DE29825084U1 - Detergent compositions include mannanase and percarbonate - Google Patents

Abstract

Detergent composition comprising a mannanase enzyme and percarbonate.

Description

Field of the Invention

The The present invention relates to detergent compositions comprising a mannanase and percarbonate.

Background of the Invention

perborate is in the field as a laundry or dishwashing additive well known what is available Oxygen over provides a hydrogen peroxide release mechanism. perborate is in laundry or dishwashing detergents due to its high performance and attractive cost in widely used.

It however, it has been recognized in the art that this occurs during the release of hydrogen peroxide by-product formed from perborate, d. H. meta borate derivatives, with sugar polymers like starch, complex and lead to cleaning disadvantages (EP-A-736 085). It is surprising it has been found that mannose polymers, like guar gum, also cross-link with perborate, which makes it more the food or cosmetic stains are made more difficult to be removed by detergents containing perborate. It is also surprisingly it has been found that the Borate crosslinking with guar gum increases the activity of the enzyme on such gum / borate complex substrates reduced.

Actually pose Food and cosmetic stains / soiling the majority from for represent and include relevant stains / soiling to the consumer frequently Food additives such as thickening / stabilizing agents. In the Indeed, hydrocolloids, gums and emulsifiers are commonly used food additives. The term "rubber" denotes one Group of industrially useful Polysaccharides (long chain polymer) or their derivatives, which in hot or cold water to form viscous solutions, dispersions or gels hydrate. Rubbers are classified as natural and modified. natural Gums or natural rubbers include algae extracts, plant extrudates, Gums from seeds or roots and through microbial fermentation received rubbers. Modified (semi-synthetic) rubbers include cellulose and starch derivatives and certain synthetic rubbers such as low methoxyl pectin, propylene glycol alginate and carboxymethyl and hydropropyl guar gums (gums in Encyclopedia Chemical Technology, 4th edition, volume 12, pp. 842-862, J. Baird, Kelco division by Merck); see also Carbohydrate Chemistry for Food Scientists (Eagan Press - 1997) by R.L. Whistler and J.N. BeMiller, Chapter 4, pp. 63–89, and Direct Food Additives in Fruit Processing by P. Laslo, Bioprinciples and Applications, Volume 1, Chapter II, pp. 313-325 (1996), Technomie Publishing. Some of these gums, such as guar gum (E412), carob (E410) are widely used alone or in combinations in many Food applications used (rubbers in ECT, 4th edition, volume 12, pp. 842-862, J. Baird, Kelco Division of Merck).

The guar gum used in these food and cosmetic stains becomes from the seed endosperm of the legume plant Cyamopsis tetragonoloba. The guar gum (also called guaran), which extracts from the dicotyledon seed is built up from a 1-4-β-D-mannopyranosyl unit backbone and will as a thickener in dressing and frozen products and in cosmetics used (H.-D. Belitz, Food Chemistry, p. 243, English version the second edition, Springer Verlag, 1987, ISBN 0-387-15043-9 (US)) & (Carbohydrate Chemistry for Food Scientists, R.L. Wilstler, Eagan Press, 1997. ISBN 0-913250-92-9) & (Industrial Gum, second edition, R.L. Whistler, p. 306, Academic Press, 1973, ISBN 0-12-74-6252-x). The locust bean gum (also known as carob bean gum or St. Jon's bread) is also used in the food industry and is made from the seed of an evergreen Plant extracted, which is grown in the Mediterranean area. The Carob gum differs from the structure of guar gum probably only in the smaller number of D-galactosyl side chains and has the same 1-4-β-D-mannopyranosyl backbone. In legume seeds is water soluble Galactomannan the main one Storage carbohydrate, in some cases comprising up to 20% of the total dry weight. In galactomannan is an α-galactose linked to the O-6 from mannose residues, and it can also to various Extent to the O-2 and the O-3 of the mannose residues may be acetylated.

In addition, the effect of percarbonate on bleachable stains is well known in the art. The active ingredient released by percarbonate, ie H ₂ O ₂ , is identical to the active ingredient released from perborate, but without the release of borate material. It has now surprisingly been found that the combined use of percarbonate and mannanase, especially at specific levels, synergistically removes problematic stains such as food and cosmetic stains. which include mannans, especially at low temperatures.

It it has also been found that the ternary system consisting of percarbonate / mannanase / protease, with specific mirrors an even better result with said Stains.

Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol. 56, No. 11, pp. 3505-3510 (1990), a dimer-form β-mannanase derived from Bacillus stearothermophilus with a MW of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J. Microbio. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a β-mannanase derived from Bacillus subtilisis with a MW of 38 kDa, an optimum activity at pH 5.0 / 55 ° C. and a pI of 4 ,8th. The JP 03047076 discloses a β-mannanase derived from Bacillus sp. with a MW of 37 +/- 3 kDa measured by gel filtration, an optimum pH of 8-10 and a pI of 5.3-5.4. The JP 63056289 describes the preparation of an alkaline thermostable β-mannanase, which β-1,4-D-mannopyranoside bonds of z. B. Mannans hydrolyzed and Manno: Oligo: Saccharide generated. The JP 63036774 relates to a Bacillus microorganism FERM P-8856, which produces β-mannanase and β-mannosidase at an alkaline pH. A purified mannanase from Bacillus amyloliquefaciens and a method of preparation therefor, useful in the bleaching of pulp and paper, is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase, such as a glucanase, xylanase or mannanase, active at extreme pH and temperature, and its preparation. WO 94/25576 describes an enzyme derived from Aspergillus aculeatus CBS 101.43, which exhibits mannanase activity which could be used for various purposes for which the degradation or modification of plant or algal cell wall material is desired. WO 93/24622 discloses a mannanase isolated from Trichoderma reesia for bleaching lignocellulose pulps.

Indeed is the synergistic combination of a mannanase and percarbonate for a superior Cleaning performance in a detergent composition, d. H. superior Stain removal, especially for cosmetic and food stains, which contain mannans, dirt cleaning and whiteness maintenance, never previously recognized.

Furthermore is the synergistic combination of a mannanase and percarbonate and protease for a higher quality Cleaning performance in a detergent composition, d. H. superior Stain removal, dirt cleaning and whiteness maintenance, never earlier been recognized.

Summary of the invention

The The present invention relates to detergent compositions comprising a mannanase and percarbonate. These compositions see a superior one Cleaning performance, d. H. higher Stain removal, especially for cosmetic and food stains, which contain mannane, dirt cleaning and maintenance of the whiteness in front.

Detailed description of the invention

On essential element of the detergent composition of the present Invention is a mannanase enzyme. The use of mannanase grants significant Stain removal benefits from stains, cosmetic and food stains, which contain hydrocolloid gums such as guar gum.

We have surprisingly found that the Combination of perborate and mannanase limited performance benefits provides. It is believed that this limited performance is based on the presence of the Metaborate, which is associated with the Stains containing hydrocolloid rubber can crosslink. In contrast it has been found that the use of percarbonate, d. H. a material that has available oxygen without formation of metaborate derivatives in combination with the mannanase the present invention an excellent synergistic cleaning provides.

Therefore, the present invention relates to the use of the mannanase enzyme in combination with percarbonate. This combination provides outstanding synergistic whitening and / or stain removal benefits for food and cosmetic stains that contain mannanase-sensitive hydrocolloid gums such as guar gum or locust bean gum. Without wishing to be bound by theory, it is believed that the percarbonate bleach does not complex with the gums present in the stains and therefore facilitates access of the enzyme and / or bleach to the stains. In addition, it is believed that this synergistic effect is due to a) the Use of percarbonate, which bleaches the chromophore of the rubber-containing stains without crosslinking, and b) the effect of mannanase on the hydrocolloid polymer with the formation of more soluble small residues and provision for a high removal of the hydrocolloid residues, which are known to have a high affinity for the cotton surface of the garments. Furthermore, the synergy is believed to be due to the absence of borate ions, which are known to act as cross-linking agents with hydrated guar gum (see Industrial Gum, second edition, RL Whistler, p. 317, Academic Press, 1973, ISBN 0-12-74-6252 -x).

The mannana enzyme

On essential element of the detergent compositions of the present Invention is a mannanase enzyme.

In The following three mannane-degrading agents of the present invention Enzymes covered: EC 3.2.1.25: β-mannosidase, EC 3.2.1.78: Endo-l, 4-β-mannosidase, hereinafter referred to as "mannanase" and EC 3.2.1.100: 1,4-β-mannobiosidase (IUPAC classification - Enzyme gymnastics, 1992, ISBN 0-12-227165-3, Academic Press).

Further preferably the detergent compositions of the present invention Invention of a β-1,4-mannosidase (EC 3.2.1.78), which is called Mannanase. The term "mannanase" or "galactomannanase" means a mannanase enzyme which according to the subject is defined by the fact that it officially bears the name Mannan-endo-1,4-beta-mannosidase and the has alternative names beta-mannanase and endo-1,4-mannanase and catalyzes the following reaction: statistical hydrolysis of 1,4-beta-D-mannosidic Bonds in mannans, galactomannans, glucomannans and galactoglucomannans.

In particular mannanases (EC 3.2.1.78) form a group of polysaccharases, which break down mannans and denote enzymes, which are capable of Cleavage of polyose chains, which contain mannose units, d. H. able to for cleaving glycosidic bonds in mannans, glucomannans, Are galactomannans and galactoglucomannans. Mannans are polysaccharides with a basic framework, built up from β-1,4 linked mannose; Glucomannans are polysaccharides with a backbone of more or less regular yourself alternating β-1,4 linked mannose and glucose; Galactomannans and galactoglucomannans are mannans and glucomannans with α-1,6 linked galactose side branches. This Connections can be acetylated.

The Degradation of galactomannans and galactoglucomannans is due to the full or partial removal of the galactose side branches facilitated. Furthermore, the breakdown of acetylated mannans, glucomannans, galactomannans and galactoglucomannans by complete or partial deacetylation facilitated. Acetyl groups can be removed by alkali or Mannan acetylesterases. The Oligomers derived from mannanases or from a combination of mannanases and α-galactosidase and / or Mannan acetylesterases can be released are broken down to free maltose by β-mannosidase and / or β-glucosidase release.

Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol. 56, No. 11, pp. 3505-3510 (1990) a dimer-form beta-mannanase derived from Bacillus stearothermophilus with a molecular weight of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from Bacillus subtilis with a molecular weight of 38 kDa, an optimum activity at pH 5.0 / 55 ° C. and a pI from 4.8. The JP 03047076 discloses a beta-mannanase derived from Bacillus sp. with a molecular weight of 37 +/- 3 kDa measured by gel filtration, an optimum pH of 6-10 and a pI of 5.3-5.4. JP-63056289 describes the preparation of an alkaline, thermostable beta-mannanase which contains beta-1.4-D-mannopyranoside bonds from e.g. B. Mannans hydrolyzed and generated manno-oligosaccharides. JP-63036774 relates to a Bacillus microorganism FERM P-8856, which produces beta-mannanase and beta-mannosidase at an alkaline pH. The JP 08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001. A purified Mannanase from Bacillus amyloliquefaciens, useful in the bleaching of pulp and paper, and a manufacturing method therefor is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase, such as a glucanase, xylanase or mannanase, active at extreme pH and temperature. WO 94/25576 discloses an Aspergillus aculeatus CBS 101.43 enzyme showing mannanase activity, which may be useful for the degradation or modification of plant or algal cell wall material. WO 93/24622 discloses one Mannanase isolated from Trichoderma reseei for bleaching lignocellulose pulps. A hemicellulase capable of breaking down mannan-containing hemicellulose is described in WO 91/18974, and a purified mannanase from Bacillus amyloliquefaciens is described in WO 97/11164.

in the In particular, this mannanase enzyme becomes an alkaline mannanase be most preferably one of one, as defined below bacterial source-derived mannanase. In particular, the laundry detergent composition of the present invention comprise an alkaline mannanase selected from the mannanase from the Bacillus agaradherens and / or Bacillus strain subtilisis strain 168, gene yght.

The Term "alkaline Mannanase enzyme "is intended to encapsulate an enzyme with an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of its maximum activity in one given pH in the range from 7 to 12, preferably 7.5 to 10.5.

At the most preferred is the detergent composition of the present invention which include alkaline mannanase from Bacillus agaradherens. The said mannanase is

• i) a polypeptide manufactured by Bacillus agaradherens, NCIMB 40482, or
• ii) a polypeptide comprising an amino acid sequence as shown in positions 32-343 from SEQ ID No .: 2, or
• iii) an analog of the polypeptide defined in i) or ii), which is at least 70% homologous to the polypeptide, or from the polypeptide by substitution, deletion or addition of one or more amino acids is derived or obtained immunologically with a polyclonal antibody against the polypeptide, in purified form.

The The present invention also includes an isolated polypeptide with mannanase activity, chosen from the group consisting of

• (a) Polynucleotide molecules encoding a polypeptide with mannanase activity and comprising a sequence of nucleotides as shown in SEQ-ID No .: 1 from nucleotide 97 to nucleotide 1029;
• (b) species homologues of (a);
• (c) polynucleotide molecules, which code for a polypeptide with mannanase activity, which is at least 70 % identical to the amino acid sequence SEQ ID NO: 2 of amino acid residue 32 to amino acid residue Is 343;
• (d) molecules, complementary to (a), (b) or (c); and
• (e) degenerate nucleotide sequences of (a), (b), (c) or (d).

The Plasmid pSJ1678 comprising the polynucleotide molecule (the DNA sequence), coding for a mannanase of the present invention is in a strain of Escherichia coli has been transformed by the inventors according to the Budapest Contract over international recognition of the deposit of microorganisms for the purpose of the patent procedure for the German Collection of Microorganisms und Zellkulturen GmbH, Mascheroder Weg 1b, D-38124 Braunschweig, Federal Republic of Germany, on May 18, 1998 under the deposit number DSM 12180 was deposited.

On second strongest preferred enzyme is the mannanase from Bacillus subtilisis strain 168, the mannanase:

• i) from the coding part of the DNA sequence, shown in SEQ ID NO: 5 or an analog of the sequence is encoded, and or
• ii) a polypeptide comprising an amino acid sequence as shown in SEQ ID No .: 6, or
• iii) an analog of the polypeptide defined in ii) which at least is 70% homologous to the polypeptide, or from the polypeptide by substitution, deletion or addition of one or more Amino acids derived or with a polyclonal antibody obtained against the polypeptide, is immunologically reactive in purified form.

The present invention also an isolated polypeptide with mannanase activity selected from the group consisting of

• (a) Polynucleotide molecules encoding a polypeptide with mannanase activity and comprising a sequence of nucleotides as shown in SEQ-ID No .: 5
• (b) species homologues of (a);
• (c) polynucleotide molecules, which for encode a polypeptide with mannanase activity which at least 70% identical to the amino acid sequence 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 this invention in further detail discussed the following terms are defined first:

The The term "ortholog" (or "species homolog") denotes a Polypeptide or protein obtained from a species that has homology to an analog polypeptide or protein from a different species having.

The The term "paralog" denotes a polypeptide or protein obtained from a given species, which has homology to another polypeptide or protein from this same species having.

The The term "expression vector" refers to a DNA molecule linearly or circular, which comprises a segment coding for a polypeptide of interest, in working order additional Segments which for ensure its transcription. Such additional segments can be promoter and terminator sequences lock in, and can optionally one or more origins of replication, one or more selectable markers, an enhancer and a polyadenylation signal or similar lock in. Expression vectors are generally derived from plasmid or viral DNA derived or can be elements included by both. The expression vector of the invention can be a be any expression vector, which in a convenient manner recombinant DNA approaches undergoes, and the selection of the vector is often made by depend on the host cell, into which the vector is inserted shall be. Thus the vector can be an autonomously replicating vector be d. H. a vector that exists as an extrachromosomal entity, their replication independently from chromosomal replication, e.g. B. a plasmid. alternative the vector can also be one which, when introduced into a host cell is integrated into the host cell genome and together replicated with the chromosome (s) into which it has been integrated becomes.

The Expression "recombinant expressed "or" to recombinant Way expressed ", that herein in connection with the expression of a polypeptide or protein is used according to the standard definition in Specialty defined. The recombinant expression of a Protein is generally generated using an expression vector, as described immediately above.

The Term "isolated" when applied to a polynucleotide molecule, means that Polynucleotide from its natural genetic milieu has been removed and thus free from others strange or unwanted coding sequences, and in a suitable form for use is present within genetic engineering protein production systems. such isolated molecules are those who are separated from their natural environment, and close cDNA and genomic clones. Isolated DNA molecules of the present Invention are free from other genes with which they are usually can be associated however, of course occurring 5'- and 3'-untranslated Include regions such as promoters and terminators. The Identification of associated regions is made by the average person skilled in the art be obvious (see for example Dynan and Tijan, Nature 316: 774-78, 1985).

The Term "an isolated Polynucleotide " alternatively as "a cloned polynucleotide ". When applied to a protein / polypeptide, the term "isolated" indicates that the protein in one of its natural Environment different state is encountered. In a preferred one The isolated protein is essentially free of form Proteins, especially other homologous proteins (i.e., "homologous contaminants" (see below)). It is preferred to use the protein in a form more than 40% pure, more preferably to provide more than 60% pure form.

Yet more preferably, it is preferred to have the protein in a highly purified To provide form, d. H. more than 80% pure, more preferably more than 95% pure, and even stronger preferably more than 99% pure, as determined by SDS-PAGE.

The Term "isolated Protein / polypeptide " alternatively "cleaned Protein / polypeptide " become.

The Term "homologous Impurities " any contamination (e.g. a different polypeptide than the polypeptide of the invention), which is derived from the homologous cell from which the polypeptide of the invention is originally obtained. The term "obtained from" as used herein in connection used with a specific microbial source means that this Polynucleotide and / or polypeptide from the specific source or from a cell. into which a gene from the source has been inserted is being manufactured.

The Term "operably linked" when referenced on DNA segments, means that the Segments are arranged so that they in interaction for their intended purposes work, e.g. B. the transcription initiated at the promoter and through the coding segment to the terminator progresses.

The The term "polynucleotide" denotes a single or double-stranded Polymer read from deoxyribonucleotide or ribonucleotide bases from the 5 'to the 3' end. polynucleotides conclude RNA and DNA, and can from natural Sources isolated, synthesized in vitro, or a combination of natural synthetic molecules getting produced.

The Term "Complements of polynucleotide molecules "denotes polynucleotide molecules with a complementary base sequence and a reverse orientation compared to a reference sequence. To the Example is the sequence 5'-ATGCACGGG-3 'complementary to 5'CCCGTGCAT-3'.

The Term "degenerate Nucleotide Sequence " a sequence of nucleotides that degenerate one or more Includes codons (compared to a reference polynucleotide molecule which encodes a polypeptide). Degenerate codons contain different ones Triplets of nucleotides but encode the same amino acid residue (i.e. GAU and GAC triplets each encode Asp).

The The term "promoter" denotes one Section of a gene containing DNA sequences necessary for binding of RNA polymerase and for ensure the initiation of the transcription. Promoter sequences frequently, but not always, in the 5 'non-coding Region of genes found.

The Expression "secretory Signal sequence "referred to a DNA sequence encoding a polypeptide (a "secretory peptide") which as a component of a larger polypeptide the larger polypeptide through a secretory path of a cell in which it synthesizes will steer. The bigger peptide is usually cleaved to pass the secretory peptide through to remove the secretion pathway.

Like a sequence of the invention is used to obtain other related sequences.

The Sequence information disclosed herein regarding a polynucleotide sequence encoding a mannanase of the invention can be used as a tool for Identification of other homologous mannanases can be used. To the For example, polymerase chain reaction (PCR) can be used to amplify sequences which other homologous mannanases encode from a variety of microbial sources, particularly from different Bacillus species.

Activity Assay test

On Polypeptide of the invention with mannanase activity can be according to mannanase activity in the art known standard test procedures are tested as by Application of a solution to be tested on 4mm diameter holes, punched out in agar plates containing 0.2% AZCL-galactomannan (carob), d. H. Substrate for the assay of Endo-1,4-beta-D-mannanase, available as Cat.No. I-AZGMA by the company Megazyme for US $ 110.00 per 3 grams (Megazyme website: http://www.megazyme.com/Purchase/index.html).

polynucleotides:

On isolated polynucleotide of the invention is delivered to similar sized regions of SEQ ID NO. 1, or a complementary one Sequence, hybridize under at least medium stringency conditions.

In particular, polynucleotides of the invention will hybridize to a denatured double-stranded DNA probe comprising either the complete sequence shown in positions 97-1029 of SEQ ID NO: 1 or any probe comprising a sub-sequence of SEQ ID NO .: 1 with a length of at least about 100 base pairs under at least medium stringency conditions, but preferably at high ones Stringency conditions, as described in detail below. Suitable experimental conditions for determining the hybridization at medium or high stringency between a nucleotide probe and a homologous DNA or RNA sequence include pre-soaking the filter with the DNA fragments or RNA which are to be hybridized in 5 × SSC (sodium chloride / sodium citrate , Sambrook et al., 1989) for 10 minutes, and prehybridizing the filter in a solution of 5 × SSC, 5 × Denhardt's solution (Sambrook et al., 1989), 0.5% SDS and 100 μg / ml denatured sonicated Salmon sperm DNA (Sambrook et al., 1989), followed by hybridization in the same solution containing a concentration of 10 ng / ml of a statistically primed (Feinberg, AP and Vogelstein, B. (1983) Anal. Biochem. 132: 6 -13), ³² P-dCTP-labeled (specific activity higher than 1 × 10 ⁹ cpm / μg) probe for 12 hours at 45 ° C. The filter is then run twice in 30 × SSC, 0.5% SDS, at least 60 ° C (medium stringency), even more preferably at least 65 ° C (medium / high stringency), even more preferably at least 70 ° C (high stringency), and more preferably at least 75 ° C (very high stringency).

Molecules to which the oligonucleotide probe is hybridized under these conditions using an x-ray film demonstrated.

How previously noted, close which isolate polynucleotides of the present invention DNA and RNA. Methods for isolating DNA and RNA are in the art well known. DNA and RNA coding for genes of interest can in gene banks or DNA libraries using those known in the art Procedures are cloned.

For polypeptides with mannanase activity Polynucleotides encoding the invention are then identified and isolated for example by hybridization or PCR. The present The invention also sees counterpart polypeptides and polynucleotides from different bacterial strains (Orthologist or paralogue). Mannanase polypeptides are of particular interest from gram positive alkalophilic strains, including species from Bacillus.

species homologs of a polypeptide with mannanase activity of the invention can be found at Use of the information and compositions provided by the present invention can be provided in combination with conventional Cloning techniques are cloned. For example, a DNA sequence of the present Invention can be cloned using chromosomal DNA, obtained from a cell type that expresses the protein. suitable Sources of DNA can by probing Northern blots with probes derived from those herein Disclosed sequences were designed. be identified. Then becomes a library of chromosomal DNA from a positive cell line manufactured. A DNA sequence of the invention encoding a polypeptide with mannanase activity, can then be isolated by a variety of methods, such as by probing with probes designed from the sequences in the present description and claims, or with one or more sentences of degenerate probes based on the sequences disclosed. A DNA sequence of the invention can also be performed using the polymerase chain reaction or PCR (Mullis, U.S. Patent 4,683,202), wherein primers designed from the sequences disclosed herein become. Within an additional The DNA library procedure can be used to generate host cells to transform or transfect, and the expression of the DNA of interest can be identified with a (monoclonal or polyclonal) antibody it can be demonstrated which was obtained against that from B. agaradherens, NCIMB 40482, cloned mannanase, expressed and purified as described in materials and methods and example 1, or through an activity test, which relates to a polypeptide with mannanase activity.

The Mannanase coding part of the DNA sequence cloned into the plasmid pSJ1678, present in Escherichia coli DSM 12180, and / or one Analog DNA sequence of the invention can be derived from a bacterial strain Species Bacillus agaradherens, preferably the strain NCIMB 40482, which produces the enzyme with mannan-degrading activity, or another or related organism, as described herein.

alternative the analog sequence can be obtained on the basis of the DNA sequence the plasmid present in Escherichia coli DSM 12180 (which is assumed to be identical to the attached SEQ-ID No .: 1 is), e.g. B. a sub-sequence thereof, and / or by introducing Nucleotide substitutions that do not result in a different amino acid sequence of the mannanase encoded by the DNA sequence, but which of the codon use of for the production of the enzyme corresponds to the intended host organism, or by introduction of nucleotide substitutions which lead to a different amino acid sequence (e.g., a variant of the mannan-degrading enzyme of the invention) to lead can, be constructed.

polypeptide:

The Sequence of the amino acids No. 32-343 from SEQ ID NO: 2 is a mature mannanase sequence.

The The present invention also provides mannanase polypeptides which essentially homologous to the polypeptide of SEQ ID NO: 2 and species homologs (Paralogue or orthologist) of it. The term "substantially homologous" is used herein around polypeptides with 70%, preferably at least 80%, more preferred at least 85% and even stronger preferably at least 90% sequence identity to the sequence shown in the amino acids No. 32-343 from SEQ ID No: 2, or to designate their orthologist or paralogue. Such polypeptides are preferably at least 95% identical and the strongest preferably 98% or more identical to the sequence shown in amino acids no. 32-343 from SEQ ID No: 2 or their orthologs or paralogues. The percentage sequence identity determined by conventional Methods using computer programs known in the art, such as GAP, included 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 disclosed in Needleman, S.B. and wish, C.D. (1970), Journal of Molecular Biology, 48, 443-453, which is incorporated herein in its entirety by reference. GAP comes with the following settings for polypeptide sequence comparison used: GAP- "Creation Penalty "of 3.0 and GAP "extension Penalty "of 0.1.

The sequence identity of polynucleotide molecules is made by similar Procedure using GAP with the following settings for DNA sequence comparison determined: GAP- "Creation Penalty "of 5.0 and GAP "Extension Penalty" of 0.3.

The enzyme preparation the invention is preferably from a microorganism from a bacterium, an archaebacterium or a fungus, in particular from a bacterium, such as a bacterium belonging to Bacillus, preferably an alkalophilic Bacillus strain, which are chosen can be from the group consisting of the species Bacillus agaradherens and highly related Bacillus species, derived from all species preferably at least 95%, more preferably at least 98 % homologous to Bacillus agaradherens based on aligned or stacked in parallel 16S rDNA sequences. Essentially homologous proteins and polypeptides are characterized by having one or more amino acid substitutions, -Deletions or - additions. These changes are preferably of a minor nature, i.e. H. conservative amino acid substitutions (see Table 2) and other substitutions that do the folding or activity not significantly affect the protein or polypeptide; small Deletions, typically from one to about 30 amino acids; and small amino or carboxy terminal extensions, such as an amino terminal Methionine residue, a small linker peptide of up to about 20-25 residues or a little extension, which facilitates cleaning (an affinity tag), such as a poly-histidine tract, Protein A (Nilsson et al., EMBO J. 4: 1075, 1985; Nilsson et al., Methods Enzymol. 198: 3, 1991; see generally Ford et al., Protein Expression and Purification 2: 95-107, 1991, which is herein by reference to it). DNAs used for affinity tags encoding are available from commercial manufacturers (e.g. B. Pharmacia Biotech, Piscataway, NJ; New England Biolabs, Beverly, MA). Even though the changes described above however, preferably of a minor nature, such changes also of a larger nature be like a fusion of larger polypeptides of up to 300 amino acids or more than both amino and carboxy terminal extensions on a mannanase polypeptide of the invention.

Table 1 Conservative amino acid substitutions

In addition to the 20 standard amino acids, non-standard amino acids (such as 4-hydroxyproline, 6-N-methyllysine, 2-aminoisobutyric acid, isovalin and a-methylserine) can be substituted for amino acid residues of a polypeptide according to the invention. A limited number of non-conservative amino acids, amino acids that are not encoded by the genetic code, and unnatural amino acids can be substituted for amino acid residues. "Unnatural amino acids" have been modified after protein synthesis and / or have a chemical structure in their side chain (s) which is different from that of the standard amino acids. Unnatural amino acids can be chemically synthesized, or are preferably commercially available, and include pipecolic acid, thiazolidine carboxylic acid, dehydroproline, 3- and 4-methylproline and 3,3-dimethylproline.

essential amino acids in the mannanase polypeptides of the present invention can be according to the art known practices are identified as more localized Mutagenesis or "Alanine Scanning" mutagenesis (Cunningham and Wells, Science 244: 1081-1085, 1989). In the latter technique, single alanine mutations at every residue in the molecule introduced, and the resulting mutant molecules are tested for biological activity (i.e. Mannanase activity) tested for amino acid residues identify which ones for the activity of the molecule are critical; 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 as determined by such techniques as nuclear magnetic resonance, crystallography, Electron diffraction or photoaffinity labeling, related Mutation of putative contact point amino acids; please refer for example, de Vos et al., Science 255: 306-312, 1992; Smith et al., J. Mol. Biol. 224: 899-904, 1992; Wlodaver et al., FEBS Lett. 309: 59-64, 1992. On the identities of essential amino acids can also be concluded from the analysis of homologies with polypeptides which are related to a polypeptide according to the invention.

It can Multiple amino acid substitutions made and using known methods for mutagenesis, Recombination and / or exchange followed by a relevant one Screening procedure, such as that disclosed by Reidhaar-Olson and Sauer (Science 241: 53-57, 1988), Bowie and Sauer (Proc. Natl. Acad. Sci. USA 86: 2152-2156, 1989), WO 95/17413 or WO 95/22625. In short, these authors reveal Method for randomizing two or more at a time Positions in a polypeptide or for recombination / exchange followed by various mutations (WO 95/17413, WO 95/22625) by selecting for a functional polypeptide and then sequencing of the mutagenized polypeptides for determining the spectrum of permissible Substitutions at any position. Other procedures that are used can be conclude Phage display (e.g. B. Lowman et al., Biochem. 30: 10832-10837, 1991; Ladner et al., U.S. Patent No. 5,223,409; Huse, WIP0 publication WO 92/06204) and region-directed mutagenesis (Derbyshire et al., Gene 46: 145, 1986; Ner et al., DNA 7: 127, 1988).

Mutagenesis / Vertauschungs method, as disclosed above with automatic high-throughput screening methods for detection of activity of cloned mutagenized polypeptides combined in host cells become. Mutagenized DNA molecules, which for can encode active polypeptides from the host cells and quickly sequenced using modern equipment become. These methods allow the meaning to be determined quickly individual amino acid residues in a polypeptide of interest and can be based on polypeptides of unknown Structure can be applied. Using the ones discussed above One of ordinary skill in the art can process a variety of polypeptides identify and / or manufacture which are essentially homologous to residues 32 to 343 of SEQ ID No: 2 and the mannanase activity of the wild-type protein maintained.

Protein production:

The Proteins and polypeptides of the present invention, including full-length proteins, Fragments thereof and fusion proteins can be genetically engineered Host cells according to conventional techniques getting produced. Suitable host cells are those cell types which is transformed or transfected with exogenous DNA and in culture cultured can be and close Bacteria, fungal cells and cultured higher eukaryotic cells. Bacterial cells, in particular cultivated cells from gram-positive organisms, are preferred. Gram positive cells from the genus Bacillus particularly preferred, such as from the group consisting of Bacillus subtilis, Bacillus lentus, Bacillus brevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillus thuringiensis, Bacillus licheniformis, and Bacillus agaradherens, especially Bacillus agaradherens.

Techniques for manipulating cloned DNA molecules and introducing exogenous DNA into a variety of host cells are disclosed by Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989; Ausubel et al. (Ed.), Current Protocols in Molecular Biology, John Wiley and Sons, Inc., NY, 1987; and "Bacillus subtilis and Other Gram-Positive Bacteria", Sonensheim et al., 1993, American Society for Microbiology, Washington DC, which are herein incorporated by reference Terms are involved. 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 terminator, within an expression vector. The vector will usually also contain one or more selectable markers and one or more origins of replication, although those skilled in the art will recognize that selectable markers can be provided on separate vectors within certain systems and replication of the exogenous DNA can be provided by integration into the host cell genome. The selection of promoters, terminators, selectable markers, vectors and other elements is a matter of routine design within the ordinary skill in the art. Many such elements are described in the literature and are available through commercial manufacturers.

Around to direct a polypeptide into the secretory pathway of a host cell is a secretory signal sequence (also known as a "leader" sequence, prepro sequence or pre-sequence) provided in the expression vector. The secretory signal sequence can be that of the polypeptide or can be from another secreted protein can be derived or synthesized de novo become. There are numerous suitable secretory signal sequences known in the art and reference is made to "Bacillus subtilis and Other Gram-Positive Bacteria ", Sonensheim et al., 1993, American Society for Microbiology, Washington D.C .; and Cutting, S.M. (Ed.) "Molecular Biological Methods for Bacillus ", John Wiley and Sons, 1990, for a further description of suitable secretory signal sequences, specifically for secretion in a Bacillus host cell. The secretory signal sequence is added to the DNA sequence in the correct read name. secretory Signal sequences are generally 5 'to the DNA sequence encoding the polypeptide of Interest, positioned though certain signal sequences elsewhere may be positioned in the DNA sequence of interest (see z. B. Welch et al., U.S. Patent No. 5,037,743; Holland et al., U.S. Patent No. 5,143,830).

transformed or transfected host cells are processed in accordance with conventional procedures a culture medium containing nutrients and other components which are for the growth of the chosen host cells are cultivated. A variety of suitable media, including defined media and complex media are known in the art and close generally a carbon source, a nitrogen source, essential Amino acids, Vitamins and minerals. Media can also use such components such as growth factors or serum as needed. The growth medium will generally make a selection on cells, which contain the exogenously added DNA, for example by Drug selection or deficiency in an essential nutrient, which is complemented by the selectable marker which carried on the expression vector or co-transfected into the host cell becomes.

Protein Isolation:

If the expressed recombinant polypeptide is secreted, that can Polypeptide can be purified from the growth medium. Preferably become the expression host cells before purification of the polypeptide removed from the medium (e.g. by centrifugation).

If the recombinant polypeptide was not expressed from the host cell is secreted, the host cell is preferably broken up and the polypeptide is released in an aqueous "extract" which is the first stage of such cleaning techniques. Preferably the expression host cells are removed from the medium before the cell breakdown collected (e.g. by centrifugation).

The Cell breakdown can be done by conventional means Techniques performed as if by lysozyme digestion or by pressing the cells under high pressure; see (Robert K. Scobes, Protein Purification, second edition, Springer-Verlag) for another Description of such cell disruption techniques.

If the expressed recombinant polypeptides (or chimeric polypeptides) be secreted or not, they can be applied using fractionation and / or conventional Cleaning procedures and media to be cleaned.

Ammonium sulfate precipitation and acid or chaotropic extraction can be used for the fractionation of samples. Exemplary purification steps can include hydroxyapatite, size exclusion, FPLC, and reverse phase high performance liquid chromatography. Suitable anion exchange media include derivatized dextrans, agarose, cellulose, polyacrylamide, special silicas and the like. PEI, DEAE, QAE and Q derivatives are preferred, with DEAE fast flow Sepharose (Pharmacia, Piscataway, NJ) being particularly preferred. Exemplary chromatographic media include those media a, derivatized with phenyl, butyl or ocytl 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, cellulose resins, agarose beads, cross-linked agarose beads, polystyrene beads, cross-linked polyacrylamide resins and the like, which are insoluble under the conditions in which they are to be used. These supports can be modified with reactive groups which allow proteins to be attached by amino groups, carboxyl groups, sulfhydryl groups, hydroxyl groups and / or carbohydrate residues. Examples of the coupling chemistry include cyanogen bromide activation, N-hydroxysuccinimide activation, epoxy activation, sulfhydryl activation, hydrazide activation and carboxyl and amino derivatives for carbodiimide coupling chemistry. These and other solid media are well known and are widely used in the art and are available from commercial manufacturers.

The Choosing a particular procedure is a matter of routine design and is determined in part by the properties of the selected carrier; see for example Affinity Chromatography: Principles & Methods, Pharmacia LKB Biotechnology, Uppsala, Sweden, 1988.

polypeptides of the invention or fragments thereof can also be obtained by chemical Synthesis can be made. Polypeptides of the invention can be monomers or multimers; glycosylated or non-glycosylated; pegylated or be non-pegylated; and can an initial Methionine amino acid residue lock in, or not.

Based on the sequence information disclosed herein, a full length DNA sequence, encoding a mannanase of the invention and comprising that in SEQ-ID No: 1 shown DNA sequence, at least the DNA sequence from position 97 up to position 1029.

The Cloning is performed using standard procedures known in the art carried out, like through

• - Produce a genomic library from a Bacillus strain, in particular the strain B. agaradherens, NCIMB 40482;
• - plating such a library on suitable substrate plates;
• - Identify a clone comprising a polynucleotide sequence of the invention by standard hybridization techniques using a probe, which is based on SEQ ID No. 1; or by
• - Identify a clone from the Bacillus agaradherens genomic library, NCIMB 40482, using an inverse PCR strategy Primers based on the sequence information from SEQ-ID No. 1. Reference is made to M.J. MCPherson et al. ("PCR A practical approach", Information Press Ltd., Oxford, England) for further details regarding inverse PCR.

On based on the sequence information disclosed herein (SEQ ID NO. 1, SEQ ID No. 2) it is for a matter of routine for the person skilled in the art, consequent polynucleotide sequences, coding for a homologous mannanase of the invention by a similar one Strategy using related genomic libraries microbial organisms, especially from genomic libraries from other tribes to the genus Bacillus, such as alkalophilic species from Bacillus isolate.

alternative the DNA coding for the mannan or galactomannan degrading enzyme of the invention, according to well known ones Appropriate procedures an appropriate source, such as any of the above mentioned Organisms, by using synthetic oligonucleotide probes, prepared on the basis of the DNA sequence, obtainable from the plasmid which is present in Escherichia coli DSM 12180.

consequently can the polynucleotide molecule of the invention can be isolated from Escherichia coli, DSM 12180, in which that obtained by cloning as described above Plasmid is deposited. The present invention further relates to an isolated essentially pure biological culture of the Escherichia strain coli, DSM 12180.

In the present context, the term "enzyme preparation" is intended to mean either a conventional enzymatic fermentation product, possibly isolated and purified, from a single species of a microorganism, such preparation usually comprising a number of different enzymatic activities; or a mixture of monocomponent enzymes, preferably enzymes derived from bacterial or fungal species using conventional recombinant techniques, the enzymes being fermented and possibly isolated and purified separately and where they can be derived from different species, preferably fungal or bacterial species; or the fermentation product of a microorganism which acts as a host cell for the expression of a recombinant mannanase, but the microorganism simultaneously produces other enzymes, e.g. B. pectin-degrading enzymes, proteases or cellulases, which are naturally occurring fermentation products of the microorganism, ie the enzyme complex, which is conventionally produced by the corresponding naturally occurring microorganism.

A method for producing the enzyme preparation of the invention is the method comprising culturing a microorganism, e.g. B. a wild-type strain capable of producing the mannanase under conditions which allow the production of the enzyme, and recovering the enzyme from the culture. Cultivation can be carried out using conventional fermentation techniques, e.g. B. Cultivate in shake flasks or fermenters under agitation to ensure adequate aeration on a growth medium which induces the production of the mannanase enzyme. The growth medium may contain a conventional N source, such as peptone, extract or casamino 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. The extraction can be carried out using conventional techniques, e.g. B. Separation of biomass and supernatant by centrifugation or filtration, recovery of the supernatant or disruption of cells if the enzyme of interest is intracellular, optionally followed by further purification as described in EP 0 406 314 , or crystallization as described in WO 97/15660.

Immunological cross reactivity:

Polyclonal antibodies to be used in the determination of immunological cross-reactivity can be produced using a purified mannanase enzyme. More specifically, an antiserum against the mannanase of the invention can be obtained 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 pp. 27-31). Preferred immunoglobulins can be obtained from the antisera, for example by salt precipitation ((NH ₄ ) ₂ SO ₄ ), followed by dialysis and ion exchange chromatography, e.g. B. on DEAE-Sephadex. The immunochemical characterization of proteins can either by Ouchterlony double diffusion analysis (O. Ouchterlony in: Handbook of Experimental Immunology (DM Weir, ed.), Blackwell Scientific Publications, 1967, pp. 655-706), by crossed immunoelectrophoresis (N. Axelsen et al., See above, chapters 3 and 4), or by Rocket immunoelectrophoresis (N. Axelsen et al., Chapter 2).

Examples of useful Bacteria producing 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, more preferably a strain of Bacillus agaradherens, especially the strain Bacillus agaradherens NCIMB 40482.

The present invention includes an isolated mannanase with the properties described above one that is free of homologous contaminants and using conventional recombinant techniques is produced.

Determination of the catalytic activity (ManU) by Mannanase

colorimetric Assay: Substrate: 0.2% AZCL galactomannan (Megazyme, Australia) from carob in 0.1 M glycine buffer, pH 10.0. The assay is in an Eppendorf microtube of 1.5 ml on a thermomixer with stirring and temperature control of 40 ° C carried out. Incubate 0.750 ml substrate with 0.05 ml enzyme 20 Minutes, and is centrifuged for 4 minutes 15,000 rpm stopped. The color of the supernatant is at 600 nm in a 1 cm cell measured. One ManU (Mannanase Units) gives 0.24 abs in 1 cm.

Obtained the Bacillus agaradherens mannanase NCIMB 40482

strains

Bacillus agaradherens NCIMB 40482 the for the DNA sequence encoding the mannanase enzyme.

E. coli strain: cells from E. coli SJ2 (Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, BR, Sjøholm, C. (1990) Cloning of aldB, which encodes alpha-acetolactate decarboxylase, an exoenzyme from Bacillus brevis. J. Bacteriol., 172, 4315-4321) were prepared for and transformed by electroporation. a Gene Pulser ^™ electroporator from BIO-RAD was used as described by the manufacturer.

B. subtilis PL2306. This strain is the B. subtilis DN1885, with an interrupted one apr and npr genes (Diderichsen, B., Wedsted, U., Hedegaard, L., Jensen, B.R., Sjøholm, C. (1990) Cloning of aldB, which encodes alpha-acetolactate decarboxylase, an exoenzyme from Bacillus brevis. J. Bacteriol., 172, 4315-4321) in the transcription unit of the well-known Bacillus subtilis cellulase gene, which leads to cellulase negative cells. The disruption was in the essentially performed as described in (ed .: A.L. Sonenshein, J.A. Hoch and Richard Losick (1993) Bacillus subtilis and other Gram-Positive Bacteria, American Society for Microbiology p. 618).

competent Cells were made 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 detailed described in WO 94/19454, which is incorporated herein by reference is).

pMOL944: This plasmid is a pUB 110 derivative that essentially contains elements which make the plasmid propagable in Bacillus subtilis, and contains a kanamycin resistance gene, and contains a strong promoter and a signal peptide from the amyL gene from B. licheniformis ATCC14580. The signal peptide contains a SacII site, which is used for cloning the DNA coding for the mature Part of a protein useful in fusion with the signal peptide. this leads to for expression of a pre-protein, which towards the outside space is directed towards the cell.

The Plasmid was made using conventional constructed genetic engineering procedures, which are in the following be briefly described.

construction from pMOL944:

The pUB110 plasmid (McKenzie, T., et al., 1986, plasmid 15: 93-103) digested with the unique restriction enzyme NciI. A PCR fragment, amplified from the amyL promoter, encoded on the plasmid pDN1981 (P.L. Jørgensen et al., 1990, Gene, 96, pp. 37-41), was digested with NciI and inserted in the NciI digested pUB 110, whereby the plasmid pSJ2624 was obtained.

The two PCR primers used have the following sequences:

The Primer # LWN5494 performs a NotI site in the plasmid.

The Plasmid pSJ2624 was then digested with SacI and NotI, and a new one PCR fragment, amplified by the amyL promoter, encoded on pDN1981, was digested with SacI and NotI, and this DNA fragment was inserted into the SacI-NotI digested pSJ2624, causing the plasmid pSJ2670 was obtained.

This Cloning replaces the first amyL promoter with cloning the same promoter, but in the opposite direction. The two for Primers used in PCR amplification have the following sequences:

The Plasmid pSJ2670 was digested with the restriction enzymes PstI and BclI, and a PCR fragment amplified from a cloned DNA sequence, coding for the alkaline amylase SP722 (disclosed in the international patent application, released as WO 95/26397, which is incorporated herein by reference in its entirety was digested and inserted with PstI and BclI, whereby the plasmid pMOL944 was obtained. The two for PCR amplification primers used have the following sequence:

The Primer # LWN7901 performs a SacII site in the plasmid.

Cloning of the mannanase gene from Bacillus agaradlierens

manufacturing of genomic DNA:

The Strain Bacillus agaradherens NCIMB 40482 was in liquid medium propagates as described in WO 94/01532. After 16 hours longer Incubation at 30 ° C at 300 and 300 rpm, the cells were harvested and the genomic DNA 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 guanidinium thiocyanate. Lett. Appl. Microbiol. 8, 151-156) has been described.

construction a genomic library:

genomic DNA was partially digested with the restriction enzyme Sau3A and by size electrophoresis on a 0.7% agarose gel separated. The fragments were between 2 and 7 kb in size isolated by electrophoresis on DEAE cellulose paper (Dretzen, G., Bellard, M., Sassone-Corsi, P., Chambon, P. (1981) A reliable method for the recovery of DNA fragments from agarose and acrylamide gels. Anal. Biochem., 112, 295-298). Isolated DNA fragments were ligated to BamHI-digested pSJ1678 plasmid DNA, 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 on LB agar plates containing 0.2% AZCL-galactomannan (Megazyme) and 9 µg / ml Chloramphenicol, screened and over Night at 37 ° C incubated. Clones expressing mannanase activity appeared with blue diffusion courtyards. Plasmid DNA one of these clones was made using Quiagen plasmid spin preparations from 1 ml overnight culture nutrient solution (cells were at 37 ° C in TY with 9 μg / ml Chtoramphenicol and when shaken incubated at 250 rpm) isolated.

This Clone (MB525) was also cloned by DNA sequencing Characterized Sau3A DNA fragment. DNA sequencing was done by using "primer walking" of the Taq deoxy terminal cycle sequencing kit (Perkin-Elmer, USA), fluorescently labeled terminators and matching oligonucleotides performed as a primer.

The Analysis of the sequence data was carried out according to Devereux et al. (1984) Nucleic Acids Res. 12, 387-395. The Sequence encoding the mannanase is shown in SEQ ID No. 1. The derived protein sequence is shown in SEQ ID No. 2.

Subcloning and expression from Mannanase in B. subtilis:

The for mannanase DNA sequence encoding the invention was PCR amplified at Use of the PCR primer set consisting of these two oligonucleotides:

The Restriction sites SacII and NotII are underlined.

Chromosomal DNA isolated from B. agaradherens NCIMB 40482 as described above was used as a template in a PCR reaction using Amplitaq DNA polymerase (Perkin Elmer) according to the manufacturer's instructions. The PCR reaction was carried out in PCR buffer (10 mM Tris-HCl, pH 8.3, 50 mM KCl, 1.5 mM MgCl ₂ , 0.01% (w / v) gelatin) containing 200 μM each dNTP, 2.5 units of AmpliTaq polymerase (Perkin-Elmer, Cetus, USA) and 100 pmol of each primer.

The PCR reaction was performed using a DNA thermal cycler (Landgraf, Germany). Incubation was at 94 ° C for 1 minute followed by thirty PCR cycles using a cycle profile of 30 seconds denaturation at 94 ° C, Annealing or attachment during 1 minute at 60 ° C and 2 minute extension at 72 ° C. Five microliter aliquots of the amplification product were 0.7% by electrophoresis Agarose gels (NuSieve, FMC) analyzed. The appearance of a DNA fragment size of 1.4 kb indicated the correct amplification of the gene segment.

Subcloning of the PCR fragment

Forty-five µl aliquots of the PCR products generated as described above were used the QIAquick PCR purification kit (Quiagen, USA) according to the instructions of the manufacturer cleaned. The purified DNA was dissolved in 50 μl 10 mM Tris-HCl, pH 8.5 eluted.

5 µg pMOL944 and twenty-five ul of the purified PCR fragments were digested with SacII and NotI in 0.8% agarose gels of low gelation temperature (SeaPlaque GTG, FMC) electrophoretically separated, the relevant fragments were cut out of the gels and using the QIAquick gel extraction kit (Quiagen, USA) according to the instructions of the manufacturer cleaned. The isolated PCR DNA fragment was then ligated to the SacII-NotI digested and purified pMOL944. The ligation was over Night at 16 ° C using 0.5 μg every DNA fragment, 1 U T4 DNA ligase and T4 ligase buffer (Boehringer Mannheim, Germany) carried out.

The Ligation mix was used to make competent B. subtilis PL2306 to transform. The transformed cells were placed on LBPG-10 ug / ml kanamycin plates plated. After 18 hours of incubation at 37 ° C were colonies seen on the plates. Several clones were isolated by isolating Plasmid DNA from overnight culture medium analyzed.

On such positive clone was repeated several times on agar plates, streaked as used above and this clone became MB594 called. The clone MB594 was over Night in TY-10 μg / ml Kanamycin at 37 ° C used, and closest Day 1 ml of cells was used to remove the plasmid from the cells using the Qiaprep Spin Plasmid Miniprep Kit # 27106 as recommended of the manufacturer for B. subtilis plasmid preparations isolate. This DNA was subjected to DNA sequencing and showed the DNA sequence corresponding to the mature part of the mannanase, d. H. Positions 94-1404 the attached SEQ ID No: 3. The derived mature protein is in SEQ ID No: 4 shown. It will be apparent that the 3 'end of the sequence shown by SEQ ID No: 1 encoded mannanase to one which is shown in SEQ ID No: 3 is shown due to the design of the lower one used in the PCR Primers changed has been. The resulting amino acid sequence is shown in SEQ ID NO: 4 and it is obvious that the C-terminus SEQ ID No: 2 (SHHVREIGVQFSAADNSSGQTALYVDNVTLR) to the C-terminus changed from SEQ ID No: 4 (IIMLGK) is.

Media:

• TY (as described in Ausubel, F.M. et al. (Ed.) "Current protocols in Molecular Biology ". John Wiley and Sons, 1995).
• LB agar (as described in Ausubel, F.M., et al. (Ed.) "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. BPX medium as described in EP 0 506 780 (WO 91/09129).

Expression, purification and characterization of mannanase from Bacillus agaradherens

Clone MB 594, obtained as described above under Materials and Methods, was grown for 5 days in 25 × 200 ml BPX medium with 10 μg / ml kanamycin in two 500 ml baffle plate shake flasks at 37 ° C. at 300 rpm , 6500 ml of the shake flask culture fluid from clone MB 594 (batch # 9813) was collected. and the pH was adjusted to 5.5. 146 ml cationic agent (C521) and 292 ml of anionic agent (A130) were added with stirring to flocculate. The flocculated material was separated by centrifugation for 20 minutes using a Sorval RC 3B centrifuge at 9000 rpm at 6 ° C. The supernatant was clarified using Whatman GF / D and C glass filters and finally concentrated on a 10 kDa Filtron. 750 ml of this concentrate was brought to pH 7.5 using sodium hydroxide. The clear solution was applied to anion exchange chromatography using a 900 ml Q-Sepharose column which had been equilibrated with 50 mmol Tris pH 7.5. Bound mannanase activity was eluted using a sodium chloride gradient.

The pure enzyme gave a single band in SDS-PAGE with a molecular weight of 38 kDa.

The amino acid sequence of the mannana enzyme, d. H. the translated DNA sequence. is in SEQ ID NO: 2.

Determination of kinetic constants:

substrate: Carob gum and analysis of reducing sugar (PHBAH). Carob gum from Sigma (G-0753).

kinetic Determination using different concentrations of locust bean gum and 20 minute Incubation at 40 ° C at pH 10

kcat: 467 per sec

K _m : 0.08 grams per liter

MG: 3 8 kDa

pi (isoelectric point): 4.2

It it was found that the The optimum temperature of the mannanase is 60 ° C. The pH activity profile showed maximum activity between pH 8 and 10. DSC differential scanning calorimetry gave 77 ° C as a melting point at pH 7.5 in Tris buffer, which shows that this Enzyme is very thermostable.

The Detergent compatibility using 0.2% AZCL galactomannan from locust beans as a substrate and incubation as described above at 40 ° C shows excellent compatibility with conventional liquid Detergents and good tolerance with conventional Powder detergents.

Obtained the Bacillus subtilisis mannanase 168

The Bacillus subtilisis β-mannanase was characterized and purified as follows: The Bacillus subtilis genome was generated with a known Bacillus sp.-β-mannanase gene sequence (Mendoza et al., Biochemica et Biophysica Acta 1243: 552-554, 1995) for homology searched. The coding region of ydhT, whose product is unknown showed a 58% similarity to the well-known Bacillus-β-mannanase. The following Oligonucleotides were designed to amplify the sequences what che for encode the mature region 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 '. Total genomic DNA from Bacillus subtilis strain 1A95 was used as a template to use the mature ydhT region the aforementioned Amplify primer. The PCR is carried out using the GENE-AMP-PCR kit with AMPLITAQ-DNA polymerase (Perkin Elmer, Applied Biosytems, Foster City, CA). On an initial melting period at 95 ° C while 5 minutes were followed by 25 cycles of the following program: melting at 95 ° C while 1 minute, annealing or conditioning at 55 ° C for 2 minutes and extension at 72 ° C while 2 minutes. After the last cycle, the reaction was 10 minutes at 72 ° C kept the extension to complete. The PCR products were made using the QIAquick PCR purification kit (Qiagen, Chatsworth, CA).

The mature ydhT region amplified from Bacillus subtilis strain 1A95 was inserted into the expression vector pPG1524 (previously described) as follows. The amplified 1028bp fragment was digested with Mfel 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 lipase (13 h, 16 ° C) and used to transform a competent E. coli strain DH5-α. Colonies resistant to ampicilin were cultivated for DNA preparations. The DNA was then characterized by restriction analysis. The plasmid pPG3200 contains the mature region of the ydhT gene. The plasmid pPG3200 was then used to transform the competent Bacillus subtilis strain PG 632 (Saunders et al., 1992).

Seven Kanamycin-resistant Bacillus subtilis clones and a PG 632 control clone were picked and placed in 20 ml of 20/20/5 medium (20 g / l tryptone, 20 g / l yeast extract, 5 g / l NaCI), supplemented with 1 ml 25% maltrine, 120 μl 10 mM MnCl ₂ and 20 μl 50 mg / ml kanamycin. The clones were used overnight in 250 ml baffle flasks, shaking at 250 rpm, at 37 ° C. for the expression of the protein. The cells were spun down at 14,000 rpm for 15 minutes. One ul of each supernatant was diluted in 99 ul 50 mM sodium acetate (pH 6.0). One µl of this dilution was assayed using the Endo-1,4-β-mannanase "Beta Mannazyme Tabs" (Megazyme, Ireland) according to the manufacturer's instructions. The absorbance was read at 590 nm on a Beckman DU640 spectrophotometer. Clone 7 showed the highest absorbance of 1.67. The PG632 control showed no absorbance at 590 nm.

The supernatant was by SDS-PAGE on a 10-20% Tris-Glycine-Gel (Novex, San Diego, Ca) analyzed to get the expected protein size of 38 kDa to confirm. The samples were made as follows. A 500 μl sample from ydhT clone 7 and PG632 supernatants with 55.5 μl 100% trichloroacetic acid (Sigma) like with 100 μl 5% trichloroacetic acid washed, in 50 ul Tris Glycine SDS Sample Buffer (Novex) resuspended and boiled for 5 minutes. One μl of each sample was placed on the Gel electrophoresed at 30 mA for 90 minutes or pherographiert. A large protein band was observed to be at 38 kDa for the ydhT clone 7 migrated.

A 10-1 fermentation of Bacillus subtilis ydhT clone 7 was carried out in one B. Braun Biostat C fermenter performed. The fermentation conditions were as follows. The cells were kept in a complete medium similar to for 18 hours 20/20/5, at 37 ° C used. At the end of the fermentation batch, the cells removed, and the supernatant concentrated to 1 liter using a tangential flow filtration system has been. The final yield of β-mannanase in the concentrated supernatant was determined to 3 g / l.

The Purification of the β-mannanase from the fermentation supernatant was carried out as follows: 500 ml of supernatant were at 4 ° C for 10 minutes Centrifuged at 10,000 rpm. The centrifuged supernatant was then over Night at 4 ° C in two 4 l changes of 10 mM potassium phosphate (pH 7.2) by one Spectrapor membrane with a molecular weight exclusion of 12000-14000 (spectrum) dialyzed. The dialyzed supernatant was at 4 ° C for 10 minutes Centrifuged at 10,000 rpm. A 200 ml Q-Sepharose Fast Flow (Pharmacia) anion exchange column was made equilibrated with 1 liter of 10 mM potassium phosphate (pH 7.2) at 20 ° C, and 300 ml of supernatant were on the pillar loaded. Two flow fractions 210 ml (sample A) and 175 ml (sample B) were collected. The two fractions were assayed as above, except that the samples with 199 μl 50 mM sodium acetate (pH 6.0) were diluted and they showed an absorbance of 0.38 or 0.52. Two ul of each sample became 8 ul of tris-glycine SDS sample buffer (Novex, CA) added and cooked for 5 minutes. The resulting Samples were added on a 10-20% Tris-Glycine gel (Novex, Ca) 30 mA pherographed for 90 minutes. A main gang, accordingly at 38 kDa, was present in each sample and comprised more than 95% of the total protein. A BCA protein assay (Pierce) was carried out according to the manufacturer's instructions performed on both samples, bovine serum albumin was used as the standard. Samples A and B contained 1.3 mg / ml and 1.6 mg / ml β-mannanase, respectively. The identity of the protein was by ion spray mass spectrometry and amino terminal amino acid sequence analysis approved.

The purified β-mannanase samples were used to characterize the enzyme activity as follows. All assays used endo-1,4-β-mannanase beta-mannaryme tabs (Megazyme, Ireland) as described earlier. The activity was tested at a pH range of 3.0-9.0 in 50 mM citrate phosphate buffer, for an activity determination at pH 9.5, 50 mM CAPSO (Sigma) and for the pH range of 10.0-11 , 50 mM CAPS buffer was used. The optimum pH for the Bacillus subtilis β-mannanase was found to be pH 6.0-6.5. Temperature activity profiles were created in 50 mM citrate phosphate buffer (pH 6.5). The enzyme showed optimum activity at 40-45 ° C. Bacillus subtilis β-mannanase maintained significant activity at less than 15 ° C and more than 80 ° C. The specific activity against β-1,4-galactomannan was found to be 160000 µmol / min · mg β-mannanase, Endo-1,4-β-mannanase beta-Mannazyme tabs (Megazyme, Ireland) according to the Manufacturer's instructions were used. The nucleotide and amino acid sequences of Bacillus subtilisis-β-mannanase are in SEQ ID Nos. 5 and 6 shown.

The Mannanase is preferred in the compositions of the invention at a level of 0.0001 to 2% by weight, more preferably 0.0005 up to 0.1% by weight, the strongest preferably 0.001 to 0.02% by weight of pure enzyme, based on the weight the composition. brought in.

The enzyme of the invention comprises, in addition to the enzyme core comprising the catalytic domain, also a cellulose binding domain (CBD), the cellulose binding domain and the enzyme core (the catalytically active domain) of the enzyme being operably linked. The cellulose binding domain (CBD) can also be an integral part of the encoded enzyme, or a CBD from another source can be introduced into the enzyme, thereby creating an enzyme hybrid. In this context, it is intended that the term "cellulose binding domain" be understood as defined by Peter Tomme et al. "Cellulose Binding Domains: Classification and Properties" in "Enzymatic Degradation of Insoluble Carbohydrates", John N. Saddler and Michael H. Penner (ed.). ACS Symposium Series, No. 618, 1996. This definition classifies more than 120 cellulose-binding domains in 10 families (IX), and shows that CBDs are found in various enzymes such as cellulases, xylanases, mannanases, arabinofuranosidases, acetylesterases and chitinases. CBDs have also been found in algae, e.g. B. the red alga Porphyra purpurea, as a non-hydrolytic polysaccharide binding protein, see Tomme et al., Op.cit. However, most CBDs come from cellulases and xylanases. CBDs are found on the N- and C-termini of proteins or are internal. Enzyme hybrids are known in the art, see e.g. B. WO 90/00609 and WO 95/16782, and can by transforming a DNA construct which comprises at least one DNA fragment coding for the cellulose-binding domain, ligated, with or without linker, to a DNA sequence which is suitable for the mannanase enzyme is encoded, produced in a host cell and by using the host cell to express the fused gene. Enzyme hybrids can be described by the following formula: CBD - MR - X, wherein CBD is the N-terminal or the C-terminal region of an amino acid sequence corresponding to at least the celulose-binding domain; MR is the central region (the linker) and can be a bond or a short linking group, preferably from about 2 to about 100 carbon atoms, more preferably from 2 to 40 carbon atoms; or preferably about 2 to about 100 amino acids, more preferably 2 to 40 amino acids long; and X is an N-terminal or C-terminal region of the enzyme of the invention.

The mentioned above Enzymes can of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. The origin can also mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or unpurified forms of these enzymes can be used become. Nowadays it is a common practice Wild-type enzymes over Modify protein / genetic engineering approaches to improve their performance efficiency in cleaning compositions of the invention. To the Example the variants should be designed in such a way that the compatibility of the enzyme too common found components of such compositions is increased. Alternatively, the variant can be designed so that the optimal pH Bleach or chelator stability, and catalytic activity and the like tailored to the enzyme variant in order to meet the respective cleaning application.

In particular should, in the case of bleach stability, attention to amino acids which are sensitive across from Are oxidation, and for the surfactant compatibility on the surface charges be focused. The isoelectric point of such enzymes can be determined by the substitution of some charged amino acids are modified, e.g. B. can be an increase The isoelectric point will help ensure compatibility with anionic To improve surfactants. The stability of the enzymes can continue by generating z. B. of additional salt bridges and the reinforcement of metal binding sites to increase chelating stability be enlarged.

The percarbonate compound

The Detergent compositions described herein typically contain 0.1 to 50% by weight, preferably 0.5 to 35% by weight, most preferred 1 to 25% by weight of an alkali metal percarbonate bleach in the form of particles with an average size of 250 to 900 microns, preferably 500 to 700 microns. Laundry additives typically contain 20 to 80% of said percarbonate particles.

Preferred detergent compositions according to the present invention comprise a level of mannanase (pure enzyme based on the weight of the total composition) from 0.0001 to 2 Wt .-%, and a level of percarbonate from 0.1 to 50 wt .-% of the total composition, preferably a mannana level from 0.0005 to 0.5 wt .-% and a percarbonate level from 0.5 to 35 wt .-% %, more preferably a level of mannanase from 0.001 to 0.1%, and a percarbonate level from 1 to 25%.

The alkali metal percarbonate bleach is usually in the form of the sodium salt. Sodium percarbonate is an addition compound with a formula corresponding to 2Na ₂ CO ₃ .3H ₂ O ₂ . To increase storage stability, the percarbonate bleach can be coated, e.g. B. with another mixed salt of an alkali metal sulfate and carbonate. Such coatings, along with coating methods, have previously been described in GB 1,466,799 issued to Interox on March 9, 1977. The weight ratio of the mixed salt coating material to percarbonate is in the range of 1: 2000 to 1: 4, more preferably 1:99 to 1: 9, and most preferably 1:49 to 1:19. The mixed salt preferably consists of sodium sulfate and sodium carbonate, which has the general formula Na2SO4.n.Na2CO3, in which n is 0.1 to 3, preferably n 0.3 to 1.0 and most preferably n 0.2 to 0, 5 is.

suitable Percarbonate for the purpose of the present invention is sodium percarbonate, which is described in WO 97/35591, characterized by a intrinsic mean particle size of 500 up to 100 µm, with no more than 20% less than 350 µm, and a moisture absorption of not more than 30 g per 1000 g-sample at 80% relative humidity and 32 ° C in 24 hours, or labeled by an average particle size of 500 up to 1200 μm and a 7-day aging heat emission 40 ° C from under 3 mu W / g in 16 hours. The sodium percarbonate will also suitably from hydrogen peroxide and sodium carbonate aqueous medium made without the use of chloride salting agents, such as described in WO 97/35806.

Other suitable coating materials are sodium silicate with a SiO ₂ : Na ₂ O ratio of 1.6: 1 to 2.8: 1, and magnesium silicate.

in the Commercially available Carbonate / sulfate coated percarbonate bleach can do one low levels of a heavy metal masking agent, such as EDTA, 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP) or an aminophosphonate, which during of the manufacturing process is included. preferred Heavy metal masking agent for incorporation as hereinbefore described, close the organic phosphonates and aminoalkylene poly (alkylene phosphonates), such as the alkali metal ethane-1-hydroxydiphosphonates, the nitrilotrimethylene phosphonates, the ethylenediaminetetramethylenephosphonates and the diethylenetriaminepentamethylenephosphonates on.

Detergent components

The Detergent compositions of the invention must have at least one additional one Detergent component included. The exact nature of this additional Component, and its contribution level, are determined by the physical Form of composition and nature of the cleaning process for which they should be used depend.

The Detergent compositions according to the invention can Liquids, Pastes, gels, bars, Tablets, sprays, foam, powder or granules. Granular compositions can also available in "compact" form, and the liquid Compositions can also be in a "concentrated" form.

In a preferred embodiment The present invention relates to a laundry composition comprising a mannanase and a percarbonate. In a second embodiment The present invention relates to dishwashing compositions.

The Compositions of the invention can be used, for example, as manual and automatic dishwashing compositions, manual and machine laundry detergent compositions, including laundry additive compositions and compositions suitable for use in impregnation and / or Pretreatment of soiled textiles and added to the rinse cycle Fabric softening compositions can be formulated.

When formulated as compositions for use in manual dishwashing processes, the compositions of the invention preferably contain a surfactant and preferably other detergent compounds selected from organic polymeric compounds, foam-enhancing agents, metal ions Group II, solvents, hydrotropes and additional enzymes.

at Formulation as compositions suitable for use in a machine laundry process, The compositions of the invention preferably contain both a surfactant as well as a builder compound and an additional one or several detergent components, preferably selected from organic polymeric compounds, bleaches, additional Enzymes, foam suppressants, Dispersants, lime soap dispersants. soil suspension and anti-redeposition agents and corrosion inhibitors. Laundry compositions can also plasticizers as additional Detergent components included. Such compositions containing Mannanase and percarbonate Textile cleaning, stain removal, whiteness retention, color appearance, Provide dye transfer inhibition and disinfection if they as laundry detergent compositions be formulated.

The Compositions of the invention can also be used as detergent additive products in solid or liquid Shape can be used. Such additive products supplement or intended to increase the Performance of conventional Detergent composition and can be added at any stage of the cleaning process.

If needed is the density of the laundry detergent compositions described herein in the range from 400 to 1200 g / liter, preferably 500 to 950 g / liter the composition, measured at 20 ° C.

The "compact" form of the herein compositions described is best determined by the density, and in terms of composition, by the amount of inorganic filler salt reflected; inorganic filler salts are conventional Constituents of detergent compositions in powder form; in conventional Detergent compositions are essentially the filler salts Amounts, typically 17-35 % By weight of the total composition. In the compact compositions is the filler salt present in amounts which do not exceed 15% by weight of the total composition, preferably not over 10% by weight, the strongest preferably not over Go 5% by weight of the composition. The inorganic filler salts as meant in the present compositions are selected from the Alkali and alkaline earth metal salts of sulfates and chlorides. On preferred filler salt is sodium sulfate.

Liquid detergent compositions according to the present Invention can even in a "concentrated Shape ". In such a case, the liquid detergent compositions according to the present Invention a lower amount of water, compared to conventional liquid detergents, contain. Typically is the water content of the concentrated liquid detergent is preferred less than 40 wt%, more preferably less than 30 wt%, am most preferably less than 20% by weight of the detergent composition.

suitable Detergent compounds for use herein are selected from the group selected which consists of the compounds described below.

surfactant

The Detergent compositions according to the present Invention generally comprise a surfactant system, the surfactant from nonionic and / or anionic and / or cationic and / or ampholytic and / or zwitterionic and / or semipolar surfactants chosen can be.

The Surfactant is typically at a level of 0.1 to 60% by weight available. Stronger preferred incorporation levels range from 1 to 35% by weight, the strongest preferably 1 to 30% by weight of the detergent compositions according to the invention.

The Surfactant is preferably formulated to be included in the composition existing enzyme components to be compatible. In liquid or The most preferred gel-like composition is the surfactant formulated so that it the stability promotes or at least does not promote any enzyme in these compositions deteriorated.

According to the present Preferred surfactant systems to be used in the invention include one or more of the nonionic and / or anionic described herein Surfactant as a surfactant.

Polyethylene, polypropylene and polybutylene oxide condensates of alkylphenols are used suitable as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being 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, in either a straight or branched chain configuration with the alkylene oxide. In a preferred embodiment, the ethylene oxide is present in an amount equal to about 2 to about 25 moles, more preferably about 3 to about 15 moles, of ethylene oxide per mole of alkylphenol. Commercially available nonionic surfactants of this type include Igepal ^™ CO-630, marketed by GAF Corporation, and Triton ^™ X-45, X-114, X-100 and X-102, all of which are marketed by the Rohm & Haas Company. on. These surfactants are commonly referred to as alkylphenol alkoxylates (e.g., alkylphenol ethoxylates).

The condensation products of primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention. The alkyl chain of the aliphatic alcohol can be either straight or branched, primary or secondary and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl group of about 8 to about 20 carbon atoms, more preferably about 10 to 18 about carbon atoms, with about 2 to about 10 moles of ethylene oxide per mole of alcohol. There are about 2 to about 7 moles of ethylene oxide and most preferably 2 to 5 moles of ethylene oxide per mole of alcohol in the condensation products. Examples of commercially available nonionic surfactants of this type include: Tergitol ^™ 15-S-9 (the condensation product of linear C ₁₁ -C ₁₅ alcohol with 9 moles of ethylene oxide) and Tergitol ^™ 24-L-6 NMW (the condensation product of primary C ₁₂ -C ₁₄ alcohol with 6 moles of ethylene oxide with a narrow molecular weight distribution), both marketed by Union Carbide Corporation; Neodol ^TM 45-9 (the condensation product of linear C ₁₄ -C ₁₅ alcohol with 9 moles of ethylene oxide), Neodol ^TM 23-3 (the condensation product of linear C ₁₂ -C ₁₃ alcohol with 3.0 moles of ethylene oxide), Neodol ^TM 45-7 (the condensation product of C ₁₄ -C ₁₅ linear alcohol with 7 moles of ethylene oxide), Neodol ^™ 45-5 (the condensation product of C ₁₄ -C ₁₅ linear alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company; Kyro ^™ EOB (the condensation product of C ₁₃ -C ₁₅ alcohol with 9 moles of ethylene oxide), marketed by The Procter & Gamble Company; and Genapol LA O3O or O5O (the condensation product of C ₁₂ -C ₁₄ alcohol with 3 or 5 moles of ethylene oxide), marketed by Hoechst. The preferred HLB range in these products is 8-11 and most preferably 8-10.

Likewise useful as the nonionic surfactant of the surfactant systems of the present Invention are the alkyl polysaccharides disclosed in U.S. Patent 4 565,647, Llenado, issued January 21, 1986, with a hydrophobic Group about 6 to about 30 carbon atoms, preferably about 10 to about 16 carbon atoms, contains and a hydrophilic polysaccharide, e.g. B. a polyglycoside group with about 1.3 until about 10, preferably approximately 1.3 to approximately 3, most preferably from about 1.3 to about 2.7, Saccharide units. Any 5 or 6 carbon atom containing reducing saccharide, e.g. B. glucose, can be used, galactose and galactosyl residues can for the Glucosyl residues can be substituted (the hydrophobic is optional Group tied to the 2-, 3-, 4-, etc. positions, creating a Glucose or galactose as opposed to a glucoside or galactoside is obtained). The intersaccharide bonds can e.g. B. between the first Position of additional Saccharide units and the 2-, 3-, 4- and / or 6-position of the previous one Saccharide units are.

The preferred alkyl polyglycosides have the formula R ² O (C _n H _2n O) _t (glycosyl) _x wherein R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof, in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is 0 to about 10, preferably 0; and x is 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. The glycosyl is preferably derived from glucose. To make these compounds, the alcohol or alkyl polyethoxy alcohol is first formed and then reacted with glucose or a source of glucose to form the glucoside (attachment at the 1-position). The additional glycosyl units can then be attached between their 1-position and the 2-, 3-, 4- and / or 6-position of the preceding glycosyl units, preferably mainly at the 2-position.

The condensation products of ethylene oxide with a hydrophobic base, which are formed by the condensation of propylene oxide with propylene glycol, are also suitable for use as additional nonionic surfactant systems of the present invention. The hydrophobic portion of these compounds preferably has a molecular weight from about 1500 to about 1800 and shows water insolubility. The addition of polyoxyethylene residues to this hydrophobic portion tends to increase the water solubility of the molecule as a whole and the liquid character of the product is maintained to the point in which the polyoxyethylene content is approximately 50% of the total weight of the condensation product, which corresponds to a condensation with up to approximately 40 moles of ethylene oxide. Examples of compounds of this type include certain of the commercially available Plurafac ^™ LF404 and Pluronic ^™ surfactants, marketed by BASF.

Also suitable for use as the nonionic surfactant 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 remainder of these products consists of the reaction product of ethylenediamine and an excess of propylene oxide and generally has a molecular weight from about 2,500 to about 3,000. This hydrophobic residue is condensed with ethylene oxide to the extent that the condensation product contains from about 40 to about 80 weight percent polyoxyethylene and has a molecular weight from about 5,000 to about 11,000. Examples of this type of nonionic surfactant include certain of the commercially available Tetronic ^™ compounds that are marketed by BASF.

Preferred for use as the nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkylphenols, condensation products of primary and secondary aliphatic alcohols with about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides, and mixtures thereof. Most preferred are C ₈ -C ₁₄ alkylphenol ethoxylates with 3 to 15 ethoxy groups and C ₈ -C ₁₈ alcohol ethoxylates (preferably C ₁₀ average) with 2 to 10 ethoxy groups and mixtures thereof.

worin R¹ H ist, oder R¹ C₁-C₄-Hydrocarbyl, 2-Hydroxyethyl, 2-Hydroxypropyl oder eine Mischung davon ist; R² ein C₅-C₃₁-Hydrocarbyl ist, und Z ein Polyhydroxyhydrocarbylrest mit einer linearen Hydrocarbylkette mit mindestens 3 Hydroxylen, welche direkt mit der Kette verknüpft sind, oder ein alkoxyliertes Derivat davon ist. Vorzugsweise ist R¹ Methyl, R² ist eine geradkettige C₁₁-C₁₅-Alkyl- oder C₁₆-C₁₈-Alkyl- oder -Alkenylkette, wie Cocosnussallcyl oder Mischungen hiervon, und Z wird aus einem reduzierenden Zucker, wie Glucose, Fructose, Maltose, Lactose, in einer reduktiven Aminierungsreaktion abgeleitet.Highly preferred nonionic surfactants are the polyhydroxy fatty acid amide surfactants of the formula:

wherein R ^{1 is} H, or R ^{1 is} C ₁ -C ₄ hydrocarbyl, 2-hydroxyethyl, 2-hydroxypropyl, or a mixture thereof; R ^{2 is} a C ₅ -C ₃₁ hydrocarbyl, and Z is a polyhydroxyhydrocarbyl group having a linear hydrocarbyl chain with at least 3 hydroxyls directly linked to the chain, or an alkoxylated derivative thereof. Preferably R ^{1 is} methyl, R ² is a straight chain C ₁₁ -C ₁₅ alkyl or C ₁₆ -C ₁₈ alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is made from a reducing sugar such as glucose or fructose , Maltose, lactose, derived in a reductive amination reaction.

Suitable anionic surfactants that can be used are linear alkyl benzene sulfonate, alkyl ester sulfonate surfactants, including linear esters of C ₈ -C ₂₀ carboxylic acids (ie fatty acids), which are mixed with gaseous SO ₃ according to "The Journal of the American Oil Chemists Society", 52 ( 1975), pages 323-329, are sulfonated. Suitable starting materials include natural fatty substances as derived from tallow, palm oil, etc.

worin R³ ein C₈-C₂₀-Hydrocarbyl, vorzugsweise ein Alkyl oder eine Kombination davon ist, R⁴ ein C₁-C₆-Hydrocarbyl, vorzugsweise ein Alkyl oder eine Kombination davon ist, und M ein Kation ist, das ein wasserlösliches Salz mit dem Alkylestersulfonat bildet. Geeignete salzbildende Kationen schließen Metalle, wie Natrium-, Kalium- und Lithium, und substituierte oder nichtsubstituierte Ammoniumkationen, wie Monoethanolamin, Diethanolamin und Triethanolamin, ein. Vorzugsweise ist R³ C₁₀-C₁₆-Alkyl und R⁴ Methyl, Ethyl oder Isopropyl. Besonders bevorzugt sind die Methylestersulfonate, worin R³ C₁₀-C_16-Alkyl ist.The preferred alkyl ester sulfonate surfactant, especially for laundry applications, comprises alkyl ester sulfonate surfactants of the following structural formula:

wherein R ^{3 is} a C ₈ -C ₂₀ hydrocarbyl, preferably an alkyl or a combination thereof, R ^{4 is} a C ₁ -C ₆ hydrocarbyl, preferably an alkyl or a combination thereof, and M is a cation which is a water-soluble Salt forms 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. R ³ is preferably C ₁₀ -C ₁₆ alkyl and R ^{4 is} methyl, ethyl or isopropyl. The methyl ester sulfonates in which R ^{3 is} C ₁₀ -C ₁₆ alkyl are particularly preferred.

Other suitable anionic surfactants include the alkyl sulfate surfactants, which are water soluble sal ze of acids of the formula ROSO ₃ M, wherein R is preferably a C ₁₀ -C ₂₄ hydrocarbyl, preferably an alkyl or hydroxyalkyl with a C ₁₀ -C ₂₀ alkyl component, more preferably a C ₁₂ -C ₁₈ alkyl or hydroxyalkyl , and MH or a cation, e.g. An alkali metal cation (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 alkylamines such as ethylamine , Diethylamine, triethylamine-derived quaternary ammonium cations, and mixtures thereof, etc.). Typically, alkyl chains of C ₁₂ -C _{16 are} preferred for lower wash temperatures (e.g. below about 50 ° C) and C ₁₆ -C ₁₈ alkyl chains are preferred for higher wash temperatures (e.g. above about 50 ° C).

Other anionic surfactants useful for detergent purposes can also be included in the detergent compositions of the present invention. These can include salts (including e.g. sodium, potassium, ammonium and substituted ammonium salts such as mono-, di- and triethanolamine salts) of soap, primary or secondary C ₈ -C ₂₂ alkanesulfonates, C ₈ -C ₂₄ - Olefin sulfonates, sulfonated polycarboxylic acids, produced by the sulfonation of the pyrolyzed product of alkaline earth metal citrates, such as. For example, described in British Patent No. 1,082,179, C ₈ -C ₂₄ alkyl polyglycol ether sulfates (containing up to 10 moles of ethylene oxide); Alkyl glycerol, fatty acyl, Fettoleoylglycerinsulfaten, alkyl phenol, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates, Allcylsuccinamaten and -sulfosuccinaten, Monoestern of sulfosuccinates (especially saturated and unsaturated C ₁₂ -C ₁₈ monoesters) and diesters of sulfosuccinates (especially saturated and unsaturated C ₆ -C ₁₂ diesters), acyl sarcosinates, sulfates of alkyl polysaccharides, such as the sulfates of alkyl polyglucoside (the nonionic, non-sulfated compounds are described below), branched primary alkyl sulfates and alkyl polyethoxy carboxylates, such as those of the formula RO (CH ₂ CH ₂ O) _k -CH ₂ -COO ^- M ⁺ , wherein R is a C ₈ -C ₂₂ alkyl, k is an integer from 1 to 10 and M is a soluble salt-forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin and resin acids and hydrogenated resin acids, which are present in or derived from tall oil.

Further Examples are in "Surfase Active Agents and Detergents "(Vol I and II by Schwartz, Perry and Berch). A variety such surfactants are also generally described in U.S. Patent 3,929,678; issued December 30, 1975 to Laughlin et al., which herein by reference, at column 23, line 58, to Column 29, line 23.

at Incorporation therein include the laundry detergent compositions typically about 1 to about 40% by weight of the present invention, preferably approximately 3 to about 20% by weight of such anionic surfactants.

Highly preferred anionic surfactants here include the alkyl alkoxylated sulfate surfactants, which are water-soluble salts or acids of the formula RO (A) _m SO ₃ M, in which R is an unsubstituted C ₁₀ -C ₂₄ alkyl or hydroxyalkyl group with a C ₁₀ - C ₂₄ alkyl component, preferably a C ₁₂ -C ₂₀ alkyl or hydroxyalkyl, more preferably a C ₁₂ -C ₁₈ alkyl or hydroxyalkyl, A is an ethoxy or propoxy moiety, m is greater than zero, typically between approximately 0.5 and about 6, more preferably between about 0.5 and about 3, and is MH or a cation which is, for example, a metal cation (e.g. sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or can be a substituted ammonium cation. Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein. Specific examples of substituted ammonium cations include methyl, dimethyl, trimethylammonium cations and quaternary ammonium cations such as tetramethylammonium and dimethylpiperidinium cations, and those derived from alkylamines such as ethylamine, diethylamine, triethylamine, mixtures thereof and the like. Exemplary surfactants are C ₁₂ -C ₁₈ alkyl polyethoxylate (1.0) sulfate (C ₁₂ -C ₁₈ E (1.0) M), C ₁₂ -C ₁₈ alkyl polyethoxylate (2.25) sulfate (C ₁₂ -C ₁₈ E (2.25) M), C ₁₂ -C ₁₈ alkyl polyethoxylate (3.0) sulfate (C ₁₂ -C ₁₈ E (3.0) M) and C ₁₂ -C ₁₈ alkyl polyethoxylate (4.0) sulfate (C ₁₂ -C ₁₈ E (4.0) M), where M is advantageously selected from sodium and potassium.

The Detergent compositions of the present invention can also cationic, ampholytic, zwitterionic and semipolar surfactants, as well as different non-ionic ones from those already described here and / or contain anionic surfactants.

Cationic detergent surfactants suitable for use in the detergent compositions of the present invention are those with a long chain hydrocarbon group. Examples of such cationic surfactants include ammonium surfactants, such as alkyltrimethylammonium halides, and such surfactants having the formula: [R ² (OR ³ ) _y ] [R ⁴ (OR ³ ) _y ] ₂ R ⁵ N ⁺ X ^- a wherein R ^{2 is} an alkyl or alkylbenzyl group having 8 to 18 Is carbon atoms in the alkyl chain, each R ^{3 is selected} from -CH ₂ CH ₂ -, -CH ₂ CH (CH ₃ ) -, -CH ₂ CH (CH ₂ OH) -, -CH ₂ CH ₂ CH ₂ - and mixtures existing group is selected; 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 connecting the two R ⁴ groups, -CH ₂ CHOH-CHOHCOR ⁶ CHOHCH ₂ OH wherein R ^{6 is} any hexose or hexose polymer having a molecular weight below about 1000 and hydrogen, if y is not 0, is selected from the group consisting; R ^{5 is} the same as R ⁴ or an alkyl chain, the total number of carbon atoms of R ² plus R ^{5 being} no more than about 18; each y is from 0 to about 10 and the sum of the y values is from 0 to about 15; and X is any compatible anion

wobei R1 ein Alkyl mit kurzer Kettenlänge (C6-C10) oder Alkylamidoalkyl der Formel (II) ist:

y 2–4, vorzugsweise 3 ist,
wobei R2 H oder ein C1-C3-Alkyl ist,
wobei x 0–4, vorzugsweise 0–2, am stärksten bevorzugt 0 ist,
wobei R3, R4 und R5 entweder gleich oder verschieden sind und entweder ein kurzkettiges Alkyl (C1-C3) oder alkoxyliertes Alkyl der Formel III sein können, wobei X ein Gegenion, vorzugsweise ein Halogenid, z. B. Chlorid oder Methylsulfat ist.

R6 ist C₁-C₄ und z ist 1 oder 2.
Bevorzugte Quat-Ammoniumtenside sind diejenigen, wie definiert in Formel I, wobei
R₁ für C₈, C₁₀ oder Mischungen davon steht, x = 0,
R₃, R₄ = CH₃ und R₅ = CH₂CH_2OH.A quaternary ammonium surfactant suitable for the present invention has the formula (I):

where R1 is a short chain alkyl (C6-C10) or alkylamidoalkyl of formula (II):

y is 2-4, preferably 3,
where R2 is H or a C1-C3 alkyl,
where x is 0-4, preferably 0-2, most preferably 0,
wherein R3, R4 and R5 are either the same or different and can be either short-chain alkyl (C1-C3) or alkoxylated alkyl of formula III, where X is a counter ion, preferably a halide, e.g. B. is chloride or methyl sulfate.

R6 is C ₁ -C ₄ and z is 1 or 2.
Preferred quat ammonium surfactants are those as defined in Formula I, wherein
R _{1 represents} C ₈ , C ₁₀ or mixtures thereof, x = 0,
R ₃ , R ₄ = CH ₃ and R ₅ = CH ₂ CH _2O H.

Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition, with the formula: R ₁ R ₂ R ₃ R ₄ N ⁺ X ^- (i) wherein R _{1 is} C ₈ -C ₁₆ alkyl, each of _R2 , R ₃ and R _{4 is} independently C ₁ -C ₄ alkyl, C ₁ -C ₄ hydroxyalkyl, benzyl and - (C ₂ H ₄₀ ) _X H , where x is from 2 to 5 and X is an anion. No more than one of R ₂ , R _3, or R ₄ should be benzyl.

The preferred alkyl chain length for R ₁ is C ₁₂ -C ₁₅ , especially if the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat, or synthetically derived from olefin expansion or OXO alcohol synthesis. Preferred groups for R ₂ , R ₃ and R ₄ are methyl and hydroxyethyl groups, and the anion X can be selected from halide, methosulfate, acetate and phosphate ions. Examples of suitable quaternary ammonium compounds of formulas (i) for use herein are:

• Kokosnußtrimethylammoniumchlorid or bromide;
• Kokosnußmethyldihydroxyethylammoniumchlorid or bromide;
• decyl triethyl ammonium chloride;
• Decyldimethylhydroxyethylammonium chloride or bromide;
• C ₁₂ -C ₁₅ dimethylhydroxyethylammonium chloride or bromide;
• Kokosnußdimethylhydroxyethylammoniuinchlorid or bromide;
• myristyl;
• Lauryldimethylbenzylammonium chloride or bromide;
• Lauryldimethyl (ethenoxy) ₄ ammonium chloride or bromide;
• Choline ester (compound of formula (i), wherein R ₁
• 
• Dialkylimidazolines [Compounds of Formula (i)].

Other cationic surfactants useful herein are also in U.S. Patent 4,228,044, Cambre, issued October 14, 1980, and in the European patent application EP 000 224 described.

typical cationic fabric softener components close the water-insoluble ones quaternary ammonium fabric softening agents or their corresponding amine precursor, the most common double alkyl chain ammonium chloride or methyl sulfate used are.

preferred cationic plasticizers among these include the following:

• 1) ditallow dimethyl ammonium chloride (DTDMAC);
• 2) di-hydrogenated tallow dimethyl ammonium chloride;
• 3) dihydrogenated tallow dimethylammonium methyl sulfate;
• 4) distearyldimethylammonium chloride;
• 5) dioleyldimethylammonium chloride;
• 6) dipalmitylhydroxyethylmethylammonium chloride;
• 7) stearylbenzyldimethylammonium chloride;
• 8) tallow trimethyl ammonium chloride;
• 9) hydrogenated tallow trimethyl ammonium chloride;
• 10) C ₁₂ -C ₁₄ alkylhydroxyethyldimethylammonium chloride;
• 11) C ₁₂ -C ₁₈ alkyl dihydroxyethyl methyl ammonium chloride;
• 12) di (stearoyloxyethyl) dimethylammonium chloride (DSOEDMAC);
• 13) di (tallow-oxy-ethyl) dimethylammonium chloride;
• 14) ditallow imidazolinium methyl sulfate;
• 15) 1- (2-tallowoylamidoethyl) -2-tallowylimidazolinium methyl sulfate.

biological degradable quaternaries Ammonium compounds are used as alternatives to those conventionally Dual alkyl chain ammonium chlorides and methyl sulfates proposed Service.

Such quaternary Ammonium compounds contain long-chain alk (en) yl groups, interrupted by functional groups, such as carboxy groups. The materials and fabric softening compositions, which contain these are published in numerous publications discloses such as EP-A-0 040 562 and FP-A-0 239 910.

worin Q gewählt ist aus -O-C(O)-, -C(O)-O-, -O-C(O)-O-, -NR⁴-C(O)-, -C(O)-NR⁴-;
R¹ ist (CH₂)_n-Q-T² oder T³;
R² ist (CH₂)_m-Q-T⁴ oder T⁵ oder R³;
R³ ist C₁-C₄-Alkyl oder C₁-C₄-Hydroxyalkyl oder H;
R⁴ ist H oder C₁-C₄-Alkyl oder C₁-C₄-Hydroxyalkyl;
T¹, T², T³, T⁴, T⁵ sind unabhängig voneinander C₁₁-C₂₂-Alkyl oder Alkenyl;
n und m sind ganze Zahlen von 1 bis 4; und
X^– ist ein weichmacherkompatibles Anion. Nicht-einschränkende Beispiele von weichmacherkompatiblen Anionen schließen Chlorid oder Methylsulfat ein.The quaternary ammonium compounds and amine precursors herein have the following formulas (I) or (II): (

wherein Q is selected from -OC (O) -, -C (O) -O-, -OC (O) -O-, -NR ⁴ -C (O) -, -C (O) -NR ⁴ -;
R ¹ is (CH ₂ ) _n -QT ² or T ³ ;
R ² is (CH ₂ ) _m -QT ⁴ or T ⁵ or R ³ ;
R ³ is C ₁ -C ₄ alkyl or C ₁ -C ₄ hydroxyalkyl or H;
R ⁴ is H or C ₁ -C ₄ alkyl or C ₁ -C ₄ hydroxyalkyl;
T ¹ , T ² , T ³ , T ⁴ , T ⁵ are independently C ₁₁ -C ₂₂ alkyl or alkenyl;
n and m are integers from 1 to 4; and
X ^- is a plasticizer-compatible anion. Non-limiting examples of plasticizer-compatible anions include chloride or methyl sulfate.

The alkynl or alkenyl chain T ¹ , T ² , T ³ , T ⁴ , T ⁵ must contain at least 11 carbon atoms, preferably at least 16 carbon atoms. The chain can be straight or branched. Tallow is a convenient and inexpensive source of long chain alkyl and alkenyl material. The compounds in which T ¹ , T ² , T ³ , T ⁴ , T ^{5 represent} the mixture of long chain materials which are typical of tallow are particularly preferred.

specific Examples of for use in the aqueous fabric softening compositions herein suitable quaternaries Close ammonium compounds:

• 1) N, N-di (tallowoyloxyethyl) -N, N-dimethylammonium chloride;
• 2) N, N-di (tallowoyloxyethyl) -N-methyl-N- (2-hydroxyethyl) ammonium methyl sulfate;
• 3) N, N-di (2-tallowoyloxy-2-oxoethyl) -N, N-dimethylammonium chloride;
• 4) N, N-di (2-tallowoyloxyethylcarbonyloxyethyl) -N, N-dimethylammonium chloride;
• 5) N- (2-tallowoyloxy-2-ethyl) -N- (2-tallowoyloxy-2-oxo-ethyl) -N, N-dimethylammonium chloride;
• 6) N, N, N-tri (tallowoyloxyethyl) -N-methylammonium chloride;
• 7) N- (2-tallowoyloxy-2-oxoethyl) -N- (tallowyl) -N, N-dimethylammonium chloride; and
• 8) 1,2-ditalgoyl-oxy-3-trimethylammonium propane chloride; and mixtures any of the above materials.

at Incorporation herein includes the detergent compositions of the present Invention typically 0.2 to about 25% by weight, preferably approximately 1 to about 8% by weight of such cationic surfactants.

ampholytic Surfactants are for use in the detergent compositions of the present invention also suitable. These surfactants can be rough as aliphatic derivatives of secondary or tertiary amines or aliphatic derivatives of heterocyclic, secondary and tertiary Amines in which the aliphatic radical is straight or branched can be described. One of the aliphatic substituents contains at least approximately 8 carbon atoms, typically about 8 to about 18 carbon atoms, and contains at least one an anionic, water solubilizing group, e.g. B. carboxy, sulfonate, Sulfate; see U.S. Patent No. 3,929,678, issued December 30 1975 to Laughlin et al., Column 19, lines 18-35, for examples of ampholytic Surfactants.

at Incorporation herein includes the detergent compositions of the present Invention typically 0.2 to about 15% by weight, preferably approximately 1 to about 10% by weight of such ampholytic surfactants.

Zwitterionic surfactants are also suitable for use in detergent compositions. These surfactants can be roughly classified as derivatives of secondary and tertiary amines, derivatives of heterocyclic, secondary and tertiary amines or as derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds; see that on December 30, 1975 to Laughlin et al. issued U.S. Patent No. 3,929,678, column 19, line 38 to column 22, line 48, for examples of zwitterionic surfactants.

at Incorporation herein includes the detergent compositions of the present Invention typically 0.2 to about 15% by weight, preferably approximately 1 to about 10% by weight of such zwitterionic surfactants.

semipolar nonionic surfactants are a special category of nonionic Surfactants, which are water-soluble Amine oxides with an alkyl group of about 10 to about 18 carbon atoms and two from the group of alkyl groups and hydroxyalkyl groups with about 1 to approximately Group consisting of 3 carbon atoms; water soluble phosphine oxides with an alkyl group of approximately 10 to about 18 carbon atoms and 2 from that of alkyl groups and hydroxyalkyl groups with about 1 to about Group consisting of 3 carbon atoms; and water-soluble sulfoxides with an alkyl group of approximately 10 to about 18 carbon atoms and one of the alkyl and hydroxyalkyl radicals with about 1 to about 3 carbon group consisting of selected radical.

worin R³ eine Alkyl-, Hydroxyalkyl- oder Alkylphenylgruppe oder Mischungen davon mit ungefähr 8 bis ungefähr 22 Kohlenstoffatomen ist; R⁴ eine Alkylen- oder Hydroxyalkylengruppe mit ungefähr 2 bis ungefähr 3 Kohlenstoffatomen oder Mischungen davon bedeutet; x 0 bis ungefähr 3 ist; und jedes R⁵ eine Alkyl- oder Hydroxyalkylgruppe mit ungefähr 1 bis ungefähr 3 Kohlenstoffatomen oder eine Polyethylenoxidgruppe mit ungefähr 1 bis ungefähr 3 Ethylenoxidgruppen ist. Die R⁵-Gruppen können miteinander verbunden sein, z. B. durch ein Sauerstoff- oder Stickstoffatom, wodurch eine Ringstruktur gebildet wird.Semipolar nonionic detergent surfactants include the amine oxide surfactants with the following formula:

wherein R ^{3 is} an alkyl, hydroxyalkyl or alkylphenyl group or mixtures thereof having from about 8 to about 22 carbon atoms; R ^{4 represents} an alkylene or hydroxyalkylene group having about 2 to about 3 carbon atoms or mixtures thereof; x is 0 to about 3; and each R ^{5 is} an alkyl or hydroxyalkyl group with about 1 to about 3 carbon atoms or a polyethylene oxide group with about 1 to about 3 ethylene oxide groups. The R ⁵ groups can be connected to one another, e.g. B. by an oxygen or nitrogen atom, whereby a ring structure is formed.

These amine oxide surfactants include, in particular, C ₁₀ -C ₁₈ alkyl dimethyl amine oxides and C ₈ -C ₁₂ alkoxyethyl dihydroxyethyl amine oxides.

at Incorporation herein include the cleaning compositions of present invention typically 0.2 to about 15% by weight, preferably approximately 1 to about 10% by weight of such semipolar nonionic surfactants.

The Detergent compositions of the present invention can also be used comprise a cosurfactant from the group of primary or tertiary Amines.

Suitable primary amines for use herein include amines according to the formula R ₁ NH ₂ , wherein R1 is a C ₆ -C ₁₂ , preferably C ₆ -C ₁₀ alkyl chain or R ₄ X (CH ₂ ) _n , X -O- , -C (O) NH- or -NH-, R _{4 is} a C ₆ -C ₁₂ alkyl chain, and n is between 1 to 5, preferably 3. R ₁ alkyl chains can be straight or branched and can be interrupted with up to 12, preferably less than 5, ethylene oxide units.

preferred Amines according to the here Formula above are n-alkyl amines. Suitable amines for use in this can chosen are made from 1-hexylamine, 1-octylamine, 1-decylamine and laurylamine. Other preferred primary Close amines C8-C10 oxypropylamine, octyloxypropylamine, 2-ethylhexytoxypropylamine, laurylamidopropylamine and amidopropylamine.

sind, _R3 entweder eine C₆-C₁₂-, vorzugsweise C₆-C₁₀-Alkylkette ist, oder R₃ R₄X(CH₂)_n ist, wobei X -O-, -C(O)NH- oder -NH- ist, R₄ ein C₄-C₁₂ ist, n zwischen 1 bis 5, bevorzugt 2–3 ist, R₅ H oder C₁-C₂-Alkyl ist und x zwischen 1 und 6 beträgt.Suitable tertiary amines for use herein include tertiary amines having the formula R ₁ R ₂ R ₃ N, wherein R1 and R2 are C ₁ -C ₈ alkyl chains

_{R3 is} either a C ₆ -C ₁₂ , preferably C ₆ -C ₁₀ alkyl chain, or R ₃ R _{4 is} X (CH ₂ ) _n , where X is -O-, -C (O) NH- or - Is NH-, R _{4 is} a C ₄ -C ₁₂ , n is between 1 to 5, preferably 2-3, R _{5 is} H or C ₁ -C ₂ alkyl and x is between 1 and 6.

R ₃ and R ₄ can be linear or branched; R ₃ alkyl chains can be interrupted with up to 12, preferably less than 5, ethylene oxide groups.

sind, worin R₅H oder CH₃ ist, und x = 1–2 ist.Preferred tertiary amines are R ₁ R ₂ R ₃ N, in which R _{1 is} a C ₆ -C ₁₂ allyl chain, R ₂ and R _{3 are} C ₁ -C ₃ alkyl or

where R _{5 is} H or CH ₃ and x = 1-2.

worin R₁ C₆-C₁₂-Alkyl ist, n 2–4 ist, vorzugsweise n 3 ist; R₂ und R₃ für C₁-C₄ stehen.The amidoamines of the formula are also preferred

wherein R _{1 is} C ₆ -C ₁₂ alkyl, n is 2-4, preferably n 3; R ₂ and R _{3 are} C ₁ -C ₄ .

The most preferred amines of the present invention include 1-octylamine, 1-hexylamine, 1-decylamine, 1-dodecylamine, C _8-10 oxypropylamine, N-coco-1,3-diaminopropane, coconut alkyl dimethyl amine, lauryl dimethyl amine, lauryl bis (hydroxyethyl) amine, coconut bis (hydroxyethyl) amine, laurylamine with 2 moles propoxylated, octylamine with 2 moles propoxylated, laurylamidopropyldimethylamine, C _8-10 amidopropyldimethylamine and C10 amidopropyldimethylamine. The most preferred amines for use in the compositions described herein are 1-hexylamine, 1-octylamine, 1-decylamine and 1-dodecylamine. Particularly desirable are n-dodecyldimethylamine and bishydroxyethyl coconut alkylamine and oleylamine, 7-fold ethoxylated, laurylamidopropylamine and cocosamidopropylamine.

Conventional detergent enzymes

The Detergent compositions can additionally in addition to the mannanase enzyme and percarbonate, one or more enzymes include which cleaning services, textile care and / or Provide disinfection benefits. Preferably the detergent composition of the present invention comprise a protease. It is surprising it has been found that the Compositions of the present invention which further comprise a Protease enzyme include, provide better whiteness and stain removal benefits.

Suitable proteases are the proteases from the ICTPAC classification EC 3.4 .-, preferably the endo-serine protease from the IUPAC classification EC 3.4.21.-, more preferably the subtilisin proteases from the IUPAC classification EC 3.4.21.62. These EC 3.4.21.62 proteases are the subtilisins which are obtained from certain strains of B. subtilis and B. licheniformis (subtilisin BPN and BPN '). One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, 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 from Novo. Other suitable proteases include ALCALA-SE ^® , DLIRAZYM ^® and SAVINASE ^® from Novo and MAXATASE ^® , MAXACAL ^® , PROPERASE ^® and MAXAPEM ^® (protein genetically modified Maxacal) from Gist-Brocades. Proteolytic enzymes also include modified bacterial serine proteases, such as those described in European Patent Application Serial No. 87 303 761.8, filed April 28, 1987 (particularly pages 17, 24 and 98}, and which are referred to herein as "Protease B", and European Patent Application 199,404, Venegas, published October 29, 1986, which relates to a modified bacterial serine proteolytic enzyme, referred to herein as "Protease A." Suitable is the protease, which is referred to herein as "Protease C "which is a variant of a Bacillus alkaline serine protease in which lysine replaces arginine at position 27, tyrosine replaces valine at position 104, serine replaces asparagine at position 123, and alanine replaces threonine at position 274. Protease C is described in EP 90 915 956.4 , corresponding to WO 91/06637, published May 16, 1991. Genetically modified variants, in particular of protease C, are also included here.

A preferred protease referred to as "Protease D" is a carbonyl hydrolase variant with an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a variety of amino acid residues at one position in the Carbonyl hydrolase is derived, which is equivalent to position +76, preferably also in combination with one or more amino acid residue positions, equivalent to those selected from the group consisting of +99, +101, +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218 , +222, +260, +265 and / or +274 according to the numbering of Bacillus amyloliquefaciens subtilisin, as described in WO95 / 10591 and in the patent application by C. Ghosh et al., "Bleaching Compositions Comprising Protease Enzymes" serial number 08 / 322,677, which was filed on October 13, 1994. Also suitable is a carbonyl hydrolase variant of the protease described in WO 95/10591 with an amino acid sequence which was derived by replacing a plurality of amino acid residues exchanged in the precursor enzyme, corresponding to position +210, in combination with one or more of the following residues : +33, +62, +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, + 164, +166, +167, +170, +209, +215, +217, +218 and +222, the numbered position being the naturally occurring subtilisin from Bacillus amyloliquefaciens or equivalent amino acid residues in other carbonyl hydrolases or subtilisins such as Bacillus lentus- Subtilisin, corresponds to (copending patent application US serial number 60 / 048,550, filed June 4, 1997).

Proteases described in the patent applications are also suitable for the present invention EP 251 446 and WO91 / 06637, Protease BLAP ^® , described in WO91 / 02792, and their variants, which are described in WO95 / 23221.

See also a high pH protease from Bacillus sp. NCIMB 40338, described in WO93 / 18140 A by Novo. Enzymatic detergents comprising protease, one or more other enzymes and a reversible protease inhibitor are described in WO92 / 03529 A by Novo. If desired, a protease with reduced adsorption and increased hydrolysis is available, as described in WO95 / 07791 from Procter & Gamble. A recombinant trypsin-like protease for detergents which is suitable herein is described in Novo WO94 / 25583. Other suitable proteases are in the EP 516 200 described by Unilever.

The proteolytic enzymes are used in the detergent compositions the present invention at a level of 0.0001% to 2%, preferably 0.001% to 0.2%, more preferably 0.005% to 0.1% pure Enzyme, based on the weight of the composition.

The Close enzymes Enzymes selected from cellulases, hemicellulases, peroxidases, glucoamylases, amylases, Xylanases, lipases, phospholipases, esterases, cutinases, pectinases, Keratanases, reductases, oxidases, phenol oxidases, lipoxygenases, Ligninases, pullulanases, tannases, pentosanases, malanases, β-glucanases, Arabinosidases, hyaluronidase, chondroitinase, laccase or mixtures hereof.

A preferred combination is a detergent composition with a Cocktail usable conventionally Enzymes such as protease, amylase, lipase, cutinase and / or cellulase in connection with one or more plant cell wall-degrading Enzymes.

The cellulases usable in the present invention include both bacterial and fungal cellulases. They will preferably have a pH optimum between 5 and 12 and a specific activity above 50 CEVU / mg (cellulose viscosity unit, cellulose viscosity unit). Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al., JP 61078384 and WO96 / 02653, which discloses fungal cellulase made by Humicola insolens, Trichoderma, Thielavia and Sporotrichum, respectively. The EP 739 982 describes cellulases isolated from new Bacillus species. Suitable cellulases are also described in GB-A-2 075 028; GB-A-2 095 275; DE-OS-2 247 832 and WO95 / 26398.

Examples of such cellulases are insolens by a strain of Humicola (Humicola grisea var. Thermoidea), especially the Humicola strain DSM 1800, cellulases produced.

Other suitable cellulases are cellulases from Humicola insolens with a molecular weight of approximately 50 KDa, an isoelectric point of 5.5 and with 415 amino acids; and a ∼43 kD endoglucanase derived from Humicola insolens, DSM 1800, which shows cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. WO 91/17243. Also suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum, described in WO 94/21801; Genencor, published September 29, 1994. Particularly suitable cellulases are the cellulases which have color care advantages. Examples of such cellules sen are the cellulases described in European Patent Application No. 91 202 879.2, filed November 6, 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A / S) are particularly useful; see also WO91 / 17244 and WO91 / 21801. Other suitable cellulases for textile care and / or cleaning properties are described in WO96 / 34092, WO96 / 17994 and WO95 / 24471.

The said cellulases are normally in the detergent composition at levels from 0.0001% to 2% pure enzyme by weight the detergent composition.

Peroxidase enzymes are used in combination with oxygen sources, e.g. B. percarbonate, Perborate, persulfate, hydrogen peroxide, etc., and with a phenolic Substrate as bleach-enhancing molecule used. They are used for "solution bleaching", i.e. H. to prevent transfer from during washing Substrates removed dyes or pigments on other substrates in the washing solution. Peroxidase enzymes are known in the art and include e.g. B. Horseradish peroxidase, ligninase and haloperoxidase, such as chlorine and bromine peroxidase. Peroxidase-containing detergent compositions are described, for example, in the international PCT application WO 89/099813, WO 89/09813 and in European Patent application EP No. 91 202 882.6, filed November 6 1991 and in EP No. 96 870 013.8, filed on February 20 1996. The laccase enzyme is also suitable.

enhancer are generally contained at a level of 0.1 to 5% by weight of the total composition. Preferred enhancers are substituted phenthiazine and phenoxasin, 10-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazine propionic acid (POP) and 10-methylphenoxazine (described in WO 94/12621) and substituted syringates (C3-C5-substituted Alkyl-syringate) and Phenols. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide.

The Peroxidases are usually found in the detergent composition at levels from 0.0001% to 2% pure enzyme by weight the detergent composition.

Other preferred enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for cleaning use include those made by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154 as disclosed in British Patent 1,372,034. Suitable lipases include those made which show a positive immunological cross-reaction with the antibody of the lipase by means of the microorganism Pseudomonas flourescent 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 commercially available lipases include Amano-CES, lipases from Chromobacter viscosum, e.g. B. Chromobacter viscosum var. Lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from US Biochemical Corp., USA, and Disoynth Co., Netherlands, and lipases from Pseudomonas gladioli. Particularly suitable lipases are lipases such as M1-Lipase ^R and Lipomax ^R (Gist-Brocades) and Lipolase ^R and Lipolase Ultra ^R (Novo), which have been found to be very effective when used in combination with the compositions of the present invention become. The lipolytic enzymes described in are also suitable EP 258 068 , WO 92/05249 and WO 95/22615 from Novo Nordisk and in WO 94/03578, WO 95/35381 and WO 96/00292 from Unilever.

Likewise cutinases [EC 3.1.1.50], which are a special Type of lipase can be viewed, namely lipases that do not Interfacial activation require. The addition of Cutina sen to detergent compositions is z. B. in WO-A-88/09367 (Genencor); WO 90/09446 (Plant Genetic System) and WO 94/14963 and WO 94/14964 (Unilever).

The Lipases and / or cutinases are normally used in the detergent composition at levels from 0.0001% to 2% pure enzyme by weight the detergent composition.

Amylases (α and / or β) can be included to remove carbohydrate-based stains. WO94 / 02597, Novo Nordisk A / S, published February 3, 1994, describes detergent compositions containing mutant amylases .; see also WO95 / 10603, Novo Nordisk A / S, published April 20, 1995. Other amylases known for use in detergent compositions include both α- and β-amylases. α-amylases are known in the art and include those disclosed in U.S. Patent No. 5,003,257; EP 252 666 ; WO 91/00353; FR 2 676 456; EP 285 123 ; EP 525 610 ; EP 366 341 and British Patent No. 1,296,839 (Novo). Other suitable amylases are stability-improved amylases, described in WO94 / 18314, published August 18 1994, and WO96 / 05295, Genencor, published February 22, 1996, and amylase variants with additional modification in the immediate parent form, available from Novo Nordisk A / S, disclosed in WO95 / 10603, published April 1995. Also suitable are amylases, which are described in EP 277 216 , WO95 / 26397 and WO96 / 23873 (all from Novo Nordisk).

Examples of commercially available α-amylase products are Purafect Ox Am ^® from Genencor and Termamyl ^® , Ban ^® , Fungamyl ^® and Duramyl ^® , all available from Novo Nordisk A / S Denmark. WO 95/26397 describes other suitable amylases: α-amylases characterized in that it comprises at least 25% higher specific activity than the specific activity of Termamyl ^® at a temperature range of 25 ° C to 55 ° C and at a pH Have a value in the range of 8 to 10, measured by the Phadebas ^® -α-amylase activity assay. Variants of the above enzymes, described in WO 96/23873 (Novo Nordisk), are suitable. Other amylolytic enzymes with improved properties with regard to the activity level and the combination of heat stability and a higher activity level are described in WO95 / 35382.

The amylolytic enzymes are used in the detergent compositions of the present invention at a level of 0.0001% to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme, based on the weight of the composition.

The mentioned above Enzymes can of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. The origin can also mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). purified or unpurified forms of these enzymes can be used. today outcrop it's a common one Practice, wild-type enzymes using protein / genetic engineering techniques to modify their performance efficiency in the detergent compositions optimize the invention. For example, the variants can be designed this way be that the compatibility of the enzyme with frequently found components of such compositions is increased. Alternatively, the variant can be designed so that the optimal pH, bleaching or chelating stability, catalytic activity and the like tailored to the enzyme variant in order to meet the respective cleaning application.

In particular in the case of bleach instability, attention should be focused on amino acids, which are sensitive to Oxidation are, and on the surface charges, for surfactant compatibility. The isoelectric Such enzymes can be charged by substitution of some charged amino acids be modified, e.g. B. can increase the isoelectric point help maintain compatibility with to improve anionic surfactants. The stability of the enzymes can also be determined by the generation z. B. additional salt bridges and the reinforcement of calcium binding sites to increase chelating stability be enlarged. Special attention must be paid to the Cellulases are dedicated as most of the cellulases are separate binding domains (CBD). The properties of such enzymes can by Modifications in these domains changed become.

The Enzymes are usually included in the detergent compositions Levels of 0.0001% to 2% active enzyme by weight the detergent composition. The enzymes can be used as separate individual components (prills, granules, stabilized liquids etc. containing an enzyme) or as mixtures of two or more Enzymes (e.g. co-granules) can be added.

Other suitable detergent ingredients that can be added are enzyme oxidation eliminators, which are described in copending European patent application EP 92 870 018.6 , filed January 31, 1992. Examples of such enzyme oxidation removers are ethoxylated tetraethylene polyamines.

A number of enzyme materials and agents for their incorporation in synthetic detergent compositions are also disclosed in WO 9307263 A and WO 9307260 A from Genencor International, WO 8908694 A from Novo and US 3,553,139, January 5, 1971 from McCarty et al. Enzymes are further disclosed in U.S. 4,101,457, Place et al., July 18, 1978, and in U.S. 4,507,219, Hughes, March 26, 1985. Enzyme materials useful for liquid detergent formulations and their incorporation into such formulations are disclosed in U.S. 4 261,868, Hora et al., April 14, 1981. Enzymes for use in detergents can be stabilized by various techniques. Enzyme stabilization techniques are disclosed and exemplified in US 3,600,319, August 17, 1971, Gedge et al., EP 199 405 and EP 200 586, 29 , October 1986, Venegas. Enzyme stabilization systems are also described, for example, in US 3,519,570. A usable Bacillus, sp.AC13, which gives proteases, xylanases and cellulases, is described in US Pat WO 9401532 A from Novo.

Color care and textile care benefits

technologies, which provide a type of color care benefit can also be included. Examples of these technologies are metallocatalysts for color retention. Such metallocatalysts are used in the pending at the same time European Patent Application No. 92 870 181.2. Dye-fixing agent, Anti-wrinkle polyolefin dispersant for improved water absorbency, Fragrance and amino-functional polymer (PCT / US97 / 16546) for color care treatment and perfume adhesiveness are other examples of color care / textile care technologies, which is also pending Patent Application No. 96 870 140.9, filed November 7, 1996, are described.

Also Textile plasticizers can in detergent compositions according to the present invention be involved. These agents can be of inorganic or be organic type. Inorganic plasticizers are made by the smectite clays disclosed in GB-A-1,400,898 and USP 5,019,292 exemplified. Organic fabric softeners conclude the water-insoluble tertiary Amines as disclosed in GB-A-1 514 276 and EP-B-0 011 340, and their combination with mono-C12-C14 quaternary ammonium salts is described in EP-B-0 026 527 and EP-B-0 026 528, and double-chain amides, as in EP-B-0 242 919. Other useful organic components of fabric softening systems conclude High molecular weight polyethylene oxide materials as described in EP-A-0 299 575 and 0 313 146.

shares smectite clay is normally in the range of 2 to 20% by weight, more preferably 5 to 15% by weight, the material being a dry mixed component is added to the rest of the formulation. Organic fabric softening agents, such as the water-insoluble ones tertiary Amines, or double-chain amide materials, are used in proportions from 0.5 to 5% by weight, usually from 1 to 3% by weight, while the High molecular weight polyethylene oxide materials and the water-soluble cationic materials at levels of 0.1 to 2% by weight, normally from 0.15 to 1.5% by weight can be added. These materials will be usually the spray dried Proportion of composition added, although in some cases it may be more appropriate can add them as a dry mixed particulate, or it as a molten liquid spray on the other solid components of the composition.

bleach

In addition to Percarbonate can be the composition of the present invention optionally include other bleaching agents, such as bleach activators, light activated bleach, bleaching species producing enzyme and Bleach catalysts.

alternative Sources of available Oxygen includes percarboxylic acid bleach and salts thereof. Suitable examples of this class of agents conclude Magnesium monoperoxyphthalate hexahydrate, the magnesium salt of metachloroperbenzoic acid, 4-nonylamino-4-oxoperoxybutyric acid and diperoxydodecanedioc on. Such bleaching agents are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740 446, the European Patent Application 0 133 354 and U.S. Patent 4,412,934.

strongly close preferred bleaches also 6-nonylamino-6-oxoperoxycaproic acid, as described in U.S. Patent 4,634,551.

A another category of bleaching agents that can be used contains the halogen bleach. Examples of hypohalite bleaches conclude for example trichloroisocyanuric acid and the sodium and potassium dichloroisocyanurates and N-chloro and N-bromoalkanesulfonamides. Such materials are usually at 0.5-10 % By weight of the finished product, preferably 1-5% by weight added.

worin R₁ eine lineare oder verzweigtkettige gesättigte oder ungesättigte C₇-C₁₃-Alkylgruppe ist, R₂ eine lineare oder verzweigtkettige gesättigte oder ungesättigte C₁-C₈-Alkylgruppe ist und R₃ eine lineare oder verzweigtkettige gesättigte oder ungesättigte C₁-C₄-Alkylgruppe ist.The hydrogen peroxide releasing agents can be used in combination with bleach activators, such as tetraacetylethylene diamine (TAED), nonanoyloxybenzenesulfonate (NOBS, described in US 4,412,934 ), 3,5-trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120 591 ) or pentaacetyl glucose (PAG) or phenolsulfonate ester of N-nonanoyl-6-aminocaproic acid (NACA-OBS, described in WO 94/28106), which are perhydrolyzed to form a peracid as the active bleaching species, resulting in an improved bleaching effect. Also suitable activators are acylated citrate esters, as disclosed in co-pending European Patent Application No. 91 870 207.7, and unsymmetrical acyclic imide bleach activators of the following formula, as described in the appendices Pending patent applications by Procter & Gamble of US serial number 60 / 022,786 (filed July 30, 1996) and number 60 / 028,122 (filed October 15, 1996):

wherein R _{1 is} a linear or branched chain saturated or unsaturated C ₇ -C ₁₃ alkyl group, R _{2 is} a linear or branched chain saturated or unsaturated C ₁ -C ₈ alkyl group and R _{3 is} a linear or branched chain saturated or unsaturated C ₁ -C ₄ alkyl group.

helpful Bleach, including peroxyacids and bleaching systems, including bleach activators and peroxygen bleach compounds, for use in detergent compositions according to the invention are described in our pending at the same time Applications USSN 08 / 136,626, PCT / US95 / 07823, WO 95/27772, WO 95/27773, WO 95/27774 and WO 95/27775 are described.

The Hydrogen peroxide can also be added by adding an enzymatic system (i.e. an enzyme and its substrate), which is able to hydrogen peroxide at the beginning or during the Washing and / or rinsing process to create. Such enzymatic systems are in EP patent application 91 202 655.6, filed October 9, 1991.

Metal-containing catalysts for use in bleaching compositions include cobalt-containing catalysts such as pentaamine acetate cobalt (III) salts 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 peroxygen compound, a gan containing bleach activator and a chelating agent is described in Patent Application No. 94 870 206.3.

Of Different bleaches are also available known in the field and can be used herein. A type of non-oxygen bleach of particular interest includes light activated ones Bleaching agents, such as the sulfonated zinc and / or aluminum phthalocyanines, on. These materials can while of the washing process are deposited on the substrate. When irradiated with light in the presence of oxygen, such as when hanging from Clothes to dry in daylight, the sulfonated zinc phthalocyanine activated and consequently the substrate is bleached. A favorite Zinc phthalocyanine and a light activated bleaching process in U.S. Patent 4,033,718. Typically, detergent compositions approximately 0.025 to approximately Contain 1.25% by weight of sulfonated zinc phthalocyanine.

system Builder

The Compositions according to the present Invention can further include a builder system. Any conventional builder system is Suitable for use herein, including aluminosilicate materials, Silicates, polycarboxylates, alkyl or alkenyl succinic acids and fatty acids, Materials such as ethylenediaminetetraacetate, diethylenetriaminepentamethylene acetate, Metal ion masking agents such as aminopolyphosphonates, in particular Ethylenediaminetetramethylenephosphonic acid and diethylenetriaminepentamethylenephosphonic acid. phosphate builder can can also be used herein.

suitable Builders can an inorganic ion exchange material, often an inorganic hydrated one Aluminum silicate material, especially a hydrated synthetic Zeolite, such as hydrated zeolite A, X, B, HS or MAP.

Another suitable inorganic builder material is layered silicate, e.g. B. SKS-6 (Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na ₂ Si ₂ O ₅ ).

Suitable carboxylates having a carboxyl group include lactic acid, glycolic acid and ether derivatives thereof, as described in Belgian Patent Nos. 831,368, 821,369 and 821,370. Potycarboxylates with two carboxyl groups include the water-soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, maleic acid, diglycolic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates, which are described in German Offenlegungsschrift 2,446,686 and 2,446,687 and the US patent No. 3 935 257 and the sulfinyl carboxylates described in Belgian Patent No. 840 623. Polycarboxylates with three carboxyl groups include, in particular, water soluble citrates, aconitrates and citraconates, as well as succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1,379,241, lactoxysuccinates described in Dutch application 7205873 and the oxypolycarboxylate materials such as 2- Oxa-1,1,3-propane tricarboxylates described in British Patent No. 1,387,447.

polycarboxylates close with four carboxy groups Oxydisuccinates, disclosed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates, 1,1,3,3-propane tetracarboxylates and 1,1,2,3-propane tetracarboxylates. Polycarboxylates with sulfo substituents include the sulfosuccinate derivatives, which are disclosed in British Patent Nos. 1,396,421 and 1,398,422 and in U.S. Patent No. 3,936,448 and the sulfonated pyrolyzed Citrates described in British Patent No. 1,082,179 a while Polycarboxylates with phosphonic substituents in British Patent No. 1,439,000 are described.

alicyclic and heterocyclic polycarboxylates include cyclopentane cis, cis, cis tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydrofuran-cis, cis, cis-tetracarboxylate, 2,5-tetrahydrofuran-cis-dicarboxylate, 2,2,5,5-tetrahydrofuran tetracarboxylates, 1,2,3,4,5,6-hexane hexacarboxylates and carboxymethyl derivatives of polyhydric alcohols, such as sorbitol, Mannitol and xylitol, a. Aromatic polycarboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No. 1,425,343 on.

Of the above, the preferred polycarboxylates are hydroxycarboxylates with up to three carboxy groups per molecule, especially citrates.

preferred Builder systems for use in the present compositions conclude a mixture of a water-insoluble Aluminum silicate builders, such as zeolite A, or a layered silicate (SKS-6) and a water-soluble Carboxylate chelating agents such as citric acid. Other preferred Close builder systems a mixture of a water-insoluble Aluminum silicate builders such as Zeolite A and a water soluble Carboxylate chelating agents such as citric acid. Preferred builder systems for use in liquid Detergent compositions of the present invention are soaps and polycarboxylates.

Other Builder materials that are part of the builder system for use in granular Can form compositions conclude inorganic materials, such as alkali metal carbonates, bicarbonates, silicates, and organic materials such as the organic phosphonates, aminopolyallcylene phosphonates and aminopolycarboxylates. Other suitable water soluble organic Salts are the homo- or copolymeric acids or their salts in which the polycarboxylic acid comprises at least two carboxyl radicals which are separated from one another no more than two carbon atoms are separated. Polymers this Types are disclosed in GB-A-1 596 756. Examples of such Salts are polyacrylates with a MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of 20,000 to 70,000, in particular about 40,000.

Detergent builder salts are normally in amounts of 5 to 80 wt .-% of the composition preferably 10 to 70% by weight and most usually 30 to 60% by weight locked in.

chelating agents

The Detergent compositions described herein may optionally be used also contain one or more iron or manganese chelating agents. Such chelating agents can chosen are selected from the group consisting of aminocarboxylates, aminophosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures thereof, as all defined hereinafter are. Without you wants to be tied to a theory it is believed that the Benefits of these materials are due in part to their exceptional ability to iron and manganese ions through formation of soluble Chelates from washing solutions to remove.

As optional chelating agents include ethylenediaminetetracetates Amino carboxylates, N-hydroxyethylethylenediaminetriacetates, nitrilotriacetates, ethylenediamine tetraproprionates, triethylenetetraaminehexaacetates, diethylenetriaminepentaacetates, and ethanoldiglycines, alkali metal, ammonium and substituted ammonium salts thereof and mixtures thereof. Aminophosphonates are also suitable for use as chelating agents in the compositions of the invention when at least low levels of Total phosphorus is allowed in the detergent compositions and include ethylenediaminetetrakis (methylenephosphonates) such as DEQUEST. These aminophosphonates preferably contain no alkyl or alkenyl groups with more than 6 carbon atoms. Polyfunctionally-substituted aromatic chelating agents are also applicable in the compositions described herein; see that on May 21, 1974 to Connor et al. issued U.S. Patent 3,812,044. Preferred compounds of this type in acid form are dihydroxydisulfobenzenes, such as 1,2-dihydroxy-3,5-disulfobenzene.

On preferred, biodegradable chelating agent for use herein is ethylenediamine disuccinate ("EDDS"), especially the [S, S] isomer as described in U.S. Patent 4 704,233, November 3, 1987, by Hartman and Perkins.

The Compositions described herein may also include water-soluble methylglycinediacetic acid (MGDA) salts (or the acid form) contain as a chelating agent or a co-builder, for example useful with insoluble Builders such as zeolites, layered silicates and the like.

Provided used, these chelating agents are generally about 0.1 to approximately 15% by weight of the detergent compositions described herein. Further preferred are the chelating agents, if used, approximately 0.1 to approximately Make up 3.0% by weight of such compositions.

Suds suppressors

On another optional component is a foam suppressor, exemplified through silicones and silica-silicone mixtures. Silicones can generally represented are made by alkylated polysiloxane materials, while silica usually is used in finely divided forms, exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. This Materials can be introduced as particulates in which the foam suppressant is advantageously releasable in a water soluble or water-dispersible, essentially non-surface-active, Detergent-impermeable Carrier introduced is. Alternatively, the foam suppressor can be dissolved in a liquid carrier or be dispersed and by spraying on one or more of the other components can be applied. A preferred silicone foam suppressant is disclosed in Bartollota et al., U.S. Patent 3,933,672. Others particularly useful Suds suppressors are the self-emulsifying silicone foam suppressors published in German patent application DTOS 2 646 126 on April 28, 1977. An example of such a connection is DC-544, available in the stores from Dow Corning, which is a siloxane / glycol copolymer. Especially preferred antifoam consist in the foam suppression system, comprising a mixture of silicone oils and 2-alkyl alkanols. Suitable 2-allylalkanols are 2-butyloctanol, which is commercially available under the trade name Isofol 12 R. is. Such foam suppression systems are described in the co-pending European patent application No. 92 870 174.7, filed November 10, 1992.

Particularly preferred foam suppressants are described in copending European Patent Application No. 92 201 649.8. The compositions can comprise a silicone-silica mixture in combination with non-porous fumed silica such as Aerosil ^R.

The Foam suppressors described above are typically used in Mirror from 0.001 to 2% by weight of the composition, preferably 0.01 to 1 wt .-% used.

additional

It can further components used in detergent compositions such as dirt suspending agents, dirt repellants, optical Brighteners, abrasives, bactericides, tarnish preventers, colorants and / or encapsulated or non-encapsulated fragrances.

Particularly suitable encapsulating materials are water soluble capsules consisting of a matrix of polysaccharide and polyhydroxy compounds as described in GB 1 464 616. Other suitable water soluble encapsulating materials include dextrins derived from ungelatinized starch esters of substituted dicarboxylic acids as described in US 3,455,838 , These acid ester dextrins are preferably made from starches such as waxy corn, waxy sorghum, sago, tapioca and potato. Suitable examples of such encapsulating materials include N-Lok manufactured by National Starch. The encapsulating material N-Lok consists of a modified maize starch and gluco se. The starch is modified by the addition of monofunctionally substituted groups, such as octenyl succinic anhydride.

Here in suitable anti-redeposition and soil suspending agents include cellulose derivatives such as Methyl cellulose, carboxymethyl cellulose and hydroxyethyl cellulose, and homo- or copolymeric polycarboxylic acids or their salts. polymers of this type close the polyacrylates and maleic anhydride-acrylic acid copolymers, who previously mentioned as a builder were, and copolymer of maleic anhydride with ethylene, methyl vinyl ether or methacrylic acid a, the maleic anhydride accounts for at least 20 mole percent of the copolymer. These materials are usually at levels from 0.5 to 10 wt .-%, further preferably 0.75 to 8% by weight, most preferably 1 to 6% by weight of the composition used.

Preferred optical brighteners are of anionic character, examples of which are disodium 4,4'-bis- (2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, disodium 4, 4'-bis- (2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, disodium 4,4'-bis- (2,4-dianilino-s-triazine -6-ylamino) stilbene-2,2'-disulfonate, monosodium 4 ', 4 "-bis- (2,4-dianilino-s-triazin-6-ylamino) stilbene-2-sulfonate, disodium-4,4 '-bis- (2-anilino-4- (N-methyl-N-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene 2: 2'-disulfonate, disodium 4,4'-bis- ( 4-phenyl-2,1,3-triazol-2-yl} -stilbene-2: 2'-disulfonate, disodium 4,4'bis- (2-anilino-4- (1-methyl-2-hydroxyethylamino) -s-triazin-6-ylamino) stilbene 2: 2'-disulfonate, sodium 2 (stilbyl-4 "- (naphtho-1 ', 2': 4.5) -1,2,3-triazole-2 "-sulphonate and 4,4'-bis (2-sulfostyryl) biphenyl. Highly preferred brighteners are the specific brighteners disclosed in EP 753 567 ,

Other useful polymeric materials are the polyethylene glycols, especially those with a molecular weight of 1000-10000, more precisely 2000 up to 8000 and strongest preferably about 4000. These are at levels of 0.20 to 5 wt .-%, more preferably 0.25 to 2.5 wt .-% used. These polymers and the earlier mentioned Homo- or copolymeric polycarboxylate salts can be used for improvement whiteness retention, the textile ash deposit and the cleaning performance compared to clay, proteinaceous and oxidizable soiling in the presence of transition metal impurities.

Soil repellants useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and / or propylene glycol units in various arrangements. Examples of such polymers are disclosed in commonly assigned U.S. Patent Nos. 4,116,885 and 4,711,730 and published European Patent Application No. 0 272 033. A particularly preferred polymer according to EP-A-0 272 033 has the formula (CH ₃ (PEG) ₄₃ ) _0.75 (POH) _0.25 [T-PO) _2.8 (T-PEG) _0.4 ] T (PO-H) _0.25 ((PEG) ₄₃ CH ₃ ) _0.75 wherein PEG is - (OC ₂ H ₄ ) O-, PO is (OC ₃ H ₆ O) and T is (pcOC ₆ H ₄ CO).

Likewise very helpful are modified polyesters such as statistical copolymers of dimethyl terephthalate, Dimethyl sulfoisophthalate, ethylene glycol and 1,2-propanediol, where the end groups predominantly from sulfobenzoate and secondarily from monoesters of ethylene glycol and / or propanediol. The goal is one "predominantly" with sulfobenzoate groups at both ends to obtain capped polymer, the in the present context most of the copolymers herein end-capped by sulfobenzoate groups will be. However, some copolymers are less than completely capped and that’s why their end groups from monoesters of ethylene glycol and / or propane-1,2-diol exist, thus "secondary" from such species consist.

The chosen here Polyesters contain about 46% by weight dimethyl terephthalic acid, about 16% by weight propane-1,2-diol, about 10% by weight ethylene glycol, about 13 % By weight of dimethylsulfobenzoic acid and about 15% by weight sulfoisophthalic acid and have a molecular weight of about 3000. The polyesters and their manufacturing process in detail in EPA 311 342.

in the It is well known in the art that free chlorine in tap water the enzymes contained in detergent compositions quickly deactivated. Therefore, the use of chlorine scavengers such as perborate Ammonium sulfate, sodium sulfite or polyethyleneimine, at a level above of 0.1% by weight Overall composition in the formulas improved stability of detergent enzymes while of the washing process. Compositions comprising chlorine scavengers, are in the European patent application 92 870 018.6, filed January 31, 1992.

Alkoxylated polycarboxylates, such as those made from polyacrylates, are useful herein to provide additional fat removal performance. Such materials are described in WO 91/08281 and PCT 90/01815 on page 4f, incorporated herein by reference. Chemically, these materials include polyacrylates with an ethoxy side chain every 7-8 acrylate units. The side chains have the formula - (CH ₂ CH ₂ O) _m (CH ₂ ) _n CH ₃ , where m is 2-3 and n is 6-12. The side chains are ester linked to the polyacrylate "backbone", thereby providing a "comb" polymer type structure. Molecular weight can vary, but is typically in the range of about 2,000 to about 50,000. Such alkoxylated polycarboxylates can make up about 0.05 to about 10% by weight of the compositions described herein.

dispersants

The Detergent compositions of the present invention can also Contain dispersants. Suitable water-soluble organic salts are the homo- or copolymeric acids or their salts, the polycarboxylic acid having at least two carboxyl radicals which comprises one another by no more than two carbon atoms are separated. Polymers of this type are disclosed in GB-A-1 596 756. Examples of such salts are polyacrylates with a molecular weight from 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of 1000 to 100000 exhibit. In particular, a copolymer of acrylate and methyl acrylate, like the 480N with a molecular weight of 4000, with a mirror from 0.5-20 % By weight of the composition in the detergent compositions of the present invention can be added.

The Compositions of the invention can include a lime soap peptizer compound contain, which preferably have a lime soap dispersing capacity (LSDP), as defined hereinafter, not more than 8, preferably no more than 7, strongest preferably has no more than 6. The lime soap peptizer compound is preferably present at a level of 0 to 20% by weight.

A numerical measure of the effectiveness of a lime soap peptizer is given by the lime soap dispersibility (LSDP), which is determined using the lime soap dispersant test as described in an article by HC Borghetty and CA Bergman, J. Am. Oil. Chem. Soc., Vol. 27, pages 68-90, (1950). This lime soap dispersion test method is widely used by practitioners in the art and is referred to, for example, in the following review articles; WN Linfield, Surfactant Science Series, volume 7, page 3; WN Linfield, surfactants surf. det., vol. 27, pages 159-163, (1990); and MK Nagarajan, WF Masler; Cosmetics and Toiletries, vol. 104, pages 71-73 (1989). The LSDP is the weight percent ratio of dispersant to sodium oleate required to disperse the lime soap deposits formed from 0.025 g sodium oleate in 30 ml water of 333 ppm CaCO ₃ (Ca: Mg = 3: 2) equivalent hardness ,

surfactants with good lime soap peptizing ability certain amine oxides, Betaines, sulfobetaines, alkyl ethoxy sulfates and ethoxylated alcohols lock in.

Exemplary surfactants with an LSDP of no more than 8 for use in accordance with the present invention include C ₁₆ -C ₁₈ dimethylamine oxide, C ₁₂ -C ₁₈ alkyl ethoxy sulfates having an average degree of ethoxylation of 1-5, especially C ₁₂ -C ₁₅ alkyl ethoxy sulfate surfactant a degree of ethoxylation of about 3 (LSDP = 4) and the ethoxylated C ₁₄ -C ₁₅ alcohols with an average degree of ethoxylation of either 12 (LSDP = 6) or 30, sold under the trade names Lutensol A012 or Lutensol A030 by BASF GmbH ,

to Polymeric lime soap peptizers suitable for use herein in the article by M.K. Nagarajan, W.F. Masler described which one found in Cosmetics and Toiletries, volume 104, pages 71-73 (1989).

hydrophobic Bleaching agents such as 4- [N-octanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-nonanoyl-6-aminohexanoyl] benzenesulfonate, 4- [N-decanoyl-6-aminohexanoyl] benzenesulfonate and mixtures thereof; and nonanoyloxybenzenesulfonate together with Hydrophilic / hydrophobic bleach formulations can also be used as lime soap peptizer compounds be used.

Inhibition of dye transfer

The detergent compositions of the present invention can also contain compounds for Inhi Include dye transfer from solubilized and suspended dyes found in textile laundering involving colored textiles from one textile to another.

Polymeric dye transfer inhibiting medium

The Detergent compositions described herein can also 0.001 to 10% by weight, preferably 0.01 to 2% by weight, more preferably 0.05 to 1% by weight of polymeric dye transfer inhibiting agents include. The polymeric dye transfer inhibiting agents are usually incorporated into detergent compositions around the transfer of dyes from dyed textiles to it together inhibit washed textiles. These polymers have the Ability, the colored ones Textiles washed out volatile Dyes complex or adsorb before the dyes Have an opportunity to be tied to other items in your laundry to become. Particularly suitable polymeric dye transfer inhibiting Agents are polyamine-N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof. The addition of such Polymers reinforced also the performance of the enzymes according to the invention.

a) Polyamine N-oxide polymers

worin P eine polymerisierbare Einheit ist, auf welche die R-N-O-Gruppe gebunden werden kann oder wobei die R-N-O-Gruppe einen Teil der polymerisierbaren Einheit bildet, oder eine Kombination von beiden.The polyamine-N-oxide polymers suitable for use herein contain units having the following structural formula:

wherein P is a polymerizable unit to which the RNO group can be attached or where the RNO group forms part of the polymerizable unit, or a combination of both.

R stands for aliphatic, ethoxylated aliphatic, aromatic, heterocyclic or alicyclic groups or any combination of what the nitrogen of the N-O group can be attached, or wherein the nitrogen of the N-O group is part of these groups.

worin R1, R2 und R3 aliphatische Gruppen, aromatische, heterocyclische oder alicyclische Gruppen oder Kombinationen hiervon sind, x oder/und y oder/und z 0 oder 1 ist, und worin der Stickstoff der N-O-Gruppe angebunden sein kann oder worin der Stickstoff der N-O-Gruppe einen Teil dieser Gruppen bildet.The NO group can be represented by the following general structures:

wherein R1, R2 and R3 are aliphatic groups, aromatic, heterocyclic or alicyclic groups or combinations thereof, x or / and y or / and z is 0 or 1, and wherein the nitrogen of the NO group can be attached or wherein the nitrogen of the NO group forms part of these groups.

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

Other Suitable polyamine N-oxides are the polyamine oxides to which the N-O group is bound to the polymerizable unit. A preferred one The class of these polyamine N-oxides are the polyamine N-oxides with the general formula (I), wherein R is an aromatic, heterocyclic or alicyclic group, wherein the nitrogen of the functional N-O group is part of the R group. Examples of these classes are Polyamine oxides, wherein R is a heterocyclic compound, such as Pyridine, pyrrole, imidazole and derivatives thereof. Another preferred Class of polyamine N-oxides are the polyamine oxides with the general formula (I) where R is aromatic, heterocyclic or alicyclic groups, wherein the nitrogen of the functional N-O group is bound to the R groups is. Examples of these classes are polyamine oxides, where R groups can be aromatic like phenyl.

It can build any polymer backbone can be used as long as the amine oxide polymer formed is water-soluble and has dye transfer inhibiting properties. Examples of suitable primary backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, Polyacrylates and mixtures thereof.

The Amine N-oxide polymers of the present invention typically have a relationship from amine to amine N-oxide from 10: 1 to 1: 1,000,000. However can be the amount of amine oxide groups present in the polyamine oxide polymer by appropriate copolymerization or by an appropriate Extent of N oxidation can be varied. The ratio of amine to amine N-oxide is preferably from 2: 3 to 1: 1,000,000. More preferably from 1: 4 to 1: 1,000 000, the strongest preferably from 1: 7 to 1: 1,000,000. The polymers of the present Invention actually include random or block copolymers if one type of monomer is an amine N-oxide and the other type of monomer is either an amine N-oxide or Not. The amine oxide unit of the polyamine N-oxides has a pKa <10, preferably pKa <7, further preferably pKa <6. Die Polyamine oxides can can be obtained at almost any degree of polymerization. The degree of polymerization is not critical, provided the material has the desired water solubility and dye suspending assets. Typically the average molecular weight is within in the range of 500 to 1,000,000; preferably 1000 to 50000, more preferably 2,000 to 30,000, most preferably 3,000 to 20,000.

b) Copolymers of N-vinyl pyrrolidone and N-vinylimidazole

The N-vinylimidazole-N-vinylpyrrolidone polymers used in the present invention have a preferred average molecular weight range from 5,000 to 1,000 000, preferably 5000-200000. Herein for use in detergent compositions according to the present Polymers preferred by the invention comprise a polymer selected from N-vinylimidazole-N-vinylpyrrolidone copolymers, the polymer being a average molecular weight range from 5000 to 50,000, more preferably 8000 to 30,000, most preferably 10,000 to 20000. The average molecular weight range was determined by light scattering as described in Barth, H.G., and Mays, J.W., Chemical Analysis., Vol. 113, "Modern Methods of Polymer Characterization". Strongly preferred N-vinylimidazole-N-vinylpyrrolidone copolymers have an average Molecular weight range from 5000 to 50,000, more preferably from 8000 to 30000. strongest preferably 10,000 to 20,000.

The characterized by having this molecular weight range N-vinylimidazole N-vinylpyrrolidone copolymers see excellent dye transfer inhibiting properties before while the cleaning performance of detergent compositions formulated with it not adversely affect. The N-vinylimidazole-N-vinylpyrrolidone copolymer The present invention has a molar ratio of N-vinylimidazole to N-vinyl pyrrolidone from 1 to 0.2, more preferably 0.8 to 0.3, am most preferably 0.6 to 0.4.

c) polyvinyl pyrrolidone

The detergent compositions of the present invention may also use polyvinyl pyrrolidone ("PVP") having an average molecular weight of from about 2500 to about 400,000, preferably from about 5000 to about 200,000, more preferably from about 5000 to about 50,000, and most preferably from about 5000 to about 15000. Suitable polyvinylpyrrolidones are commercially available from ISP Corporation, New York, NY, and Montreal, Canada, under the product names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K-60 (average molecular weight 160,000) and PVP K-90 (average molecular weight 360,000). Other suitable polyvinylpyrrolidones that are commercially available from BASF Corporation include Sokalan HP 165 and Sokalan HP 12; Polyvinylpyrrolidones which are known to those skilled in the detergent field (see for example EP-A-262 897 and FP-A-256 696).

d) polyvinyl oxazolidone

The Detergent compositions of the present invention can also Polyvinyloxazolidone as a polymeric dye transfer inhibiting Use funds. The polyvinyloxazolidones have a medium Molecular weight of approximately 2,500 to about 400,000, preferably approximately 5000 to about 200,000, more preferably approximately 5000 to about 50,000 and the strongest preferably approximately 5000 to about 15,000.

e) polyvinylimidazole

The Detergent compositions of the present invention can also Polyvinylimidazole as a polymeric dye transfer inhibiting Use funds. The polyvinylimidazoles preferably have an average Molecular weight of approximately 2,500 to about 400,000, preferably approximately 5000 to about 200,000, more preferably approximately 5000 to about 50,000 and the strongest preferably approximately 5000 to about 15,000.

f) crosslinked polymers:

networked Polymers are polymers whose basic structure is linked to a certain extent; these ties can be chemical or physical in nature, possibly with active groups in the basic structure or on the branches; Crosslinked polymers are in the Journal of Polymer Science, volume 22, pages 1035-1039. In one embodiment the crosslinked polymers are made in such a way that she form a three-dimensional rigid structure, which dyes capture in the pores formed by the three-dimensional structure can. In another embodiment the cross-linked polymers capture the dyes by swelling. Such cross-linked polymers are described in the same pending Patent application 94 870 213.9.

Washing method

The Compositions of the invention can be in essentially any Washing or cleaning processes are used, including soaking processes, Pretreatment procedures and procedures with rinsing steps, for which a separate rinse aid composition can be added.

The The method described herein involves contacting textiles or dishes with a cleaning solution in the usual way and is exemplified hereinafter.

The The method of the invention is advantageously used in the course of the cleaning process executed. The cleaning process is preferably carried out at 5 ° C to 95 ° C, especially between 10 ° C and 60 ° C. The pH of the treatment solution is preferably from 7 to 12.

On preferred automatic dishwashing process comprises treating dirty objects with an aqueous liquid, in which an effective amount of the composition for machine Wash the dishes or rinsing solved or is distributed. A conventional one effective amount of machine dishwashing composition 8-60 g Product, solved or dispersed in a wash volume of 3-10 liters. According to one manual dishwashing process dirty dishes with an effective amount of dishwashing composition, typically 0.5-20 g (per 25 treated dishes) contacted. Preferred manual dishwashing methods include those Apply a concentrated solution on the surfaces of dishes or soaking in a large volume of dilute solution Detergent composition.

The following examples are intended compositions of the present invention illustrate, but are not necessarily intended to to limit or otherwise define the scope of the invention.

LAS

Lineares Natrium-C_11-13-Alkybenzolsufonat.

TAS

Natriumtalgalkylsulfat.

CxyAS

Natrium-C_1x C_1y-Alkylsulfat.

CxySAS

Natrium-C_1x C_1y-sekundäres (2,3)-Alkylsulfat.

CxyEz

vorwiegend linearer primärer C_1x-C_1y-Alkohol, kondensiert mit einem Durchschnitt von z Mol Ethylenoxid.

CxyEzS

Natrium-C_1x C_1y-Alkylsulfat, kondensiert mit einem Durchschnitt von z Mol Ethylenoxid.

QAS

R₂.N⁺(CH₃)₂(C₂H₄OH) mit R₂ = C₁₂–C₁₄.

QAS1

R₂.N⁺(CH₃)₂(C₂H₄OH) mit R₂ = C₈-C₁₁

APA

C_8–10-Amidopropyldimethylamin.

Seife

Lineares Natriumalkylcarboxylat, abgeleitet aus einer 80/20-Mischung von Talg- und Kokosnußfettsäuren.

nichtionisch

gemischter ethoxylierter/propoxylierter C₁₃-C₁₅-Fettalkohol mit einem durchschnittlichen Grad an Ethoxylierung von 3,8 und einem durchschnittlichen Grad an Propoxylierung von 4,5.

Neodol 45–13

lineares primäres C₁₄-C₁₅-Alkoholethoxylat, vertrieben von Shell Chemical Co.

STS

Natriumtoluolsulfonat.

CFAA

C₁₂-C₁₄-Alkyl-N-methylglucamid.

TFAA

C₁₆-C₁₈-Alkyl-N-methylglucamid.

TPKF

A getoppte Gesamtschnitt-C₁₂-C₁₄-Fettsäuren.

Silicat

Amorphes Natriumsilicat (SiO₂:Na₂O-Verhältnis = 1,6–3,2).

Metasilicat

Natriumsilicat (SiO₂:Na₂O-Verhältnis = 1,0).

Zeolith A

Hydratisiertes Natriumaluminiumsilicat der Formel Na₁₂(AlO₂SiO₂)₁₂27H₂O mit einer primären Teilchengröße im Bereich von 0,1 bis 10 Mikrometer (Gewicht ausgedrückt auf wasserfreier Basis).

Na-SKS-6

kristallines Schichtsilicat der Formel δ-Na₂Si₂O₅.

Citrat

Trinatriumcitratdihydrat einer Aktivität von 86,4 % mit einer Teilchengrößenverteilung zwischen 425 und 850 Mikrometer.

Zitronensäure

Wasserfreie Zitronensäure.

Borat

Natriumborat

Carbonat

Wasserfreies Natriumcarbonat mit einer Teilchengröße zwischen 200 und 900 Mikrometer.

Bicarbonat

Wasserfreies Natriumhydrogencarbonat mit einer Teilchengrößenverteilung zwischen 400 und 1200 Mikrometer.

Sulfat

Wasserfreies Natriumsulfat.

Mg-Sulfat

Wasserfreies Magnesiumsulfat.

STPP

Natriumtripolyphosphat.

TSPP

Tetranatriumpyrophosphat.

MA/AA

statistisches Copolymer von 4:1 Acrylat/Maleat, durchschnittliches Molekulargewicht etwa 70000–80000.

MA/AA 1

statistisches Copolymer von 6:4 Acrylat/Maleat, durchschnittliches Molekulargewicht etwa 10000.

AA

Natriumpolyacrylat-Polymer mit einem durchschnittlichem Molekulargewicht 4500.

PA30

Polyacrylsäure mit einem durchschnittlichem Molekulargewicht zwischen etwa 4500 – 8000.

480N

statistisches Copolymer von 7:3 Acrylat/Methacrylat, durchschnittliches Molekulargewicht etwa 3500.

Polygel/Carbopol:

hochmolekulargewichtige vernetzte Polyacrylate.

PB1

Wasserfreies Natriumperborat-Monohydrat der nominalen Formel NaBO₂.H₂O₂.

PB4

Natriumperborat-tetrahydrat der nominalen Formel NaBO₂.3H₂O.H₂O₂.

Percarbonat

Wasserfreies Natriumpercarbonat der nominalen Formel 2 Na₂CO₃.3H₂O₂.

NaDCC

Natriumdichlorisocyanurat.

TAED

Tetraacetylethylendiamin.

NOBS

Nonanoyloxybenzolsulfonat in der Form des Natriumsalzes.

NACA-OBS

(6-Nonamidocaproyl)oxybenzolsulfonat.

DTPA

Diethylentriaminpentaessigsäure.

HEDP

1,1-Hydroxyethandiphosphonsäure.

DETPMP

Diethylentriaminpenta(methylen)phosphonat, vertrieben von Monsanto unter dem Handelsnamen Dequest 2060.

EDDS

Ethylendiamin-N,N'-dibernsteinsäure, (S,S)-Isomer in der Form seines Natriumsalzes.

MnTACN

Mangan-1,4,7-trimethyl-1,4,7-triazacyclononan.

photoaktiviertes Bleichmittel

sulfoniertes Zinkphthalocyanin, eingekapselt in Dextrin-löslichem Polymer.

photoaktiviertes Bleichmittel 1

sulfoniertes Aluminophthalocyanin, eingekapselt in Dextrin-löslichem Polymer.

PAAC

Pentaaminacetat-Cobalt(III)-Salz.

Paraffin

Paraffinöl, vertrieben unter dem Handelsnamen Winog 70 von Wintershall.

NaBz

Natriumbenzoat.

BzP

Benzoylperoxid.

Mannanase

Mannanase aus Bacillus agaradherens, NCIMB 40482

Protease

Proteolytisches Enzym, vertrieben unter dem Handelsnamen Sauinase, Alcalase, Durazym von Novo Nordisk A/S, Maxacal, Maxapem, vertrieben von Gist- Brocades und Proteasen, beschrieben in den Patenten WO91/06637 und/oder WO95/10591 und/oder EP 251 446.

Amylase

Amylolytisches Enzym, vertrieben unter dem Handelsnamen Purafact OxAm^R, beschrieben in WO94/18314, WO96/05295, vertrieben von Genencor; Termamyl^®, Fungamyl^® und Duramyl^®, alle erhältlich von Novo Nordisk A/S, und diejenigen, beschrieben in WO 95/26397.

Lipase

Lipolytisches Enzym, vertrieben unter dem Handelsnamen Lipolase, Lipolase Ultra von Novo Nordisk A/S, und Lipomax von Gist-Brocades.

Cellulase

Cellulytisches Enzym, vertrieben unter dem Handelsnamen Carezym, Celluzyme und/oder Endolase von Novo Nordisk A/S.

CMC

Natriumcarboxymethylcellulose.

PVP

Polyvinylpolymer mit einem durchschnittlichem Molekulargewicht von 60000.

PVNO

Polyvinylpyridin-N-Oxid mit einem durchschnittlichem Molekulargewicht von 50000.

PVPVI

Copolymer von Vinylimidazol und Vinylpyrrolidon mit einem durchschnittlichem Molekulargewicht von 20000.

Aufheller 1

Dinatrium-4,4'-bis(2-sulfostyryl)biphenyl.

Aufheller 2

Dinatrium-4,4'-bis(4-anilino-6-morpholino-1,3,5-triazin-2-yl)stilben-2:2'-disulfonat.

Siliconschaumverhüter

Polydimethylsiloxan-Schaumregulator mit Siloxan-Oxyalkylen-Copolymer als Dispergiermittel mit einem Verhältnis des Schaumregulators zu dem Dispergiermittel von 10:1 bis 100:1.

Schaumunterdrücker

12 % Silicon/Silica, 18 % Stearylalkohol, 70 % Stärke, in granulärer Form.

Trübungsmittel

wasserbasierende Monostyrol-Latex-Mischung, vertrieben von BASF Aktiengesellschaft unter dem Handelsnamen Lytron 621.

SRP1

anionisch endverkappte Polyester.

SRP2

Diethoxyliertes Poly(1,2-propylenterephthalat)-Kurzblock-Polymer.

QEA

Bis((C₂H₅O)(C₂H₄O)_n)(CH₃)-N⁺-C₆H₁₂-N⁺-(CH₃)bis((C₂H₅O)-(C₂H₄O))_n, worin n = 20 bis 30.

PEI

Polyethylenimin mit einem durchschnittlichen Molekulargewicht von 1800 und einem durchschnittlichen Ethoxylierungsgrad von 7 Ethylenoxy-Resten per Stickstoff.

SCS

Natriumcumensulfonat.

HMWPEO

hochmolekulargewichtiges Polyethylenoxid.

PEGx

Polyethylenglykol mit einem Molekulargewicht von x.

PEO

Polyethylenoxid mit einem durchschnittlichen Molekulargewicht von 5000.

TEPAE

Tetraethylenpentaaminethoxylat.

BTA

Benzotriazol.

pH

gemessen als 1 %ige Lösung in destilliertem Wasser bei 20°C.

In the detergent compositions, the enzyme levels are expressed as pure enzyme, based on the Weight of the total composition, and the detergent ingredients are based on the weight of the total compositions, unless otherwise specified. The abbreviated components in it have the following meanings:

READ

Linear sodium C _11-13 alkylbenzenesulfonate.

TAS

Natriumtalgalkylsulfat.

CxyAS

Sodium C _1x C _1y alkyl sulfate.

CxySAS

Sodium C _1x C _1y secondary (2,3) alkyl sulfate.

CxyEz

predominantly linear primary C _1x -C _1y alcohol, condensed with an average of z moles of ethylene oxide.

CxyEzS

Sodium C _1x C _{1y alkyl} sulfate condensed with an average of z moles of ethylene oxide.

QAS

R ₂ .N ⁺ (CH ₃ ) ₂ (C ₂ H ₄ OH) with R ₂ = C ₁₂ -C ₁₄ .

QAS1

R ₂ .N ⁺ (CH ₃ ) ₂ (C ₂ H ₄ OH) with R ₂ = C ₈ -C ₁₁

APA

C _8-10 amidopropyldimethylamine.

Soap

Linear sodium alkyl carboxylate derived from an 80/20 blend of tallow and coconut fatty acids.

nonionic

mixed C ₁₃ -C ₁₅ ethoxylated / propoxylated fatty alcohol with an average degree of ethoxylation of 3.8 and an average degree of propoxylation of 4.5.

Neodol 45-13

C ₁₄ -C ₁₅ linear primary alcohol ethoxylate sold by Shell Chemical Co.

STS

Sodium toluene.

CFAA

C ₁₂ -C ₁₄ alkyl-N-methylglucamide.

TFAA

C ₁₆ -C ₁₈ alkyl-N-methylglucamide.

TPKF

A topped total cut C ₁₂ -C ₁₄ fatty acids.

silicate

Amorphous sodium silicate (SiO ₂ : Na ₂ O ratio = 1.6-3.2).

metasilicate

Sodium silicate (SiO ₂ : Na ₂ O ratio = 1.0).

Zeolite A

Hydrated sodium aluminum silicate of the formula Na ₁₂ (AlO ₂ SiO ₂ ) ₁₂ 27H ₂ O with a primary particle size in the range of 0.1 to 10 microns (weight expressed on an anhydrous basis).

Na-SKS-6

crystalline layered silicate of the formula δ-Na ₂ Si ₂ O ₅ .

citrate

Trisodium citrate dihydrate with an activity of 86.4% with a particle size distribution between 425 and 850 micrometers.

citric acid

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 particle size distribution between 400 and 1200 microns.

sulfate

Anhydrous sodium sulfate.

Mg sulphate

Anhydrous magnesium sulfate.

STPP

Sodium tripolyphosphate.

TSPP

Tetrasodium pyrophosphate.

MA / AA

random copolymer of 4: 1 acrylate / maleate, average molecular weight about 70000-80000.

MA / AA 1

random copolymer of 6: 4 acrylate / maleate, average molecular weight about 10,000.

AA

Sodium polyacrylate polymer with an average molecular weight of 4500.

PA30

Polyacrylic acid with an average molecular weight between about 4500 - 8000.

480N

statistical copolymer of 7: 3 acrylate / methacrylate, average molecular weight about 3500.

Polygel / Carbopol:

high molecular weight cross-linked polyacrylates.

PB1

Anhydrous sodium perborate monohydrate of the nominal formula NaBO ₂ .H ₂ O ₂ .

PB4

Sodium perborate tetrahydrate of the nominal formula NaBO ₂ .3H ₂ OH ₂ O ₂ .

percarbonate

Anhydrous sodium percarbonate of the nominal formula 2 Na ₂ CO ₃ .3H ₂ O ₂ .

NaDCC

Sodium dichloroisocyanurate.

TAED

Tetraacetylethylenediamine.

NOBS

Nonanoyloxybenzenesulfonate in the form of the sodium salt.

NACA-OBS

(6-nonamidocaproyl) oxybenzene sulfonate.

DTPA

Diethylenetriaminepentaacetic.

HEDP

1,1-hydroxyethane.

DETPMP

Diethylene triamine penta (methylene) phosphonate, sold by Monsanto under the trade name Dequest 2060.

EDDS

Ethylenediamine-N, N'-disuccinic acid, (S, S) -isomer in the form of its sodium salt.

MnTACN

Manganese 1,4,7-trimethyl-1,4,7-triazacyclononane.

photoactivated bleach

sulfonated zinc phthalocyanine, encapsulated in dextrin-soluble polymer.

photoactivated bleach 1

sulfonated aluminophthalocyanine, encapsulated in dextrin-soluble polymer.

PAAC

Pentaamine acetate cobalt (III) salt.

paraffin

Paraffin oil, sold under the trade name Winog 70 by Wintershall.

NaBz

Sodium benzoate.

BZP

Benzoyl peroxide.

mannanase

Mannanase from Bacillus agaradherens, NCIMB 40482

protease

Proteolytic enzyme sold under the trade name Sauinase, 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 trade name Purafact OxAm ^R , described in WO94 / 18314, WO96 / 05295, sold by Genencor; Termamyl ^®, Fungamyl ^® and Duramyl ^®, all available from Novo Nordisk A / S and those described in WO 95/26397.

lipase

Lipolytic enzyme sold under the tradename Lipolase, Lipolase Ultra by Novo Nordisk A / S, and Lipomax by Gist-Brocades.

cellulase

Cellulytic enzyme, sold under the trade name Carezym, Celluzyme and / or Endolase by Novo Nordisk A / S.

CMC

Sodium.

PVP

Polyvinyl polymer with an average molecular weight of 60,000.

PVNO

Polyvinyl pyridine N-oxide with an average molecular weight of 50,000.

PVPVI

Copolymer of vinylimidazole and vinylpyrrolidone with an average molecular weight of 20,000.

Brightener 1

Disodium 4,4'-bis (2-sulfostyryl) biphenyl.

Brightener 2

Disodium 4,4'-bis (4-anilino-6-morpholino-1,3,5-triazin-2-yl) stilbene-2: 2'-disulfonate.

Siliconschaumverhüter

Polydimethylsiloxane foam regulator with siloxane-oxyalkylene copolymer as a dispersant with a ratio of the foam regulator to the dispersant from 10: 1 to 100: 1.

Suds suppressors

12% silicone / silica, 18% stearyl alcohol, 70% starch, in granular form.

opacifiers

water-based monostyrene-latex mixture, sold by BASF Aktiengesellschaft under the trade name Lytron 621.

SRP1

anionic end-capped polyester.

SRP2

Diethoxylated poly (1,2-propylene terephthalate) short block polymer.

QEA

Bis ((C ₂ H ₅ O) (C ₂ H ₄ O) _n ) (CH ₃ ) -N ⁺ -C ₆ H ₁₂ -N ⁺ - (CH ₃ ) bis ((C ₂ H ₅ O) - (C ₂ H ₄ O)) _n , where n = 20 to 30.

PEI

Polyethyleneimine with an average molecular weight of 1800 and an average degree of ethoxylation of 7 ethyleneoxy radicals per nitrogen.

SCS

Sodium cumene sulfonate.

HMWPEO

high molecular weight polyethylene oxide.

PEGx

Polyethylene glycol with a molecular weight of x.

PEO

Polyethylene oxide with an average molecular weight of 5000.

TEPAE

Tetraethylenepentaamine ethoxylate.

BTA

Benzotriazole.

pH

measured as a 1% solution in distilled water at 20 ° C.

example 1

The following high density granular Laundry detergent compositions were according to the present Invention made:

Example 2

The following granular Laundry detergent compositions with particular usefulness among European Machine wash conditions were in accordance with the present invention manufactured:

Example 3

The following detergent compositions with particular utility among European Machine wash conditions were in accordance with the present invention manufactured:

Example 4

The following granular Detergent compositions were made in accordance with the present invention:

Example 5

The following detergent compositions were made according to the present invention manufactured:

Example 6

The following granular Detergent compositions were made in accordance with the present invention:

Example 7

The following detergent compositions were made according to the present invention manufactured:

Example 8

The following detergent compositions were made according to the present invention manufactured:

Example 9

The following granular Textile detergent compositions which provide "softener-while-laundry" capabilities were according to the present Invention made:

Example 10

The following detergent additive compositions were made according to the present Invention made:

Example 11

The following compact high density (0.96 kg / l) dishwashing detergent compositions were according to the present Invention made:

Example 12

The following granular Dishwashing detergent compositions with a bulk density of 1.02 kg / l were according to the present Invention made:

Example 13

SEQUENZ-AUFLISTUNG (1) Allgemeine Information: ANMELDER: Name: The Procter & Gamble Company Strasse: One Procter & Gamble Plaza Stadt: Cincinnati, OHIO Land: USA Postleitzahl: 45202 TITEL DER ERFINDUNG: Detergenszusammensetzungen, umfassend eine Mannanase und Percarbonat ANZAHL DER SEQUENZEN: 6 COMPUTER-LESBARE FORM: Mediumtyp: Diskette Computer: IBM PC-Kompatibel Betriebssystem: PC-DOS/MS-DOS Software: PatentIn Release #1.0 Version 1.25 (EPO) SEQ-ID Nr.: 1 Sequenzmerkmale: Länge: 1407 Basenpaare Typ: Nukleinsäure Strangart: einzelsträngig Topologie: linear Molekültyp : genomische DNA Ursprungsquelle Merkmal: Name/Schlüssel: CDS Lokalisierung: 1–1482 Sequenzbeschreibung SEQ-ID Nr.: 1

SEQ-ID Nr.: 2 Sequenzmerkmale: Länge: 493 Aminosäuren Typ: Aminosäure Topologie: linear Molekültyp: Protein Sequenzbeschreibung SEQ-ID Nr.: 2

SEQ-ID Nr.: 3 Sequenzmerkmale: Länge: 1407 Basenpaare Typ: Nukleinsäure Strangart: einzelsträngig Topologie: linear Molekültyp : genomische DNA Sequenzbeschreibung SEQ-ID Nr.: 3

SEQ-ID Nr.: 4 Sequenzmerkmale: Länge: 468 Aminosäuren Typ: Aminosäure Topologie: linear Molekültyp : Protein Sequenzbeschreibung SEQ-ID Nr.: 4

SLQ-ID Nr.: 5 Sequenzmerkmale: Länge: 1029 Basenpaare Typ: Nukleinsäure Strangart: einzelsträngig Topologie: linear Molekültyp : genomische DNA Sequenzbeschreibung SEQ-ID Nr.: 5

SEQ-ID Nr.: 6 Sequenzmerkmale: Länge: 363 Aminosäuren Typ: Aminosäure Topologie: linear Molekültyp: Protein Sequenzbeschreibung SEQ-ID Nr.: 6

The following tablet detergent compositions were made in accordance with the present invention by compressing a granular dishwashing detergent composition at a pressure of 13 KN / cm ² using a standard 12-head rotary press:

SEQUENCE LISTING (1) General information: LOGIN: Surname: The Procter & Gamble Company Road: One Procter & Gamble Plaza City: Cincinnati, OHIO Country: United States Post Code: 45202 TITLE OF THE INVENTION: Detergent compositions comprising a mannanase and percarbonate NUMBER OF SEQUENCES: 6 COMPUTER READABLE FORM: Media Type: diskette Computer: IBM PC compatible Operating system: PC-DOS / MS-DOS Software: PatentIn Release # 1.0 Version 1.25 (EPO) SEQ ID No .: 1 sequence characteristics: Length: 1407 base pairs Type: nucleic acid Strandedness: single stranded Topology: linear Molecule type: genomic DNA original source Characteristic: NAME / KEY: CDS localization: 1-1482 Sequence description SEQ ID No .: 1

SEQ ID No .: 2 sequence characteristics: Length: 493 amino acids Type: amino acid Topology: linear Molecule type: protein Sequence description SEQ ID No .: 2

SEQ ID No .: 3 sequence characteristics: Length: 1407 base pairs Type: nucleic acid Strandedness: single stranded Topology: linear Molecule type: genomic DNA Sequence description SEQ ID No .: 3

SEQ ID No .: 4 sequence characteristics: Length: 468 amino acids Type: amino acid Topology: linear Molecule type: protein Sequence description SEQ ID No .: 4

SLQ ID No .: 5 sequence characteristics: Length: 1029 base pairs Type: nucleic acid Strandedness: single stranded Topology: linear Molecule type: genomic DNA Sequence description SEQ ID No .: 5

SEQ ID No .: 6 sequence characteristics: Length: 363 amino acids Type: amino acid Topology: linear Molecule type: protein Sequence description SEQ ID No .: 6

Claims (13)

A detergent composition comprising a mannanase enzyme and percarbonate. The detergent composition of claim 1, wherein the Mannanase in a proportion of 0.0001% to 2%, preferably 0.0005% up to 0.5%, particularly preferably from 0.001% to 0.02% pure enzyme, based on the weight of the total composition. A detergent composition according to any one of claims 1-2, wherein the percarbonate in a proportion of 0.1% to 50%, preferably of 0.5% to 35%, particularly preferably from 1% to 25%, by weight the total composition. A detergent composition according to claims 1-3, wherein the percarbonate has an average particle size of 250 up to 900 μm having. A detergent composition according to claims 1-4, comprising still a protease. A detergent composition according to claim 5, wherein the Protease is a protease of the IUPAC classification EC 3.4. .-, preferably an endoserine protease of the IUPAC classification EC 3.4.21.-, particularly preferably a subtilisin protease of the IUPAC classification EC 3.4.21.62 is and most preferably from BLAP, Savinase and mixtures thereof existing group is selected. Detergent composition according to one of the preceding Expectations, further comprising an amylase enzyme, preferably termamyl. Detergent composition according to one of the preceding Expectations, further comprising a builder, preferably selected from the group consisting of zeolite A, layered sodium silicate, sodium tripolyphosphate, Polycarboxylate, and mixtures thereof. Detergent composition according to one of the preceding Expectations, further comprising a surfactant, preferably selected from the group consisting of anionic surfactant, nonionic surfactant as well as mixtures thereof. A detergent composition according to claim 9, wherein selected the anionic surfactant is from the group consisting of linear alkylbenzenesulfonate, Alkyl ester sulfonate and mixtures thereof. Detergent composition according to claims 9 to 10, wherein the nonionic surfactant is an alkyl polyglycoside, preferably an alkyl polyglycoside of the formula R ² O (C _n H _2n O) _t (glycosyl) _x , wherein R ^{2 is} selected from the group consisting of alkyl, alkylphenyl , Hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof, wherein 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 ranges from 0 to about 10, preferably is 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, more preferably from 1.3 to about 2.7. Detergent composition according to claims 9 to 10, wherein the nonionic surfactant is an alkyl ethoxylated nonionic Surfactant with an alkyl group having about 8 to about 20 carbon atoms, preferably approximately 10 to about Contains 18 carbon atoms, with about 2 to about 10 moles, preferably 2 to about 7 moles, particularly preferably 2 to 5 moles of ethylene oxide per mole of alcohol is. A detergent composition comprising a mannanase enzyme; Percarbonate, a second enzyme selected from the group consisting of from protease, amylase and mixtures thereof; a builder selected from the group consisting of zeolite A, layered sodium silicate, sodium tripolyphosphate, Polycarboxylate and mixtures thereof; and a surfactant selected from the group consisting of anionic surfactant, nonionic surfactant as well as mixtures thereof.