,000 AA: Sodium polyacrylate polymer with an average molecular weight of 4,500 PA30: Polyacrylic acid of average molecular weight between about 4,500-8,000. 480N: Random copolymer of 7: 3 acrylate / methacrylate, average molecular weight of approximately 3,500. Poligel / carbopol: Interlaced polyacrylates of high molecular weight. PB1: Anhydrous sodium perborate with nominal formula NaB02.H 02 PB4: Tetrahydrated sodium perborate of nominal formula NaB02.3H2O.H20 2 Percarbonate: Anhydrous sodium percarbonate of nominal formula 2Na2C? 3.3H202 NaDCC: Sodium dichloroisocyanurate. f, áfr -.-- ^ jsfc_Mjfe¡atfc * A .. ÍU TAED: Tetraacetylethylenediamine NOBS: Nonanoyloxybenzenesulfonate in the form of the sodium salt NACA-OBS: (6-nonamidocaproyl) oxybenzenesulfonate DTPA: Diethylenetriaminepentaacetic acid HEDP: Acid 1, 1 -h id roxietandifosfón ico DETPMP: Diethylenetriaminpenta (metichephosphonate), marketed by Monsanto under the trade name Dequest 2060. EDDS: Ethylenediamine-N'-disuccinic acid, isomer [S, S] in the form of its sodium salt. MnTACN: 1, 4,7-trimethyl-1, 4,7-triazacyclononane-manganese Photoactivated bleach: Sulfonated zinc phthalocyanine encapsulated in dextrin-soluble polymer Photoactivated bleach 1: Sulfonated aluminum phthalocyanine encapsulated in dextrin-soluble polymer PAAC: Salt pentaminacetatocobalto (III). Paraffin: Paraffin oil sold under the trade name Winog 70 by Wintershall. NaBz: Sodium benzoate BzP: Benzoyl peroxide Mannanase: Mannase from Bacillus agaradherens, MCIMB 40482.

Protease: Proteolytic enzyme sold under the trade name Savinase, 7 Alcalase, Durazym by Novo Nordisk A / S, Maxacal, Maxapem sold by Gist-Brocades and proteases described in patents WO91 / 06637 and / or WO95 / 10591 and / or EP 251 446. Amylase: Amylolytic enzyme sold under the name commercial Purafact Ox AmR, described in WO 94/18314, sold by Genencor, Termamyl®, Fungamyl® and Duramyl®, all available from Novo Nordisk AS and those described in W095 / 26397. Lipase: lipoitic enzyme sold under the trade name Lipolase Ultra by Novo Nordisk A / S and Lipomax by Gist-Brocades. Cellulase: Cellulite enzyme sold under the trade name Carezyme and / or Endolase by Novo Nordisk A / S CMC: Carboxymethylcellulose sodium PVP: Polyvinyl polymer, with an average molecular weight of 60,000 PVNO: N-oxide of polyvinylpyridine, with an average molecular weight of 50,000 PVPVI: Vinylimidazole copolymer and vinylpyrrolidone, with an average molecular weight of 20,000 1: 4,4'-bis (2-sulphotryl) biphenyl disodium brightener Disodium 2: 4,4'-bis (4 -anilino-6-morpholino-1, 3,5-triazn-2-yl) stilbene-2,2'-disulfonate disodium Silicone Anti-foam: Polydimethylsiloxane foam controller with siloxane-oxyalkylene copolymer as the dispersing agent with a ratio of said controller to said dispersing agent from 10: 1 to 100: 1 Foam suppressor: 12% silicone / silica, 18% stearyl alcohol, 70% starch in granulated form Opacifying: Monostyrene-latex mixture with water base, sold by BASF Aktiengesellschaft with the name Lytron 621. SRP 1: Anionically blocked polyesters at the ends SRP 2: Short block polymer of poly (1, 2propylene) diethoxylated terephthalate. QEA: bs ((C2H50) (C2H4? N) (CH3) -N + -C6H12-N + - (CH3) bis ((C2H5?) - (C2H4? N), where n = from 20 to 30 PEI: Polyethyleneimine with an average molecular weight of 1800 and an average degree of ethoxylation of 7 ethyleneoxy residues per nitrogen SCS: Sodium cumenesulfonate HMWPEO: High molecular weight polyethylene oxide PEGx: Polyethylene glycol with a molecular weight of x PEO: Polyethylene oxide with a molecular weight of 5,000.

EXAMPLE 1 The following high density laundry detergent compositions according to the present invention were prepared: I || III IV V VI LAS 8.0 8.0 8.0 2.0 6.0 6.0 TAS 0.5 0.5 1.0 0.1 C46 (S) AS 2.0 2.5 C25AS 7.0 4.5 5.5 C68AS 2.0 5.0 7.0 C25E5 3.4 10.0 4.6 4.6 1d8 C25E7 3.4 3.4 1.0 - - - C25E3S - - - 2.0 5.0 4.5 QAS - 0.8 - - - - QAS 1 - - - 0.8 0.5 1.0 Zeolite A 18.1 17.5 14.1 17.1 19.5 17.1 Cítrico - - - 2.5 - 2.5 Carbonate 13.0 13.0 27.0 10.0 10.0 13.0 Na-SKS-6 - - - 10.0 - 10.0 Silicate 1.4 1.4 3.0 0.3 0.5 0.3 Citrate - 1.0 - 3.0 - - Sulfate 26.1 26.1 26.1 6.0 - - Mg Sulfate 0.3 - - 0.2 - 0.2 MA / AA 0.3 0.3 0.3 4.0 1.0 1.0 CMC 0.2 0.2 0.2 0.2 0.4 0.4 PB4 9.0 9.0 5.0 - - - Percarbonate - - - - 18.0 18.0 TAED 1.5 0.4 1.5 - 3.9 4.2 NACA-OBS - 2.0 1.0 - - - DETPMP 0.25 0.25 0.25 0.25 - - SRP 1 - - - 0.2 - 0.2 EDDS 0.25 0.4 _ 0.5 0.5 CFAA 1.0 2.0 HEDP 0.3 0.3 0.3 0.3 0.4 0.4 QEA 0.2 0.5 Mananase 0.001 0 02 0.001 0.02 0.0015 0.001 Protease 0.009 0.009 0.01 0.04 0.05 0.03 Amylase 0.002 0.002 0.002 0.006 0.008 0.008 Cellulase 0.0007 0.0007 0.0007 0.0007 Lipase 0.006 0.01 0.01 0.01 Bleach 15 15 15 20 20 10 photoactivated (ppm) PEl 0.2 0.5 0.2 1.0 0.5 1.0 PVNO / PVPVI - - - 0.1 - - Polisher 1 0.09 0.09 0.09 - 0.09 0.09 Perfume 0.3 0.3 0.3 0.4 0.4 0.4 15 Antifoam of 0.5 0.5 0.5 _ 0.3 0.3 silicone Density in g / l 850 850 850 850 850 850 850 Various ingredients 20 and minor components Up to 100% ^^ fe ^ j EXAMPLE 2 The following laundry detergent compositions of particular utility were prepared under washing conditions in a European washing machine, in accordance with the present invention: II lll IV VI LAS 5.5 7.5 5.0 5.0 6.0 7.0 TAS 1.25 1 1..99 - 0.8 0.4 0.3 C24AS / C25AS 2.2 5.0 5.0 5.0 2.2 C25E3S 0.8 1.0 1.5 3.0 1.0 C45E7 3.25 _ _ _ _ 3.0 TFAA 2.0 C25E5 5.5 QAS 0.8 QAS 1 0.7 1.0 0.5 1.0 0.7 STPP 19.7 Zeolite A 16.75 24.0 19.5 20.0 17.0 NaSKS-6 / citric acid 10.6 10.6 (79:21) Na-SKS-6 9.0 10.0 10.0 Carbonate 6.1 21.4 9.0 10.0 10.0 18.0 Bicarbonate 2.0 7.0 5.0 2.0 Silicate 6.8 0.3 0.5 Citrate 4.0 4.0 Sulfate 36.8 5.0 12.0 Mg Sulfate 0.1 0.2 0.2 MA / AA 0.5 1.6 3.0 3.5 1.0 1.0 CMC 0.2 0.4 1.0 1.0 0.4 0.4 PB4 5.0 12.7 Percarbonate 18.0 15.0 TAED 0.5 3.1 5.0 NACA-OBS 1.0 3.5 2.5 DETPMP 0.25 0.2 0.3 0.4 0.2 HEDP 0.3 0.3 0.3 0.3 QEA 1.0 1.0 1.0 Mananase 0.001 0.02 0.001 0.015 0.02 0.001 Protease 0.009 0.03 0.03 0.05 0.05 0.02 Lipasa 0.003 0.003 0.006 0.006 0.006 0.004 Cellulase 0.0006 0.0006 0.0005 0.0005 0.0007 0.0007 Amylase 0.002 0.002 0.006 0.006 0.01 0.003 PEl 3.0 1.75 1.0 0.5 0.25 0.25 PVNO / PVPVI 0.2 0.2 PVP 0.9 1.3 0.9 SRP 1 0.2 0.2 0.2 Bleach 15 27 20 20 photoactivated (ppm) Brightener 15 photoactivated 1 (ppm) Brightener 1 0.08 0.2 0.09 0.15 Brightener 2 0.04 Perfume 0.3 0.5 0.4 0.3 0.4 0.3 Antifoam 0.5 0.5 0.3 0.5 0.3 2.0 silicon Density in g / liter 750 750 750 750 750 750 Various ingredients and minor components Up to 100% EXAMPLE 3 The following detergent compositions of particular utility were prepared under washing conditions in a European washing machine, in accordance with the present invention: faith * -. * "lll IV Blown powder LAS 6.0 5.0 11.0 6.0 TAS 2.0 - - 2.0 Zeolite A 23.5 - - 19.5 STPP - 26.0 21.0 - Sulfate 4.0 6.0 13.0 - MA / AA 1.0 4.0 6.0 2.0 Silicate 1.0 7.0 3.0 3.0 CMC 1.0 1.0 0.5 0.6 Rinse aid 1 0.2 0.2 0.2 0.2 Silicone antifoam 1.0 1.0 1.0 0.3 DETPMP 0.4 0.4 0.2 0.4 Sprays Polisher 0.02 - - 0.02 C45E7 - - - 5.0 C45E2 2.5 2.5 2.0 - C45E3 2.6 2.5 2.0 - Perfume 0.5 0.3 0.5 0.2 Silicone antifoam 0.3 0.3 0.3 - Dry additives QEA 1.0 EDDS 0.3 - - - Sulfate 2.0 3.0 5.0 10.0 Carbonate 6.0 13.0 15.0 14.0 Citrus 2.5 - - 2.0 QAS 1 0.5 - - 0.5 Na-SKS-6 10.0 - - - PEl 0.5 1.0 3.0 0.5 Percarbonate 18.5 - - - PB4 - 18.0 10.0 21.5 TAED 2.0 2.0 - 2.0 NACA-OBS 3.0 2.0 4.0 - Mananase 0.001 0.02 0.01 0.0015 Protease 0.03 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 0.004 0.004 0.004 0.003 0.003 0.003 0.003 0.006 Polisher 1 0.05 - - 0.05 Various ingredients and minor components Up to 100% The following granular detergent compositions were prepared in accordance with the present invention: I lll IV VI Blown powder LAS 23.0 8.0 7.0 9.0 7.0 7.0 TAS - - - - 1.0 - C45AS 6.0 6.0 5.0 8.0 - - C45AES - 1.0 1.0 1.0 - - C45E35 - - - - 2.0 4.0 Zeolite A 10.0 18.0 14.0 10.25 10.0 10.0 MA / AA - 0.5 - - - 2.0 MA / AA 1 7.0 - - - - - AA - 3.0 3.0 2.0 3.0 3.0 Sulfate 5.0 6.3 12.3 11.0 13.0 18.3 Silicato 10.0 1.0 1.0 1.0 1.0 1.0 Carbonate 14.5 19.0 10.0 20.7 8.0 6.0 PEG 4000 0.4 1.5 1.5 1.0 1.0 1.0 DTPA - 0.9 0.5 - - 0.5 Rinse aid 2 0.3 0.2 0.3 - 0.1 0.3 Sprinklers C45E7 - 2.0 - - 2.0 2.0 C25E9 3.0 - - - - - C23E9 _ _ 1.5 2.0 _ 2.0 Perfume 0.3 0.3 0.3 2.0 0.3 0.3 Agglomerates C45AS 5.0 5.0 2.0 5.0 LAS 2.0 2.0 - 2.0 Zeolite A 7.5 7.5 8.0 7.5 Carbonate 4.0 4.0 5.0 4.0 PEG 4000 0.5 0.5 - 0.5 Ingredients 2.0 2.0 2.0 2.0 various (water, etc.) Dry additives QAS 1.0 Citrus 2.0 PB4 12.0 1.0 * PB1 4.0 1.0 3.0 2.0 Percarbonate 2.0 10.0 Carbonate 5.3 1.8 4.0 4.0 NOBS 4.0 6.0 - 0.6 Methylcellulose 0.2 Na-SKS-6 8.0 STS 2.0 1.0 Cumen acid - 1.0 - - - 2.0 sulfonic Mananase 0.001 0.02 0.001 0.015 0.02 0.02 Protease 0.02 0.02 0.02 0.01 0.02 0.02 Lipasa 0.004 - 0.004 - 0.004 0.008 Amylase 0.003 - 0.002 _ 0.003 _ Cellulase 0.0005 0.0005 0.0005 0.0007 0.0005 0.0005 PVPVI - - - - 0.5 0.1 PVP - - - - 0.5 PVNO - - 0.5 0.3 - PEl 0.5 1.0 2.0 1.75 2.0 1.0 QEA - - - - 1.0 SRP 1 0.2 0.5 0.3 - 0.2 Antifoam of 0.2 0.4 0.2 0.4 0.1 silicon Mg sulphate - - 0.2 - 0.2 Various ingredients and minor components Up to 100% In accordance with the invention, the following detergent compositions containing no bleach of particular use were prepared in the laundry of color laundry. lll Blown Powder Zeolite A 14.5 Sulfate Sulfate - 5.0 3.0 3.0 DETPMP 0.4 0.5 CMC 0.4 0.4 MA / AA 4.0 4.0 Agglomerates C45AS - 11.0 LAS 6.0 5.0 TAS 3.0 2.0 PEl 0.5 1.0 3.0 Silicate 4.0 4.0 Zeolite A 10.0 15.0 13.0 CMC - 0.5 MA / AA - 2.0 Carbonate 9.0 7.0 7.0 Sprayable Perfume 0.3 0.3 0.5 C45E7 4.0 4.0 4.0 C25E3 2.0 2.0 2.0 Dry additives MA / AA - - 1.0 Na-SKS-6 - - 11.0 Citrate 10.0 - 8.0 Bicarbonate 7.0 3.0 5.0 Carbonate 8.0 5.0 7.0 PVPVI / PVNO 0.5 0.5 0.5 Mananase 0.001 0.02 0.015 Protease 0.03 0.02 0.05 Lipase 0.008 0.008 0.008 Amylase 0.01 0.01 0.01 Cellulase 0.001 0.001 0.001 Silicone antifoam 5.0 5.0 5.0 Sulphate - 9.0 - Density (g / liter) 700 700 700 Miscellaneous ingredients and minor components Up to 100% EXAMPLE 6 The following detergent compositions were prepared in accordance with the present invention: I || III IV Granule base Zeolite A 29.5 21.0 22.0 10.0. Sulfate 10.0 5.0 10.0 7.0 MA / AA 3.0 - - - AA - 1.6 2.0 - PEl 0.5 1.0 2.0 3.0 MA / AA 1 - 12.0 - 6.0 LAS 14.0 10.0 9.0 18.0 C45AS 8.0 7.0 9.0 7.0 C45AES - 1.0 1.0 - Silicate - 1.0 0.5 9.0 Soap - 2.0 - - Brightener 1 0.2 0.2 0.2 0.2 Carbonate 6.0 9.0 10.0 10.0 PEG 4000 - 1.0 1.5 - DTPA - 0.4 - - Sprays C25E9 5.0 C45E7 1.0 1.0 C23E9 1.0 2.5 Perfume 0.2 0.3 0.3 Dry additives Carbonate 5.0 10.0 18.0 8.0 PVPVI / PVNO 0.5 - 0.3 - Mananase 0.001 0.02 0.001 0.0015 Protease 0.03 0.03 0.03 0.02 Lipase 0.008 - - 0.008 Amylase 0.002 - - 0.002 Cellulase 0.0002 .0005 0.0005 0.0002 NOBS 4.0 - 4.5 PB1 1.0 5.0 1.5 6.0 Sulfate 4.0 5.0 _ 5.0 SRP 1 0.4 0.5 0.5 foam suppressor Various ingredients and minor components Up to 100% The following granular detergent compositions were prepared in accordance with the present invention: I II III Blown powder Zeolite A 20.0 15.0 STPP 20.0 Sulphate - - 5.0 10 Carbonate - - 5.0 TAS - - 1.0 LAS 6.0 6.0 6.0 C68AS 2.0 2.0 - Silicate 3.0 8.0 - 15 MA / AA 4.0 2.0 2.0 CMC 0.6 0.6 0.2 Brightener 1 0.2 0.2 0.1 DETPMP 0.4 0.4 0.1 STS - - 1.0 20 Sprays C45E7 5.0 5.0 4.0 Silicone antifoam 0.3 0.3 0.1 Ji Perfume 0.2 0.2 0.3 Dry additives QEA - - 1.0 Carbonate 14.0 9.0 10.0 PB1 1.5 2.0 - PB4 18.5 13.0 13.0 TAED 2.0 2.0 2.0 QAS - - 1.0 Photoactivated bleach 15 ppm 15 ppm 15 ppm Na-SKS-6 - - 3.0 Mananase 0.001 0.02 0.01 Protease 0.03 0.03 0.007 Lipase 0.004 0.004 0.004 0.004 0.004 0.006 0.006 0.006 0.003 Cellulase 0.0002 0.0002 0.0005 PEl 1.0 3.0 0.5 Sulfate 9.0 17.0 4.5 j (q / liter) 700 700 700 Various ingredients and minor components Up to 100% ÍÍ4 EXAMPLE 8 The following detergent compositions were prepared in accordance with the present invention: I II III Blown powder Zeolite A 15.0 15.0 15.C Sulfate - 5.0 - 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 4.0 2.0 2.0 Agglomerate LAS 5.0 5.0 5.0 TAS 2.0 2.0 1.0 Silicate 3.0 3.0 4.0 Zeolite A 8.0 8.0 8.0 Carbonate 8.0 8.0 4.0 Sprayable Perfume 0.3 0.3 0.3 C45E7 2.0 2.0 2.0 C25E3 2.0 Dry Additives Citrate 5.0 2.0 Bicarbonate - 3.0 - Carbonate 8.0 14.0 8.0 PEl 0.5 1.0 2.0 TAED 6.0 2.0 5.0 PB1 13.5 7.0 10.0 PEO - - 0.2 Bentonite clay - - 10.0 Mananase 0.001 0.02 0.01 Protease 0.03 0.03 0.03 Lipase 0.008 0.008 0.008 Cellulase 0.001 0.001 0.001 Amylase 0.01 0.01 0.01 Silicone antifoam 5.0 5.0 5.0 Sulphate - 3.0 - Density (g / l) 850 850 850 Miscellaneous ingredients and minor components Up to 100% EXAMPLE 9 The following detergent compositions were prepared in accordance with the present invention: I lll IV LAS 18.0 14.0 24.0 20.0 QAS 0.7 1.0 0.7 TFAA 1.0 C23E56.5 1.0 C45E7 - 1.0 - - C45E3S 1.0 2.5 1.0 - STPP 32.0 18.0 30.0 22.0 Silicate 9.0 5.0 9.0 8.0 Carbonate 11.0 7.5 10.0 5.0 Bicarbonate - 7.5 - - PB1 3.0 1.0 - - PB4 - 1.0 - - NOBS 2.0 1.0 - - DETPMP - 1.0 - - DTPA 0.5 - 0.2 0.3 SRP 1 0.3 0.2 - 0.1 MA / AA 1.0 1.5 2.0 0.5 . ? í? si-i * CMC 0.8 0.4 0.4 0.2 PE 0.4 0.4 0.4 0.4 Sulfate 20.0 10.0 20.0 30.0 Mg Sulfate 0.2 0.4 0.9 Mananase 0.001 0.02 0.001 0.01 Protease 0.03 0.03 0.02 0.02 Amylase 0.008 0.007 _ 0.004 Lipase 0.004 0.002 Cellulase 0.0003 - - 0.0001 Photo-activated bleach 30 ppm 20 ppm - 10 ppm Perfume 0.3 0.3 0.1 0.2 Rinse aid 1/2 0.05 0.02 0.08 0.1 Various ingredients and minor components Up to 100% EXAMPLE 10 The following liquid detergent formulations were prepared in accordance with the present invention (the levels are given in parts by weight, the enzymes are expressed as pure enzyme).

II lll IV V LAS 11.5 8.8 - 3.9 - C25E2.5S 3.0 18.0 - 16.0 C45E2.25S 11.5 3.0 - 15.7 - C23E9 2.7 1.8 2.0 1.0 C23E7 3.2 CFAA - - 5.2 - 3.1 TPKFA 1.6 - 2.0 0.5 2.0 Citrus (50%) 6.5 1.2 2.5 4.4 2.5 Calcium formate 0.1 0.06 0.1 - - Sodium formate 0.5 0.06 0.1 0.05 0.05 SCS 4.0 1.0 3.0 1.2 - Borato 0.6 - 3.0 2.0 2.9 Sodium hydroxide 5.8 2.0 3.5 3.7 2.7 Ethanol 1.75 1.0 3.6 4.2 2.9 1, 2 Propanediol 3.3 2.0 8.0 7.9 5.3 Monoethanolamine 3.0 1.5 1.3 2.5 0.8 TEPAE 1.6 - 1.3 1.2 1.2 Mananase 0.001 0.02 0.001 0.01 0.02 * Protease 0.03 0.01 0.03 0.02 0.02 Lipase - _ 0.002 _ _ f? 9 Amylase 0.002 Cellulase 0.0002 0.0005 0.0001 SRP 1 0.2 0.1 DTPA - - 0.3 PEl 0.4 0.4 0.4 0.4 0.4 PVNO - - 0.3 0.2 Rinse aid 1 0.2 0.07 0.1 Silicone anti-foam 0.04 0.02 0.1 0.1 0.1 Various ingredients and water Up to 100% EXAMPLE 11 The following liquid detergent formulations were prepared in accordance with the present invention (the levels are given in parts by weight, the enzymes are expressed as pure enzyme). ^ g ^ j¿-g ^ 1 II lll IV LAS 10.0 13.0 9.0 - C25AS 4.0 1.0 2.0 10.0 C25E3S 1.0 - - 3.0 C25E7 6.0 8.0 13.0 2.5 TFAA _. . 4.5 APA 1.4 TPKFA 2.0 - 13.0 7.0 Citrus 2.0 3.0 1.0 1.5 Dodecenyl / tetradecenyl acid 12.0 10.0 _ _ succinic Fatty acid mustard seed 4 4..00 2.0 1.0 - Ethanol 4.0 4.0 7.0 2.0 1, 2 Propanodiol 4.0 4.0 2.0 7.0 Monoethanolamine - - - 5.0 Triethanolamine - - 8.0 - TEPAE 0.5 - 0.5 0.2 DETPMP 1.0 1.0 0.5 1.0 Mananase 0.001 0.02 0.001 0.02 Protease 0.02 0.02 0.01 0.008 Lipase _ 0.002 _ 0.002 Amylase 0.004 0.004 0.01 0.008 Celulasa - - - 0.002 SRP 2 0.3 - 0.3 0.1 Boric acid 0.1 0.2 1.0 2.0 Calcium chloride - 0.02 - 0.01 Rinse aid 1 - 0.4 - - PE 0.4 0.4 0.2 0.2 Foam suppressor 0.1 0.3 - 0.1 Opacifying 0.5 0.4 - 0.3 NaOH up to pH 8.0 8.0 7.6 7.7 Various ingredients and water Up to 100% EXAMPLE 12 The following liquid detergent compositions were prepared in accordance with the present invention (the levels are given in parts by weight, the enzymes are expressed as pure enzyme).

Iti IV LAS 25.0 C25AS 13.0 18.0 15.0 C25E3S 2.0 2.0 4.0 C25E7 - 4.0 4.0 TFAA 6.0 8.0 8.0 APA 3.0 1.0 2.0 - TPKFA 15.0 11.0 11.0 Citrus 1.0 1.0 1.0 1.0 Dodecenyl / tetradecenyl 15.0 succinic Acid 1.0 Seed fatty acid 3.5 mustard Ethanol 7.0 2.0 3.0 2.0 1, 2 Propanodiol 6.0 8.0 10.0 13.0 Monoethanolamine 9.0 9.0 TEPAE 0.4 0.3 DETPMP 2.0 1.2 1.0 Mananase 0.001 0.02 0.001 0.01 Protease 0.08 0.02 0.01 0.02 Lipase 0.003 0.003 Amylase 0.004 0.01 0.01 0.01 Cellulase 0.004 0.003 PEl 0.2 0. 2 0.4 0.4 SRP 2 - - 0.2 0.1 Boric acid 1.0 1.5 2.5 2.5 Bentonite clay 4.0 4.0 - - Brightener 1 0.1 0.2 0.3 - Foam suppressor 0.4 - - - Opacifying 0.8 0.7 - - NaOH up to pH 8.0 7.5 8.0 8.2 Various ingredients and water Up to 100% EXAMPLE 13 The following liquid detergent compositions were prepared in accordance with the present invention (the levels are given in parts by weight, the enzymes are expressed as pure enzyme).

I II LAS 27.6 18.9 C45AS 13.8 5.9 C13E8 3.0 3.1 Oleic acid 3.4 2.5 Citrus 5.4 5.4 Sodium hydroxide 0.4 3.6 Calcium formate 0.2 0.1 Sodium formate 0.5 Ethanol 7.0 - Monoethanolamine 16.5 8.0 1, 2 propanediol 5.9 5.5 Xylenesulfonic acid - 2.4 TEPAE 1.5 0.8 Protease 0.05 0.02 Mananase 0.001 0.02 PEl 0.2 0.4 PEG - 0.7 Rinse aid 2 0.4 0.1 Perfume 0.5 0.3 Water and minor components Up to 100% E "IE, EXAMPLE 14 The following granular detergent compositions were prepared which provide "softening during washing" capability, in accordance with the present invention: 1 II C45AS - 10.0 LAS 7.6 - C68AS 1.3 - C45E7 4.0 - C25E3 - 5.0 Chloride of coconut-alkyl-dimethyl hydroxy- 1.4 1.0 ethyl ammonium Citrate 5.0 3.0 Na-SKS-6 - 11.0 Zeolite A 15.0 15.0 MA / AA 4.0 4.0 DETPMP 0.4 0.4 PB1 15.0 - Percarbonate - 15.0 TAED 5.0 5.0 Clay smectite 10.0 10.0 HMWPEO - 0.1 Mananase 0.001 0.02 Protease 0.02 0.01 Lipase 0.02 0.01 Amylase 0.03 0.005 Cellulase 0.001 - Silicate 3.0 5.0 PEl 0.2 0.4 Carbonate 10.0 10.0 Foam suppressor 1.0 4.0 CMC 0.2 0.1 Various ingredients and minor components Up to 100% EXAMPLE 15 The following laundry bar detergent compositions were prepared according to the present invention (the levels are given in parts by weight, the enzymes are expressed as pure enzyme).

I II III VI V III VI V LAS - - 19.0 15.0 21.0 6.75 8.8 C28AS 30.0 13.5 - - - 15.75 11.2 22.5 Laurato of 2.5 9.0 -sodium Zeolite A 2.0 1.25 - - - 1.25 1.25 1.25 Carbonate 20.0 3.0 13.0 8.0 10.0 15.0 15.0 10.0 Carbonate of 27.5 39.0 35.0 - - 40.0 - 40.0 Calcium Sulfate 5.0 5.0 3.0 5.0 3.0 - - 5.0 TSPP 5.0 - - - - 5.0 2.5 STPP 5.0 15.0 10.0 - - 7.0 10.0 Clay - 10.0 - - 5.0-Bentonite DETPMP - 0.7 0.6 - 0.6 0.7 0.7 0.7 CMC - 1.0 1.0 1.0 1.0 - 1.0 Talcum - - 10.0 15.0 10.0 - Silicate - - 4.0 5.0 3.0 - PVNO 0.02 0.03 - 0.01 - 0.02 MA / AA 0.4 1.0 _ _ 0.2 0.4 0.5 0.4 SRP 1 0.3 0.3 0.3 0.3 0.3 0.3 0.3 0.3 ^^^ ¿^ bÉ ^^^ tf ^, ^,! ^ - 186 Mananase 0.001 0.01 0.001 0.01 0.01 0.001 0.01 0.001 Amylase 0.01 0.002 Protease 0.004 0.003 0.003 0.003 Lipase 0.002 - 0.002 Cellulase .0003 0003 .0002 - - PEl 0.2 0.2 0.2 0.2 D.3 0.2 0.2 0.3 Perfume 1.0 0.5 0.3 0.2 D.4 _ _ 0.4 Mg Sulfate - 3.0 3.0 3.0 Brightener 0.15 0.1 0.15 - 0.1 Bleach 15.0 15.0 15.0 15.0 15.0 photoactivated (PPm) EXAMPLE 6 The following additive detergent compositions were prepared in accordance with the present invention.

I II lll LAS 5.0 5.0 PEl 0.5 1.0 3.0 STPP 29.5 - 17.0 Zeolite A 34.0 20.0 PB1 20.0 15.0 - TAED 10.0 8.0 - Mananase 0.001 0.02 0.001 Protease 0.3 0.3 Amylase 0.06 0.06 Minor components, water and various ingredients Up to 100% LIST OF SEQUENCES (1) GENERAL INFORMATION: APPLICANT: NAME: The Procter & Gamble Company STREET: One Procter & Gamble Plaza CITY: Cincinnati, OHIO COUNTRY: USA POSTAL CODE: 45202 TITLE OF THE INVENTION: Detergent compositions containing a mannanase and a soil release polymer.

NUMBER OF SEQUENCES: 6 COMPUTER LEADABLE FORM: TYPE OF MEDIUM: Flexible disk COMPUTER: IBM compatible with PC OPERATING SYSTEM: PC-DOS / MS-DOS PROGRAM: Patentln Relay # 1.0 Version 1.25 (EPO) SEQ ID NO: 1 CHARACTERISTICS OF THE SEQUENCE LENGTH: 1407 base pairs TYPE: nucleic acid TYPE OF CHAIN: simple TOPOLOGY: linear TYPE OF MOLECULE: genomic DNA ORIGINAL SOURCE CHARACTERISTICS: NAME / KEY: CDS LOCATION: 1-1482 DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 1 ATGAAAAAAAAGTTATCACAGATTTATCATTTAATTATTTGCACACTTATAA TAAGTGTGGGAATAATGGGGATTACAACGTCCCCATCAGCAGCAAGTACA GGCTTTTATGTTGATGGCAATACGTTATATGACGCAAATGGGCAGCCATT TGTCATGAGAGGTATTAACCATGGACATGCTTGGTATAAAGACACCGCTT CAACAGCTATTCCTGCCATTGCAGAGCAAGGCGCCAACACGATTCGTATT GTTTTATCAGATGGCGGTCAATGGGAAAAAGACGACATTGACACCATTCG TGAAGTCATTGAGCTTGCGGAGCAÁÁATAAAATGGTGGCTGTCGTTGAAG TTCATGATGCCACGGGTCGCGATTCGCGCAGTGATTTAAATCGAGCCGTT GATTATTGGATAGAAATGAAAGATGCGCTTATCGGTAAAGAAGATACGGT TATTATTAACATTGCAAACGAGTGGTATGGGAGTTGGGATGGCTCAGCTT GGGCCGATGGCTATATTGATGTCATTCCGAAGCTTCGCGATGCCGGCTTA ACACACACCTTAATGGTTGATGCAGCAGGATGGGGGCAATATCCGCAATC TATTCATGATTACGGACAAGATGTGTTTAATGCAGATCCGTTAAAAAATAC GATGTTCTCCATCCATATGTATGAGTATGCTGGTGGTGATGCTAACACTG TTAGATCAAATATTGATAGAGTCATAGATCAAGACCTTGCTCTCGTAATAG GTGAATTCGGTCATAGACATACTGATGGTGATGTTGATGAAGATACAATC CTTAGTTATTCTGAAGAAACTGGCACAGGGTGGCTCGCTTGGTCTTGGAA AGGCAACAGTACCGAATGGGACTATTTAGACCTTTCAGAAGACTGGGCTG GTCAACATTTAACTGATTGGGGGAATAGAATTGTCCACGGGGCCGATGG CTTACAGGAAACCTCCAAACCATCCACCGTATTTACAGATGATAACGGTG GTCACCCTGAACCGCCAACTGCTACTACCTTGTATGACTTTGAAGGAAGC ACACAAGGGTGGCATGGAAGCAACGTGACCGGTGGCCCTTGGTCCGTAA CAGAATGGGGTGCTTCAGGTAACTACTCTTTAAAAGCCGATGTAAATTTAA CCTCAAATTCTTCACATGAACTGTATAGTGAACAAAGTCGTAATCTACACG GATACTCTCAGCTCAACGCAACCGTTCGCCATGCCAATTGGGGAAATCCC GGTAATGGCATGAATGCAAGACTTTAC GTGAAAACGGGCTCTGATTATAC ATGGCATAGCGGTCCTTTTACACGTATCAATAGCTCCAACTCAGGAACAA CGTTATCTTTTGATTTAAACAACATCGAAAATAGTCATCATGTTAGGGAAA TAGGCGTGCAATTTTCAGCGGCAGATAATAGCAGTGGTCAAACTGCTCTA TACGTTGATAACGTTACTTTAAGATAÓ SEQ ID NO: 2 CHARACTERISTICS OF THE SEQUENCE: LENGTH: 493 amino acids TYPE: amino acid TOPOLOGY: linear TYPE OF MOLECULE: protein DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 2 MKKKLSQIYHLIICTLIISVGIMGITTSPSAASTGFYVDGNTLYDANGQPFVMRG INHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAEQ NKMVAWEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYG SWDGSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFN ADPLKNTMFSIHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDV DEDTILSYSEETGTGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIV HGADGLQETSKPSTVFTDDNGGHPEPPTATTLYDFEGSTQGWHGSNVTGG PWSVTEWGASGNYSLKADVNLTSNSSHELYSEQSRNLHGYSQLNATVRHA NWGNPGNGMNARLYVKTGSDYTWHSGPFTRINSSNSGTTLSFDLNNIENSH HVREIGVQFSAADNSSGQTALYVDNVTLR SEQ ID NO: 3 CHARACTERISTICS OF THE SEQUENCE: LENGTH: 1407 base pairs TYPE: nucleic acid CHAIN TYPE: simple TOPOLOGY: linear TYPE OF MOLECULE: genomic DNA DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 3 ATGAAAAAAAAGTTATCACAGATTTATCATTTAATTATTTGCACACTTATAA TAAGTGTGGGAATAATGGGGATTACAACGTCCCCATCAGCAGCAAGTACA GGCTTTTATGTTGATGGCAATACGTTATATGACGCAAATGGGCAGCCATT TGTCATGAGAGGTATTAACCATGGACATGCTTGGTATAAAGACACCGCTT CAACAGCTATTCCTGCCATTGCAGAGCAAGGCGCCAACACGATTCGTATT GTTTTATCAGATGGCGGTCAATGGGAAAAAGACGACATTGACACCATTCG TGAAGTCATTGAGCTTGCGGAGCAAAATAAAATGGTGGCTGTCGTTGAAG TTCATGATGCCACGGGTCGCGATTCGCGCAGTGATTTAAATCGAGCCGTT GATTATTGGATAGAAATGAAAGATGCGCTTATCGGTAAAGAAGATACGGT TATTATTAACATTGCAAACGAGTGGTATGGGAGTTGGGATGGCTCAGCTT GGGCCGATGGCTATATTGATGTCATTCCGAAGCTTCGCGATGCCGGCTTA ACACACACCTTAATGGTTGATGCAGCAGGATGGGGGCAATATCCGCAATC TATTCATGATTACGGACAAGATGTGTTTAATGCAGATCCGTTAAAAAATAC GATGTTCTCCATCCATATGTATTAGTATGCTGGTGGTGATGCTAACACTG TTAGATCAAATATTGATAGAGTCATAGATCAAGACCTTGCTCTCGTAATAG GTGAATTCGGTCATAGACATACTGATGGTGATGTTGATGAAGATACAATC CTTAGTTATTCTGAAGAAACTGGCACAGGGTGGCTCGCTTGGTCTTGGAA AGGCAACAGTACCGAATGGGACTATTTAGACCTTTCAGAAGACTGGGCTG GTCAACATTTAACTGATTGGGGGAATAGAATTGTCCACGGGGCCGATGG CTTACAGGAAACCTCCAAACCATCCAC CGTATTTACAGATGATAACGGTG GTCACCCTGAACCGCCAACTGCTACTACCTTGTATGACTTTGAAGGAAGC ACACAAGGGTGGCATGGAAGCAACGTGACCGGTGGCCCTTGGTCCGTAA CAGAATGGGGTGCTTCAGGTAACTACTCTTTAAAAGCCGATGTAAATTTAA CCTCAAATTCTTCACATGAACTGTATAGTGAACAAAGTCGTAATCTACACG GATACTCTCAGCTCAACGCAACCGTTCGCCATGCCAATTGGGGAAATCCC GGTAATGGCATGAATGCAAGACTTTACGTGAAAACGGGCTCTGATTATAC ATGGCATAGCGGTCCTTTTACACGTATCAATAGCTCCAACTCAGGAACAA CGTTATCTTTTGATTTAAACAACATCGAAAATATCATCATGTTAGGGAAATA G SEQ ID NO: 4 CHARACTERISTICS OF THE SEQUENCE: LENGTH: 468 amino acids TYPE: amino acid TOPOLOGY: linear TYPE OF MOLECULE: protein DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 4 MKKKLSQIYHLIICTLIISVGIMGITTSPSAASTGFYVDGNTLYDANGQPFVMRG INHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAEQ NKMVAWEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYG SWDGSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFN ADPLKNTMFSIHMYEYAGGDANTVRSNiDRVIDQDLALVIGEFGHRHTDGDV DEDTILSYSEETGTGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIV HGADGLQETSKPSTVFTDDNGGHPEPPTATTLYDFEGSTQGWHGSNVTGG PWSVTEWGASGNYSLKADVNLTSNSSHELYSEQSRNLHGYSQLNATVRHA NWGNPGNGMNARLYVKTGSDYTWHSGPFTRINSSNSGTTLSFDLNNIENIIM LGK SEQ ID NO: 5 CHARACTERISTICS OF THE SEQUENCE: LENGTH: 1029 base pairs TYPE: nucleic acid J97 TYPE OF CHAIN: simple TOPOLOGY: linear TYPE OF MOLECULE: genomic DNA DESCRIPTION OF THE SEQUENCE: SEQ ID No: 5 5 'AAT TGG CGC ATA CTG TGT CGC CTG TGA ATC CTA ATG CCC AGC CAA CAA AAA CAG TGA TGA ACT GGC TTG CGC ACC TGC CGA ACC GAA CGG AAA ACA GAG TCC TTT CCG GAG CGT TCG GAG GTT ACA GCC ATG ACA CAT TTT CTA TGG CTG AGG CTG ATA GAA TCC GAA GCG CCA CCG GGC AAT CGC CTG CTA TTT ATG GCT GCG ATT ATG CCA GAG GAT GGC TTG AAA CAG CAA ATA TTG AAG ATT CAA TAG ATG TAA GCT GCA ACG GCG ATT TAA TGT CGT ATT GGA AAA ATG GCG GAA TTC CGC AAA TCA GTT TGC ACC TGG CGA ACC CTG CTT TTC AGT CAG GGC ATT TTA AAA CAC CGA TGA CA ATG ATC AGT ATA AAA ACA TAT TAG ATT CAG CAA CAG CGG AAG GGA AGC GGC TAA ATG CCA TGC TCA GCA AAA TTG CTG ACG GAC TTC AAG AGT TGG AGA ACC AAG GTG TGC CTG TTC TGT TCA GGC CGC TGC ATG AAA TGA ACG GCG AAT GGT TTT GGT GGG GAC TCA CAT CAT ATA ACC AAA AGG ATA ATG AAA GAA TCT CTC TAT ATA AAC AGC TCT ACA AGA AAA TCT ATC ATT ATA TGA CCG ACA CAA GAG GAC TTG ATC ATT TGA TTT GGG TTT ACT CTC CCG ACG CCA ACC GAG ATT TTA AAA CTG ATT TTT ACC CGG GCG CGT CTT ACG TGG ATA TTG TCG GAT TAG ATG CGT ATT TTC AAG TG CCT ACT CGA TCA ATG GAT ACG ATC AGC TAA CAG CGC TTA ATA AAC CAT TTG CTT TTA CAG AAG TCG GCC CGC AAA CAG CAG ACG GCT GCT TCG ATT ACA GCC TGT TCA TCA ATG CAA TAA AAC AAA AAT ATC CTA AAA CCA TTT ACT TTC TGG CAT GGA ATG ATG AAT GGA GCG CAG CAG TAA ACA AGG GTG CTT CAG CTT TAT ATG ATG ACA GCT GGA CAC TCA ACA AGG GAG AAA TAT GGA ATG GTG ATT CTT TAA CGC CAG TCG TTG AGT GAA TCC GGG ATC 3 ' SEQ ID NO: 6 CHARACTERISTICS OF THE SEQUENCE: LENGTH: 363 amino acids TYPE: amino acid TOPOLOGY: linear TYPE OF MOLECULE: protein DESCRIPTION OF THE SEQUENCE: SEQ ID NO: 6 ydhT 1 LFKKHTISLLIIFLLASAVLAKPIEAHTVSPVNPNAQQTTKTVMNWLAHL 50 ydhT 51 PNRTENRVLSGAFGGYSHDTFSMAEÁDRIRSATGQSPAIYGCDYARGWLE 100 ydhT 101 TANIEDSIDVSCNGDLMSYWKNGGIPQISLHLANPAFQSGHFKTPITNDQ 150 ydhT 151 YKNILDSATAEGKRLNAMLSKIADGLQELENQGVPVLFRPLHEMNGEWFW 200 ydhT 201 WGLTSYNQKDNERISLYKQLYKKIYHYMTDTRGLDHLIWVYSPDANRDFK 250 ydhT 251 TDFYPGASYVDIVGLDAYFQDAYSINGYDQLTALNKPFAFTEVGPQTANG 300 ydhT 301 SFDYSLFINAIKQKYPKTIYFLAWNDEWSAAVNKGASALYHDSWTLNKGE 350 ydhT 351 IWNGDSLTPIVE *. 363

Claims (11)

260 NOVELTY OF LVENVENTION CLAIMS

1. - A detergent composition for laundry containing a mannanase and a cotton-releasing polymer.

2. A laundry detergent composition according to claim 1, further characterized in that said mannanase is present at a level from 0.0001% to 2%, preferably from 0.0005% to 0.5%, more preferred from 0.001% to 0.1% of pure enzyme by weight of the total composition.

3. A laundry detergent composition according to claims 1-2, further characterized in that the cotton-containing polyethylenimine polymer is contained at a level from 0.0001% to 20%, preferably from 0.001% to 15%, most preferred from 0.01 to 10%.

4. A laundry detergent composition according to claims 1-3, further characterized in that the polyethylenimine polymer releasing dirt in cotton is of the following formula: H I [H2N-R] n + 1 - [N-R] m- [N-R] n-NH2 having a modified polyamine formula V (n + < |) WmYnZ or a structure polyamine base corresponding to the formula: % * - ^ H | R [H2N-R] n-k + l- [N-R] m- [N-R] n- [N-R] k-NH2 having a modified polyamine formula V (n_k + i) WmY'kZ, where k is less than or equal to n, the base structure of the polyamine prior to the modification has a molecular weight approximately greater than 200 daltons, wherein i) the units V are terminal units having the formula: E X "E E- N- R - or E- N-R- or E- N- R- I I E E E ii) the units W are the base structure units that have the formula: O -N- R - or - N X- R '- or - N t-R- I E iii) Y units are branching units that have the formula: and iv) the Z units are terminal units that have the formula: 262 wherein the linking units R of the base structure are selected from the group consisting of C2-C alkylene < | , C4-C-2 alkenylene, C3-C- hydroxyalkylene | , C4-C-2 dihydroxyalkylene, dialkylarylene C8-C2, - (R10) XR1-, - (R10) XR5 (0R1) X-, (CH2CH (OR2) CH2O) z (R0) and R (OCH2CH (OR2) CH2) w-, -C (0) (R) rC (0) -, - CH2CH (OR2) CH2-, and mixtures thereof; where R ^ is alkylene of C2-Cß and mixtures thereof; R2 is hydrogen, - (Rl?) XB, and mixtures of the same; R ^ is C- | -C-alkyl < | 8. C7-C- arylalkyl | , substituted aryl of C7-C- | 2 alkyl, C6-C aryl < 2, and mixtures thereof; R4 is alkylene of C- | -C < | 2, C4-C- | 2 alkenylene, C8-C- | 2 arylalkylene, C-C- | Q arylene and mixtures thereof; R ^ is C- | -C? Alkylene, C3-C- | 2-dihydroxy-alkylene hydroxy alkylene of C4-C- | , dialkylarylene of C8-C- | 2, -C (O) -, - C (0) NHR6NHC (0) -, -R1 (OR1) -, -C (0) (R4) rC (0) -, -CH2CH (OH) CH2-, -CH- 2CH (OH) CH 20 (R 0) and R 1 CH 2 CH (OH) CH 2 -, and mixtures thereof, R 6 is C 2 -C 2 alkylene or C 1 -C 2 arylene; the E units are selected from the group consisting of hydrogen, C- | -C22 alkyl, C3-C22 alkenyl, C7-C22 arylalkyl, C2-C22 hydroxyalkyl, - (CH2) pC02M, - (CH2) qS03M, -CH (CH2C02M) C02M, - (CH2) pP03M, - (R10) xB, -C (0) R3, and mixtures thereof, with the proviso that when any unit E of a nitrogen is a hydrogen, said nitrogen is also not an N-oxide; B »Dfejft $$ * ß? is hydrogen, C < | -Cβ, - (CH) qS? 3M, - (CH2) pC02M, - (CH2) q (CHS03M) CH2S03M, - (CH2) q- (CHS02M) CH2S03M, - (CH2) pP03M, -PO3M, and mixtures thereof; M is hydrogen or a cation soluble in water in an amount sufficient to satisfy the charge balance; X is a water soluble anion; k and k 'have a value from 1 to approximately 15; m has the value of 4 to about 400; n has the value from 0 to about 200; p has the value of 1 to 6, q has the value of 0 to 6; r has the value of 0 or 1; w has the value 0 or 1; x has the value of 1 to 100; and has the value from 0 to 100; z has the value of 0 or 1.

5. A laundry detergent composition according to any of the preceding claims, further characterized in that the cotton-based polyethylenimine-based polymer is selected from the group consisting of polyethyleneimine 1800E7 and its derivatives of amine oxide, polyethyleneimine 1200E7 and its oxidized or quaternized derivatives, polyethyleneimine 600E20 and / or mixtures thereof .

6. A detergent composition for laundry according to any of the preceding claims, further characterized in that it contains a surfactant, preferably a non-ionic surfactant.

7. A laundry detergent composition according to claim 6, further characterized in that the nonionic surfactant is a non-ionic alkyl ethoxylated surfactant with a chain length of C8 to C20, preferably C12 to C16, and a grade of ^^ táá 264 ethoxylation from 2 to 9, preferably from 3 to 7.

8. A detergent composition for laundry according to claim 6, further characterized in that the nonionic surfactant is a surfactant based on alkylmethylglucamide with a chain length from C8 to C20, preferably from C12 to C18.

9. A detergent composition for laundry according to any of the preceding claims, further characterized in that it also contains a builder, preferably a builder selected from zeolite, sodium tripolyphosphate, layered silicate and / or mixtures thereof.

10. A laundry detergent composition according to any of the preceding claims, further characterized in that it contains a conventional soil release polymer, preferably a polyester with anionically blocked ends, diethylated polypropylene terephthalate and / or mixtures thereof.

11. A method for cleaning fabrics with a detergent composition for laundry according to any of the preceding claims.