Composition comprising lipase and peptide

Abstract

The present invention relates to compositions comprising (a) a lipase; and (b) one or more peptides that enhance / enhance the performance / activity of the lipase. The invention also relates to a method of cleaning or washing using a composition of the invention and an enzyme product comprising (a) a lipase and (b) one or more peptides. Finally, the invention also relates to a peptide capable of enhancing / enhancing the fat removal performance / activity of a lipase.

Description

[0001] Reference to the Sequence Listing

[0002] This application contains a Sequence Listing in computer-readable form, which is hereby incorporated by reference. BACKGROUND OF THE INVENTION TECHNICAL FIELD

[0004] The present invention relates to compositions for removing fatty stains from laundry during cleaning or washing of the laundry. The present invention also relates to a method for cleaning or washing laundry. Finally, the present invention also relates to enzyme products suitable for use in, for example, the detergent compositions of the present invention, and to peptides suitable for use in the compositions of the present invention and capable of enhancing / enhancing the fat-removing performance / activity of lipase. BACKGROUND ART

[0005] Detergent compositions containing enzymes for laundry cleaning or washing are well known. Although there are significant cross-regional differences in the detailed ingredient lists of detergent compositions, the main washing mechanisms are similar. Typically, dirt and stains are removed by mechanical action assisted by enzymes, surfactants, and other ingredients. Historically, proteases were first widely used for laundry washing. Nowadays, in particular, α-amylase, mannanase, cellulase, and lipase have been introduced to increase effectiveness, especially for home laundry washing at lower temperatures.

[0006] Lipase breaks down fats into fatty acids that dissolve in the surfactant.

[0007] WO 2006 / 113314 relates to a liquid laundry detergent composition comprising (a) a first washing lipase from about 5 to about 20000 LU / g, which is a polypeptide having an amino acid sequence with at least 90% identity to the wild-type lipase derived from Humicola lanuginosa strain DSM 4109, and compared to the wild-type lipase, the first washing lipase comprises a substitution of an electro-neutral or negatively charged amino acid within 15 Å of E1 or Q249 with a positively charged amino acid; and the first washing lipase may further: (I) comprise a peptide addition at the C-terminus; (II) comprise a peptide addition at the N-terminus; (III) satisfy the following restrictions: i) comprise a negatively charged amino acid at position E210 of the wild-type lipase; ii) comprise a negatively charged amino acid in the region corresponding to positions 90-101 of the wild-type lipase; and iii) comprise a neutral or negatively charged amino acid at the position corresponding to N94 of the wild-type lipase; and / or iv) have a negative or neutral charge in the region corresponding to positions 90-101 of the wild-type lipase; and (IV) mixtures thereof; (b) a modified polyethyleneimine polymer from about 0.01 wt% to about 10 wt% by weight of the composition, wherein the modified polyethyleneimine polymer comprises a polyethyleneimine backbone with a weight average molecular weight of about 300 to about 10000; the modification of the polyethyleneimine backbone is: (1) one or two alkoxylation modifications / nitrogen atoms in the polyethyleneimine backbone, the alkoxylation modification comprising replacement of a hydrogen atom with a polyalkyleneoxy chain having an average of about 1 to about 40 alkoxy moieties / modifications, wherein the terminal alkoxy moiety of the alkoxylation modification is capped with hydrogen, a C1-C4 alkyl group or a mixture thereof; (2) substitution of one C1-C4 alkyl moiety in the polyethyleneimine backbone and one or two alkoxylation modifications / nitrogen atoms, the alkoxylation modification comprising replacement of a hydrogen atom with a polyalkyleneoxy chain having an average of about 1 to about 40 alkoxy moieties / modifications, wherein the terminal alkoxy moiety is capped with hydrogen, a C1-C4 alkyl group or a mixture thereof; or (3) a combination thereof; and (c) the remainder of the composition comprising a liquid carrier.

[0008] WO 2005 / 105831 relates to antimicrobial peptides. SEQ ID NO: 93 discloses a peptide having the amino acid sequence KNLRRIIRKGIHIIKKYF.

[0009] Taboureau et al., 2006 Chem Biol Drug Des (68) pp. 48-57 relate to antimicrobial peptides designed to develop alternative treatments against multi-drug resistant microorganisms. The disclosed antimicrobial peptides include MA-Novospirin G10 having the sequence MAKNLRRIIRKGIHIIKKYG.

[0010] There is still a need for compositions having improved fat stain removal performance / activity. Summary of the Invention

[0011] The present invention relates to compositions comprising:

[0012] (a) one or more lipases; and

[0013] (b) one or more peptides selected from the group consisting of:

[0014] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2; and / or

[0015] ii) a peptide having the sequence KNLRRIIRKGIIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10.

[0016] Without being bound by any theory, it is believed that the high K (Lys) content and / or high R (Arg) content in the peptides defined in i) and ii) positively contribute to the enhancement of the fat removal performance / activity of these peptides on lipases.

[0017] The inventors unexpectedly found that when lipases are used in combination with the peptides shown in SEQ ID NO: 2 and SEQ ID NO: 10 in detergent compositions, an enhancement of the fat removal activity / performance of the lipases is obtained. This is demonstrated in the examples. According to the present invention, the benefit-risk factor can also be improved.

[0018] According to the present invention, compared to the absence of a peptide (as defined herein), in particular the absence of the peptides of SEQ ID NO: 2 and / or SEQ ID NO: 3 or 10 respectively, the compositions of the present invention provide increased fat removal, especially when used for cleaning or washing, especially when used for cleaning or washing clothes.

[0019] In an embodiment of the present invention, at least 10%, preferably at least 12%, more preferably at least 14%, more preferably at least 16%, even more preferably 18%, especially at least 20% of the fat stains are removed (as determined by the % fat removal in the washing state as described in Example 1 or 2).

[0020] In an embodiment of the present invention, compared to when no peptide (as defined) is used, in particular when no peptide of SEQ ID NO:2 and / or SEQ ID NO: 3 or 10 is used, the fat removal in the washing state is increased by at least 5%, at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 100%.

[0021] The compositions of the present invention may advantageously comprise a surfactant or a surfactant system.

[0022] In an embodiment, the compositions of the present invention comprise one or more anionic surfactants, preferably selected from the group consisting of linear alkylbenzene sulfonates (LAS), alkyl sulfates (AS), and sodium lauryl ether sulfate (SLES) and combinations thereof.

[0023] In an embodiment, the composition comprises one or more nonionic surfactants, preferably alcohol ethoxylates (AEO), especially linear alcohol (C12-15) ethoxylates (LAE).

[0024] In an embodiment, the compositions of the present invention comprise the anionic surfactants linear alkylbenzene sulfonic acid (LAS), sodium lauryl ether sulfate (SLES), and alkyl sulfate (AS), and the nonionic surfactant alcohol ethoxylate (AEO).

[0025] In another embodiment, the compositions of the present invention comprise the anionic surfactants linear alkylbenzene sulfonic acid (LAS) and sodium lauryl ether sulfate (SLES).

[0026] In an embodiment, the composition of the present invention comprises an anionic surfactant linear alkylbenzene sulfonic acid (LAS) and sodium lauryl ether sulfate (SLES), and a nonionic surfactant alcohol ethoxylate (AEO).

[0027] In an embodiment, the surfactant system comprises LAS, SLES, AS and AEO.

[0028] In an embodiment, the surfactant system comprises LAS, SLES and AEO.

[0029] In an embodiment, the ratio between the anionic surfactant and the nonionic surfactant ranges from 20:1 to 1:1, such as 15:1 to 10:1, especially about 4:1.

[0030] In a specific embodiment, the composition comprises the components in the standard Detergent J disclosed in Examples 1 and 2.

[0031] The composition of the present invention may further comprise one or more components selected from the group consisting of: builders, chelating agents, dye transfer inhibitors, dispersants, enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric dispersants, clay removal / anti-redeposition agents, brighteners, foam inhibitors, dyes, colorant dyes, fragrances, fragrance delivery systems, fabric softeners, carriers, hydrotropes, processing aids, solvents and / or pigments.

[0032] In an embodiment, the composition comprises a lipase (especially the Thermomyces lanuginosus lipase (TLL) or its variant (especially the variant disclosed herein) disclosed in SEQ ID NO: 1 or the Geotrichum candidum lipase 1 (GCL 1) disclosed in SEQ ID NO: 4 herein), the peptides shown in SEQ ID NO: 2 and SEQ ID NO: 3 or 10, DNase and / or protease, and preferably also a surfactant or a surfactant system.

[0033] In an embodiment, the composition of the present invention comprises a commercial lipase product selected from the group consisting of: Lipolase TM , Lipex™; Lipolex TM , Lipoclean TM, Lipex Evity 100L, Lipex Evity 105T, Lipex Evity 200L (from Novozymes), Lumafast (from Genencor), Preferenz L100 (Danisco US Inc.), and Lipomax (from Gist-Brocades).

[0034] The present invention also relates to methods for cleaning or washing laundry, which methods comprise contacting the laundry with a composition of the present invention.

[0035] In the context of the present invention, "laundry" particularly includes textiles, clothes, linen, etc. In particular, the laundry may be contaminated such that washing or cleaning is required to remove lipid stains such as lard, fat, oil, etc. Lipids include glycerides (e.g., triglycerides), phospholipids, glycolipids, and fatty acids.

[0036] The washing or cleaning methods of the present invention are typically carried out in a washing machine (e.g., top-loading or front-loading washing machine), but can also be carried out in other ways such as manually (e.g., in the form of a laundry soap bar).

[0037] According to the method of the present invention, lipase is administered at a concentration of 0.01 to 10, particularly 0.05 - 5 mg enzyme protein (EP) / L of the washing liquor.

[0038] In an embodiment, lipase is administered at a concentration of 0.001 - 5 ppm, particularly at a concentration of 0.01 - 1 ppm, especially 0.1 - 0.2 ppm.

[0039] In an embodiment, the peptide is administered at a concentration of 0.001 - 100 ppm, particularly at a concentration of 0.01 - 50 ppm, especially 0.1 - 25 ppm.

[0040] In an embodiment, the washing liquor contains a detergent composition from 0.01 - 10 g / L, particularly 0.05 - 5 g / L, especially 0.3 - 3 g / L (such as approximately 0.8 g / L).

[0041] In one aspect, the present invention relates to enzyme products, which enzyme products comprise:

[0042] (a) one or more lipases, particularly lipases as defined herein; and

[0043] (b) one or more peptides selected from the group consisting of:

[0044] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 2; and / or

[0045] ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or 10, respectively.

[0046] In a preferred embodiment, the enzyme product of the present invention is formulated as a liquid enzyme formulation.

[0047] In a preferred embodiment, the enzyme product of the present invention is formulated as a solid / granular enzyme formulation.

[0048] Definitions

[0049] Lipase: The terms "lipase", "lipase enzyme", "lipolytic enzyme", "lipid esterase", "lipolytic polypeptide", and "lipolytic protein" refer to enzymes in the EC 3.1.1 class as defined by Enzyme Nomenclature. It may have lipase activity (triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74), sterol esterase activity (EC 3.1.1.13), and / or wax ester hydrolase activity (EC 3.1.1.50). For the purposes of the present invention, lipase activity (i.e., the hydrolytic activity of lipase) can be determined using pNP assays with substrates of different chain lengths as described in the "Materials and Methods" section.

[0050] Fragment: The term "fragment" means a polypeptide with one or more (e.g., several) amino acids deleted from the amino and / or carboxyl terminus of a polypeptide; wherein the fragment has lipase activity. In one aspect, the fragment contains at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, or at least 95% of the number of amino acids 1 to 269 of SEQ ID NO: 1, 2, 3, or 4, but less than 100%.

[0051] Parent or parental lipase: The term "parent" or "parental lipase" means a lipase that has been altered to produce an enzyme variant. The parental lipase can be a naturally occurring (wild-type) polypeptide, but can also be a variant and / or fragment thereof. In a preferred embodiment, the parental lipase can be the parental lipase shown in SEQ ID NO: 1 or 4.

[0052] SEQ ID NO: 1 is the wild-type Thermomyces lanuginosus lipase (synonym: Humicola lanuginosa DSM 4109 lipase), commonly abbreviated as "TLL".

[0053] SEQ ID NO: 4 is the Geotrichum candidum lipase disclosed as SEQ ID NO: 1 in WO 2022 / 162043 and described by Bertolini et al. (Eur. J. Biochem. [European Journal of Biochemistry] 228, 863-869 (1995)) (incorporated herein by reference).

[0054] Peptide: The term "peptide" means an organic chemical molecule containing two or more amino acids linked together by peptide bonds. In the context of the present invention, the peptide enhances the fat removal performance / activity of the lipase, particularly during cleaning or washing.

[0055] SEQ ID NO: 2 is a peptide consisting of the following amino acids: PKGLLRRFLRALRILVPKD (peptide X)

[0056] SEQ ID NO: 3 is a peptide consisting of the following amino acids: KNLRRIIRKGIHIKKYF (peptide Y').

[0057] SEQ ID NO: 10 is a peptide consisting of the following amino acids: KNLRRIIRKGIHIIKKYF (peptide Y).

[0058] In a preferred embodiment, the peptide as defined in i) or ii) used according to the present invention does not (when used alone) have enzymatic activity.

[0059] Sequence identity: The degree of relatedness between two amino acid sequences is described by the parameter "sequence identity".

[0060] For the purposes of the present invention, the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) is used to determine the sequence identity between two amino acid sequences, which algorithm is implemented as in the Needle program of the EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277) (preferably version 5.0.0 or later). The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (the EMBOSS version of BLOSUM62) substitution matrix. The output of "longest identity" marked by Needle (obtained using the non-abbreviated (-no brief) option) is used as the percentage identity and is calculated as follows:

[0061] (Identical residues × 100) / (Alignment length - Total number of gaps in the alignment)

[0062] Clothing: According to the present invention, the term "clothing" includes textiles, garments, linens, etc., and can be made of any material, including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile materials. Fabrics made from these materials and products made from these fabrics (e.g., clothing and other items). The textile or fabric can be in the form of knitted fabric, woven fabric, denim, non-woven fabric, felt, yarn, and terry cloth. The textile can be cellulose-based, such as natural cellulose products, including cotton, linen / flax, jute, ramie, sisal, or coir, or man-made cellulose products (e.g., derived from wood pulp), including viscose / rayon, acetate fiber (triacetate), lyocell, or blends thereof. The textile or fabric can also be non-cellulose-based, such as natural polyamides, including wool, camel hair, cashmere, mohair, rabbit hair, and silk, or synthetic polymers such as nylon, aramid, polyester, acrylate, polypropylene, and spandex / elastane, or blends thereof, as well as blends of cellulose-based fibers and non-cellulose-based fibers. Examples of blends are blends of cotton and / or rayon / viscose with one or more accompanying materials, such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and / or cellulose-containing fibers (e.g., rayon / viscose, ramie, linen / flax, jute, acetate fiber, lyocell). The fabric can be conventional washable clothing, such as soiled household clothing. When the terms fabric or garment are used, it is intended to also include the broad term textile. In the context of the present invention, the term "clothing" also encompasses fabrics.

[0063] Wild-type lipase: The term "wild-type" lipase means a lipase expressed by a naturally occurring microorganism found in nature, such as a bacterium, yeast, or filamentous fungus. In an embodiment, the wild-type lipase is the lipase shown in SEQ ID NO: 1 herein, which is derived from Thermomyces lanuginosus DSM 4109 (synonym: Humicola lanuginosa DSM 4109). In another embodiment, the lipase is the lipase shown in SEQ ID NO: 4 herein, which is derived from the Geotrichum candidum strain disclosed by Bertolini et al. (Eur. J. Biochem. [European Journal of Biochemistry] 228, 863-869 (1995)).

[0064] Variant: The term "variant" means a polypeptide having lipase activity and containing alterations (i.e., substitutions, insertions, and / or deletions) at one or more (e.g., several) positions. Substitution means replacing the amino acid occupying a position with a different amino acid; deletion means removing the amino acid occupying a position; and insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.

[0065] Washing performance: Washing performance can be tested by measuring fat removal performance / activity using any suitable assay. A suitable example is the miniLOM assay used in Examples 1 and 2 herein.

[0066] Detergent for testing fat removal: For the purposes of the present invention, for example, Standard J detergent can be used to determine fat removal. Standard J detergent contains a surfactant system that contains anionic and non-ionic surfactants as described in Examples 1 and 2. Fat removal can be determined by comparing the % fat removal in the presence of the peptide in question and the % fat removal in the absence of the peptide in question as described in the examples.

[0067] Benefit-risk factor: The benefit-risk factor (BRF) describes the washing performance (benefit) compared to odor release (risk) and is defined as relative washing performance / relative odor release. If the benefit-risk factor is higher than 1.0, then the lipase combined with the peptide in question has better washing performance relative to the odor released compared to the reference lipase. A BRF higher than 1.0 allows the use of less lipase to achieve the same performance without increasing odor release compared to using the reference lipase alone.

[0068] Variant naming convention

[0069] For the purposes of the present invention, the lipase disclosed in SEQ ID NO: 1 is used to identify the corresponding amino acid residues in another lipase. The amino acid sequence of the other lipase is aligned with SEQ ID NO: 1, and based on this alignment, the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) is used to determine the amino acid position numbers corresponding to any amino acid residues in the polypeptide disclosed in SEQ ID NO: 1, as implemented in the Needle program of the EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277) (preferably version 5.0.0 or later). The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (the EMBOSS version of BLOSUM62) substitution matrix.

[0070] The identification of the corresponding amino acid residues in another lipase can be determined by aligning multiple polypeptide sequences using several computer programs with their corresponding default parameters, including but not limited to MUSCLE (Multiple Sequence Comparison by Log-Expectation; version 3.5 or later; Edgar, 2004, Nucleic Acids Research 32: 1792-1797), MAFFT (version 6.857 or later; Katoh and Kuma, 2002, Nucleic Acids Research 30: 3059-3066; Katoh et al., 2005, Nucleic Acids Research 33: 511-518; Katoh and Toh, 2007, Bioinformatics 23: 372-374; Katoh et al., 2009, Methods in Molecular Biology 537: 39-64; Katoh and Toh, 2010, Bioinformatics 26: 1899 - 1900), and EMBOSS EMMA using ClustalW (version 1.83 or later; Thompson et al., 1994, Nucleic Acids Research 22: 4673 - 4680).

[0071] When other enzymes deviate from the lipase of SEQ ID NO: 1 such that traditional sequence - based comparison methods cannot detect their relationship (Lindahl and Elofsson, 2000, J. Mol. Biol. 295:613 - 615), other pairwise sequence comparison algorithms can be used. Higher sensitivity in sequence - based searches can be obtained using search programs that utilize the probabilistic representation (profile) of a polypeptide family to search databases. For example, the PSI - BLAST program generates multiple profiles through an iterative database search process and is able to detect distant homologs (Atschul et al., 1997, Nucleic Acids Res. 25: 3389 - 3402). Even higher sensitivity can be achieved if a polypeptide family or superfamily has one or more representatives in the protein structure database. Programs such as GenTHREADER (Jones, 1999, J. Mol. Biol. 287: 797 - 815; McGuffin and Jones, 2003, Bioinformatics 19: 874 - 881) use information from multiple sources (PSI - BLAST, secondary structure prediction, structure alignment profiles, and solvation potential) as input to a neural network that predicts the structural fold of a query sequence. Similarly, the method of Gough et al., 2000, J. Mol. Biol. 313:903 - 919 can be used to align sequences of unknown structure to superfamily models present in the SCOP database. These alignments can then be used to generate homology models of the polypeptide, and the accuracy of such models can be evaluated using a variety of tools developed for this purpose.

[0072] For proteins of known structure, several tools and resources are available for retrieving and generating structural alignments. For example, the SCOP superfamilies of proteins have been structurally aligned, and those alignments are accessible and downloadable. Multiple algorithms such as the distance alignment matrix (Holm and Sander, 1998, Proteins 33: 88-96) or combinatorial extension (Shindyalov and Bourne, 1998, Protein Engineering 11: 739-747) can be used to align two or more protein structures, and implementations of these algorithms can additionally be used to query structure databases with a structure of interest in order to find possible structural homologs (e.g., Holm and Park, 2000, Bioinformatics 16: 566-567).

[0073] In the context of the present invention, the following nomenclature is adopted for convenience of reference when describing variants. The accepted IUPAC single-letter or three-letter amino acid abbreviations are used.

[0074] Substitution . For amino acid substitutions, the following nomenclature is used: the original amino acid, the position, the substituting amino acid. Accordingly, the substitution of threonine by alanine at position 226 is denoted "Thr226Ala" or "T226A". Multiple mutations are separated by a plus sign ("+"), e.g., "Gly205Arg+Ser411Phe" or "G205R+S411F" represents the substitution of glycine (G) and serine (S) at positions 205 and 411 by arginine (R) and phenylalanine (F), respectively.

[0075] Deletion . For amino acid deletions, the following nomenclature is used: the original amino acid, the position, * . Accordingly, the deletion of glycine at position 195 is denoted "Gly195*" or "G195*". Multiple deletions are separated by a plus sign ("+"), e.g., "Gly195* + Ser411*" or "G195* + S411*".

[0076] Insertion.For amino acid insertions, the following nomenclature is used: original amino acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of lysine after glycine at position 195 is denoted as "Gly195GlyLys" or "G195GK". Insertions of multiple amino acids are denoted as [original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2; etc.]. For example, the insertion of lysine and alanine after glycine at position 195 is denoted as "Gly195GlyLysAla" or "G195GKA".

[0077] In such cases, the one or more inserted amino acid residues are numbered by adding a lower case letter to the position number of the amino acid residue preceding the one or more inserted amino acid residues. In the above example, the sequence would thus be:

[0078]

[0079] Multiple changes . Variants containing multiple changes are separated by a plus sign ("+"), e.g., "Arg170Tyr+Gly195Glu" or "R170Y+G195E" represents that the arginine and glycine at positions 170 and 195 are replaced by tyrosine and glutamate, respectively.

[0080] Different changes . When different changes can be introduced at one position, these different changes are separated by a comma, e.g., "Arg170Tyr, Glu" or "R170Y, E" represents that the arginine at position 170 is replaced by tyrosine or glutamate. Thus, "Tyr167Gly, Ala + Arg170Gly, Ala" represents the following variants:

[0081] "Tyr167Gly+Arg170Gly", "Tyr167Gly+Arg170Ala", "Tyr167Ala+Arg170Gly", and "Tyr167Ala+Arg170Ala". Detailed Description

[0082] The present invention relates to improved compositions that comprise one or more lipases capable of removing fatty stains from surfaces, in particular fabrics. According to the invention, the lipases are used in combination with one or more peptides. The combination of lipase and the peptides as defined herein enhances the fat-removing performance / activity of the lipase. The present invention also relates to methods of cleaning or laundering (in particular fabrics) using the compositions of the invention. In addition, the present invention relates to enzyme products that comprise one or more lipases and one or more peptides as defined herein. Finally, the present invention relates to peptides that enhance the fat-removing activity of lipases and are suitable for use in the compositions of the invention. The enzyme products can be used in the compositions of the invention.

[0083] The composition of the present invention

[0084] In a first aspect, the present invention relates to compositions comprising a combination of a lipase and a peptide, which, under the same conditions (in particular cleaning or laundering conditions), remove more fat than the corresponding compositions comprising only the same lipase.

[0085] Specifically, the present invention relates to compositions that comprise:

[0086] (a) one or more lipases; and

[0087] (b) one or more peptides selected from the group consisting of:

[0088] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2; and / or

[0089] ii) peptides having the sequences KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10), respectively, and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10, respectively.

[0090] Without being bound by any theory, it is believed that the high K (Lys) content and / or high R (Arg) content in the peptides defined in i) and ii) above positively contribute to the enhancement of the fat removal performance of these peptides against lipase.

[0091] In embodiments, the peptides defined in i) or ii) included in the compositions of the present invention have a high K (Lys) content and / or a high R (Arg) content.

[0092] In embodiments, the peptide defined in i) has K (Lys) at positions corresponding to position 2 and / or position 18 (numbered using SEQ ID NO: 2).

[0093] In embodiments, the peptide defined in i) has R (Arg) at positions corresponding to position 6 and / or position 7 and / or position 10 and / or position 13 (numbered using SEQ ID NO: 2).

[0094] In embodiments, the peptide defined in i) has at least 2 Ks, such as 3 Ks, such as 4 Ks, such as 5 Ks.

[0095] In embodiments, the peptide defined in i) has at least 4 Rs, such as 5 Rs, such as 6 Rs, such as 7 Rs, such as 8 Rs.

[0096] In embodiments, the peptide defined in ii) has K at positions corresponding to position 1 and / or position 9 and / or position 14 and / or position 15 (numbered using SEQ ID NO: 3), or has K at positions corresponding to position 1 and / or position 9 and / or position 15 and / or position 16 (numbered using SEQ ID NO: 10).

[0097] In embodiments, the peptide defined in ii) has R at positions corresponding to position 4 and / or position 5 and / or position 8 (numbered using SEQ ID NO: 3 or 10).

[0098] In embodiments, the peptide defined in ii) has at least 4 Ks, such as 5 Ks, such as 6 Ks, such as 7 Ks.

[0099] In embodiments, the peptide defined in ii) has at least 3 Rs, such as 4 Rs, such as 5 Rs, such as 6 Rs, or such as 8 Rs.

[0100] In embodiments, the peptide defined in i) has at least 20% R (Arg), such as at least 25% R (Arg), particularly at least 30% R (Arg).

[0101] In an embodiment, the peptide defined in i) has at least 10% K (Lys), such as at least 15% K (Lys), particularly at least 20% K (Lys).

[0102] In an embodiment, the peptide defined in ii) has at least 15% R (Arg), such as at least 20% R (Arg), particularly at least 25% R (Arg).

[0103] In an embodiment, the peptide defined in ii) has at least 20% K (Lys), such as at least 25% K (Lys), particularly at least 30% K (Lys).

[0104] In an embodiment, the peptide defined in i) consists of 15 to 25 amino acids, preferably consists of 17 - 21 amino acids, such as 15 amino acids, such as 16 amino acids, such as 17 amino acids, such as 18 amino acids, particularly 19 amino acids, such as 20 amino acids, such as 21 amino acids, such as 22 amino acids, such as 23 amino acids, such as 24 amino acids, such as 25 amino acids.

[0105] In a preferred embodiment, the peptide defined in i) contains 19 amino acids or consists of 19 amino acids.

[0106] In an embodiment, the peptide defined in ii) consists of 13 to 23 amino acids, preferably consists of 15 - 21 amino acids, such as 13 amino acids, such as 14 amino acids, such as 15 amino acids, such as 16 amino acids, particularly 17 amino acids, such as 18 amino acids, such as 19 amino acids, such as 20 amino acids, such as at least 21 amino acids, such as 22 amino acids, such as at least 23 amino acids.

[0107] In a preferred embodiment, the peptide defined in ii) contains 17 or 18 amino acids or consists of 17 or 18 amino acids.

[0108] In an embodiment, the composition of the present invention comprises a surfactant or surfactant system, one or more lipases (particularly the lipases as defined herein), and one or more peptides as defined herein.

[0109] In an embodiment, the composition is used for cleaning or washing, particularly for laundry. However, the composition of the present invention can also be used for other purposes, such as manual dishwashing (e.g., hand - washing dishes or washing clothes with a soap bar) and automatic dishwashing (ADW).

[0110] Surfactant or surfactant system

[0111] In a preferred embodiment, the composition of the present invention (in particular, a detergent composition) comprises a surfactant or a surfactant system.

[0112] In an embodiment, the surfactant or surfactant system comprises one or more surfactants selected from the group consisting of: nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof.

[0113] In a preferred embodiment, one or more surfactants are present at a level of from 0.1 wt% to 60 wt%, from 0.2 wt% to 40 wt%, from 0.5 wt% to 30 wt%, from 1 wt% to 50 wt%, from 1 wt% to 40 wt%, from 1 wt% to 30 wt%, from 1 wt% to 20 wt%, from 3 wt% to 10 wt%, from 3 wt% to 5 wt%, from 5 wt% to 40 wt%, from 5 wt% to 30 wt%, from 5 wt% to 15 wt%, from 3 wt% to 20 wt%, from 3 wt% to 10 wt%, from 8 wt% to 12 wt%, from 10 wt% to 12 wt%, from 20 wt% to 25 wt% or from 25% - 60%.

[0114] Suitable anionic detersive surfactants include sulfate and sulfonate detersive surfactants.

[0115] Suitable sulfonate detersive surfactants include alkylbenzene sulfonates, in one aspect C 10-13 alkylbenzene sulfonates. Suitable alkylbenzene sulfonates (LAS) can be obtained by sulfonating commercially available linear alkylbenzenes (LAB); suitable LAB include low 2-phenyl LAB, such as Isochem® or Petrelab®, and other suitable LAB include high 2-phenyl LAB, such as Hyblene®. Suitable anionic detersive surfactants are alkylbenzene sulfonates obtained by the DETAL catalytic process, but other synthetic routes (such as HF) can also be suitable. In one aspect, the magnesium salt of LAS is used.

[0116] Suitable sulfate detersive surfactants include alkyl sulfates, in one aspect C 8-18 alkyl sulfates, or mainly C 12 alkyl sulfates.

[0117] Another suitable sulfate detersive surfactant is alkyl alkoxylated sulfate, in one aspect alkyl ethoxylated sulfate, in one aspect C 8-18 alkyl alkoxylated sulfate, in another aspect C 8-18Alkyl ethoxysulfates, typically alkyl alkoxysulfates having an average degree of alkoxylation from 0.5 to 20 or from 0.5 to 10, typically alkyl alkoxysulfates are C 8-18 Alkyl ethoxysulfates having an average degree of ethoxylation from 0.5 to 10, from 0.5 to 7, from 0.5 to 5 or from 0.5 to 3.

[0118] Alkyl sulfates, alkyl alkoxysulfates and alkylbenzene sulfonates can be straight-chain or branched-chain, substituted or unsubstituted.

[0119] The detersive surfactant can be a mid-chain branched detersive surfactant, in one aspect a mid-chain branched anionic detersive surfactant, in one aspect a mid-chain branched alkyl sulfate and / or mid-chain branched alkylbenzene sulfonate, such as mid-chain branched alkyl sulfate. In one aspect, the mid-chain branch is C 1-4 Alkyl groups, typically methyl and / or ethyl groups.

[0120] Non-limiting examples of anionic surfactants include sulfates and sulfonates, especially linear alkylbenzene sulfonates (LAS), isomers of LAS, branched alkylbenzene sulfonates (BABS), phenylalkane sulfonates, alpha-olefin sulfonates (AOS), olefin sulfonates, alkenyl sulfonates, alkane-2,3-diyl bis(sulfates), hydroxyalkane sulfonates and disulfonates, alkyl sulfates (AS) (such as sodium dodecyl sulfate (SDS) or sodium lauryl sulfate (SLS)), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), alcohol ether sulfates (AES or AEOS or FES, also known as alcohol ethoxysulfates or fatty alcohol ether sulfates), sodium lauryl ether sulfate (SLES), secondary alkane sulfonates (SAS), paraffin hydrocarbon sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerides, alpha-sulfofatty acid methyl esters (alpha-SFMe or SES) (including methyl ester sulfonate (MES)), alkyl succinic acids or alkenyl succinic acids, dodecenyl / tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, sulfosuccinic acids or diesters and monoesters of soaps, and combinations thereof.

[0121] Suitable nonionic detersive surfactants are selected from the group consisting of: C8-C 18 Alkyl ethoxylates, such as NEODOL®; C6-C 12 Alkylphenol alkoxylates, where these alkoxylate units can be ethyleneoxy units, propyleneoxy units or mixtures thereof; C 12 -C 18 Alcohols and C6-C 12 Condensates of alkylphenols with ethylene oxide / propylene oxide block polymers, such as Pluronic®; C 14 -C22 Medium-chain branched alcohols; C 14 -C 22 Medium-chain branched alkyl alkoxylates, typically having an average degree of alkoxylation from 1 to 30; alkyl polysaccharides, in one aspect alkyl polyglycosides; polyhydroxy fatty acid amides; ether-capped poly(alkoxylated) alcohol surfactants; and mixtures thereof.

[0122] Suitable nonionic detersive surfactants include alkyl polyglycosides and / or alkyl alkoxylated alcohols.

[0123] In one aspect, the nonionic detersive surfactant includes alkyl alkoxylated alcohols, in one aspect C 8-18 Alkyl alkoxylated alcohols (e.g., C 8-18 alkyl ethoxylated alcohols), which alkyl alkoxylated alcohols can have an average degree of alkoxylation from 1 to 50, from 1 to 30, from 1 to 20, or from 1 to 10. In one aspect, the alkyl alkoxylated alcohol can be C 8-18 alkyl ethoxylated alcohols, having an average degree of ethoxylation from 1 to 10, from 1 to 7, more typically from 1 to 5 or from 3 to 7. The alkyl alkoxylated alcohols can be straight-chain or branched-chain, and substituted or unsubstituted. Suitable nonionic surfactants include Lutensol®.

[0124] Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO) (such as linear alcohol (C12-15) ethoxylate (LAE)), alcohol propoxylates, propoxylated fatty alcohols (PFA), alkoxylated fatty acid alkyl esters (such as ethoxylated and / or propoxylated fatty acid alkyl esters), alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkyl polyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides (GA), or fatty acid glucamides (FAGA)), and products available under the trade names SPAN and TWEEN, and combinations thereof.

[0125] Suitable cationic detersive surfactants include alkyl pyridinium compounds, alkyl quaternary ammonium compounds, alkyl quaternary phosphonium compounds, alkyl trisulfonium compounds and mixtures thereof.

[0126] Suitable cationic detersive surfactants are quaternary ammonium compounds having the following general formula: (R)(R1)(R2)(R3)N + X - wherein R is a straight-chain or branched-chain, substituted or unsubstituted C 6-18an alkyl or alkenyl moiety, R1 and R2 are independently selected from methyl or ethyl moieties, R3 is a hydroxy, hydroxymethyl or hydroxyethyl moiety, X is an anion that provides charge neutrality, suitable anions include halides such as chloride; sulfates; and sulfonates. Suitable cationic detersive surfactants are mono-C 6-18 alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride. Highly suitable cationic detersive surfactants are mono-C 8-10 alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride, mono-C 10-12 alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride and mono-C 10 alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride.

[0127] Non-limiting examples of cationic surfactants include alkyldimethyl ethanolamine quaternary (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quaternaries, and combinations thereof.

[0128] Suitable amphoteric surfactants / zwitterionic surfactants include amine oxides and betaines (such as alkyldimethyl betaine, sulfobetaine), or combinations thereof. The amine-neutralized anionic surfactants - anionic surfactants and auxiliary anionic co-surfactants can be present in acid form, and the acid form can be neutralized to form the surfactant salts desired for use in the detergent compositions of the present invention. Typical reagents for neutralization include metal counterion bases such as hydroxides, such as NaOH or KOH. Additional preferred reagents for neutralizing the anionic surfactants of the present invention and the auxiliary anionic co-surfactants or co-surfactants in their acid form include ammonia, amines, or alkanolamines. Alkanolamines are preferred. Suitable non-limiting examples include monoethanolamine, diethanolamine, triethanolamine, and other straight-chain or branched alkanolamines known in the art; for example, highly preferred alkanolamines include 2-amino-1-propanol, 1-aminopropanol, monoisopropanolamine, or 1-amino-3-propanol. The amine neutralization can be carried out to a complete or partial extent, for example, a portion of the anionic surfactant mixture can be neutralized with sodium or potassium, and a portion of the anionic surfactant mixture can be neutralized with an amine or alkanolamine.

[0129] Non-limiting examples of semi-polar surfactants include amine oxides (AO), such as alkyldimethylamine oxide.

[0130] Surfactant systems comprising a mixture of one or more anionic surfactants, and one or more additional nonionic surfactants, and optionally additional surfactants such as cationic surfactants may be preferred. Preferred weight ratios of anionic to nonionic surfactants are at least 2:1, or at least 1:1 to 1:10.

[0131] In one aspect, the surfactant system may include a mixture of isoprenoid surfactants represented by Formula A and Formula B:

[0132]

[0133]

[0134] wherein Y is CH2 or absent, and Z can be selected such that the resulting surfactant is selected from the group consisting of: alkyl carboxylate surfactants, alkyl polyalkoxy surfactants, alkyl anionic polyalkoxy sulfate surfactants, alkyl glycerol sulfonate surfactants, alkyl dimethylamine oxide surfactants, alkyl polyhydroxy-based surfactants, alkyl phosphate surfactants, alkyl glycerol sulfonate surfactants, alkyl polygluconate surfactants, alkyl polyphosphate surfactants, alkyl phosphonate surfactants, alkyl polyglycoside surfactants, alkyl monoglycoside surfactants, alkyl diglycoside surfactants, alkyl sulfosuccinate surfactants, alkyl disulfate surfactants, alkyl disulfonate surfactants, alkyl sulfonated succinamate surfactants, alkyl glucamide surfactants, alkyl taurate surfactants, alkyl sarcosinate surfactants, alkyl glycinate surfactants, alkyl hydroxyethylsulfonate surfactants, alkyl diethanolamide surfactants, alkyl monoethanolamide surfactants, alkyl monoethanolamide sulfate surfactants, alkyl dihydroxyacetamide surfactants, alkyl dihydroxyacetamide sulfate surfactants, alkyl glycerol ester surfactants, alkyl glycerol ester sulfate surfactants, alkyl glycerol ether surfactants, alkyl glycerol ether sulfate surfactants, alkyl methyl ester sulfonate surfactants, alkyl polyglycerol ether surfactants, alkyl polyglycerol ether sulfate surfactants, alkyl sorbitan ester surfactants, alkyl aminoalkane sulfonate surfactants, alkyl amidopropyl betaine surfactants, alkyl allylated quaternary ammonium salt-based surfactants, alkyl mono-hydroxyalkyl-di-alkylated quaternary ammonium salt-based surfactants, alkyl di-hydroxyalkyl monoalkyl quaternary ammonium salt-based surfactants, alkylated quaternary ammonium salt surfactants, alkyl trimethylammonium quaternary ammonium salt surfactants, alkyl polyhydroxyalkyloxypropyl quaternary ammonium salt-based surfactants, alkyl glycerol ester quaternary ammonium salt surfactants, alkyl ethylene glycolamine quaternary ammonium salt surfactants, alkyl monomethyldihydroxyethyl quaternary surfactants, alkyl dimethylmonohydroxyethyl quaternary surfactants, alkyl trimethylammonium surfactants, alkyl imidazoline-based surfactants, olefin-2-yl-succinate surfactants, alkyl α-sulfonated carboxylic acid surfactants, alkyl α-sulfonated carboxylic acid alkyl ester surfactants, α-olefin sulfonate surfactants, alkyl phenol ethoxylate surfactants, alkyl benzene sulfonate surfactants, alkyl sulfobetaine surfactants, alkyl hydroxy sulfobetaine surfactants, alkyl ammonium carboxylate betaine surfactants, alkyl sucrose ester surfactants, alkyl alkanolamide surfactants, alkyl di(polyethylene oxide) monoalkylammonium surfactants, alkyl mono(polyethylene oxide) dialkylammonium surfactants, alkyl benzyl dimethylammonium surfactants, alkyl aminopropionate surfactants, alkyl amidopropyl dimethylamine surfactants, or mixtures thereof;And if Z is an electrically charged moiety, Z is charge balanced by a suitable metal or organic counterion. Suitable counterions include metal counterions, amines, or alkanolamines such as C1-C6 alkanolammonium. More specifically, suitable counterions include Na+, Ca+, Li+, K+, Mg+, such as monoethanolamine (MEA), diethanolamine (DEA), triethanolamine (TEA), 2-amino-1-propanol, 1-aminopropanol, methyldiethanolamine, dimethylethanolamine, monoisopropanolamine, triisopropanolamine, 1-amino-3-propanol, or mixtures thereof. In one embodiment, the composition contains from 5% to 97% of one or more non-isoprenoid surfactants; and one or more auxiliary cleaning additives; wherein the weight ratio of the surfactant of formula A to the surfactant of formula B is 50:50 to 95:5.;

[0135] In a preferred embodiment, the composition of the present invention comprises one or more anionic surfactants and / or one or more nonionic surfactants.

[0136] In an embodiment, the composition comprises one or more anionic surfactants, preferably linear alkylbenzene sulfonic acid (LAS), alcohol ether sulfate (AEOS) and / or alkyl sulfate (AS), especially sodium lauryl sulfate (SLS) and / or sodium laureth sulfate (SLES).

[0137] In an embodiment, the composition comprises one or more nonionic surfactants, preferably alcohol ethoxylates (AEO), especially linear alcohol (C12-15) ethoxylates.

[0138] In an embodiment, the composition comprises one or more anionic surfactants and one or more nonionic surfactants.

[0139] In an embodiment, the composition comprises the anionic surfactant linear alkylbenzene sulfonic acid (LAS) and the nonionic surfactant alcohol ethoxylate (AEO).

[0140] In an embodiment, the surfactant system comprises LAS, SLES, AS and AEO.

[0141] In an embodiment, the surfactant system comprises LAS, SLES and AEO.

[0142] In an embodiment, the ratio between the anionic surfactant and the nonionic surfactant is in the range of 20:1 to 1:1, such as 15:1 to 10:1, especially about 4:1.

[0143] In a specific embodiment, the surfactant system is the standard detergent J described in the examples.

[0144] The non-limiting list of composition components set forth below is suitable for use in the compositions and methods of the present invention and may desirably be incorporated into certain embodiments of the present invention, e.g., to assist or enhance fat removal and cleaning performance, for treating substrates to be cleaned, or to modify the aesthetics of the composition in conjunction with fragrances, colorants, dyes, etc. The level of any such component incorporated into any composition is in addition to any materials previously cited for incorporation. The exact nature of these additional components and their level of incorporation will depend on the physical form of the composition and the nature of the cleaning operation in which the composition will be used. Although the components mentioned below are classified by general headings according to specific functionality, this is not to be construed as limiting, since as will be understood by one of ordinary skill in the art, a component may contain additional functionality.

[0145] Unless otherwise indicated, amounts are by weight of the composition (wt%). Suitable component materials include, but are not limited to, surfactants, builders, chelating agents, dye transfer inhibitors, dispersants, enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric dispersants, clay removal / antiredeposition agents, brighteners, foam inhibitors, dyes, color dyes, fragrances, fragrance delivery systems, structurants, fabric softeners, carriers, hydrotropes, processing aids, solvents, and / or pigments. Suitable examples and levels of use of such other components, in addition to the disclosures below, are found in US 5576282, US 6306812, and US 6326348, which are hereby incorporated by reference.

[0146] Thus, in certain embodiments, the compositions of the present invention do not contain one or more of the following adjunct materials: surfactants, soaps, builders, chelating agents, dye transfer inhibitors, dispersants, additional enzymes, enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric dispersants, clay removal / antiredeposition agents, brighteners, foam inhibitors, dyes, fragrances, fragrance delivery systems, structurants, fabric softeners, carriers, hydrotropes, processing aids, solvents, and / or pigments. However, when one or more components are present, such one or more components may be present as detailed below:

[0147] Soap

[0148] The compositions of the present invention may also contain soaps. Without being bound by theory, it may be desirable to include soaps as they act in part as surfactants and in part as builders, and can be used to inhibit foaming, and furthermore, can advantageously interact with the various cationic compounds of the composition to enhance the softness of textile fabrics treated with the compositions of the present invention. Any soap known in the art for use in laundry detergents can be utilized. In one embodiment, the composition contains from 0 wt% to 20 wt%, from 0.5 wt% to 20 wt%, from 4 wt% to 10 wt%, or from 4 wt% to 7 wt% of soap.

[0149] Examples of soaps useful herein include soaps of oleic acid, palmitic acid, palm kernel fatty acids, and mixtures thereof. Typical soaps are in the form of mixtures of fatty acid soaps with different chain lengths and degrees of substitution. One such mixture is topped palm kernel fatty acid.

[0150] In one embodiment, the soap is selected from free fatty acids. In a preferred embodiment, the composition comprises coco fatty acids. Other suitable fatty acids are saturated and / or unsaturated and can be obtained from natural sources such as vegetable or animal esters (e.g., palm kernel oil, palm oil, coconut oil, babassu oil, safflower oil, tall oil, castor oil, tallow, and fish oil, fats, and mixtures thereof), or prepared synthetically (e.g., via oxidation of petroleum or via the Fischer Tropsch process of hydrogenating carbon monoxide).

[0151] Examples of suitable saturated fatty acids for use in the compositions of the present invention include capric acid, lauric acid, myristic acid, palmitic acid, stearic acid, arachidic acid, and behenic acid. Suitable classes of unsaturated fatty acids include: palmitoleic acid, oleic acid, linoleic acid, linolenic acid, and ricinoleic acid. Examples of preferred fatty acids are saturated Cn fatty acids, saturated Ci2-Ci4 fatty acids, and saturated or unsaturated Cn to Ci8 fatty acids and mixtures thereof.

[0152] When present, the weight ratio of the fabric softening cationic co-surfactant to the fatty acid is preferably from about 1:3 to about 3:1, more preferably from about 1:1.5 to about 1.5:1, and most preferably about 1:1.

[0153] The levels of soaps and non-soap anionic surfactants herein are specified as percentages by weight of the detergent composition on an acid basis. However, as is commonly understood in the art, in practice, sodium, potassium, or alkanolammonium bases such as sodium hydroxide or monoethanolamine are used to neutralize the anionic surfactants and soaps.

[0154] Hydrotropic agent

[0155] The composition of the present invention may further comprise one or more hydrotropes. A hydrotrope is a compound that dissolves hydrophobic compounds in an aqueous solution (or conversely, polar substances in a non-polar environment). Typically, hydrotropes have both hydrophilic and hydrophobic characteristics (so-called amphiphilic properties, as known for surfactants); however, the molecular structure of hydrotropes generally does not favor spontaneous self-aggregation, see for example the review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not exhibit a critical concentration above which self-aggregation, as found for surfactants, and the formation of micelles, lamellae, or other well-defined intermediate phases occur. Instead, many hydrotropes exhibit a continuous type of aggregation process in which the size of the aggregates grows with increasing concentration. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances with polar and non-polar characteristics (including mixtures of water, oil, surfactants, and polymers). Hydrotropes are routinely used in various industries ranging from pharmaceuticals, personal care, food to technical applications. The use of hydrotropes in detergent compositions allows, for example, more concentrated surfactant formulations (such as in the process of compressing liquid detergents by removing water) without causing undesirable phenomena such as phase separation or high viscosity.

[0156] The detergent composition of the present invention may contain from 0 wt% to 10 wt%, for example from 0 wt% to 5 wt%, 0.5 wt% to 5 wt%, or from 3 wt% to 5 wt% of a hydrotrope. Any hydrotrope known in the art for use in detergents can be utilized. Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluenesulfonate (STS), sodium xylenesulfonate (SXS), sodium cumenesulfonate (SCS), sodium cymenesulfonate, amine oxides, alcohols and polyethylene glycol ethers, sodium hydroxynaphthoate, sodium hydroxynaphthalenesulfonate, sodium 2-ethylhexylsulfonate, and combinations thereof.

[0157] Builder

[0158] The composition of the present invention may further comprise one or more builders, cobuilders, builder systems or mixtures thereof. When a builder is used, the cleaning composition will typically comprise from 0 wt% to 65 wt%, at least 1 wt%, from 2 wt% to 60 wt% or from 5 wt% to 10 wt% of the builder. In dishwashing cleaning compositions, the level of the builder is typically 40 wt% to 65 wt% or 50 wt% to 65 wt%. The composition may be substantially free of builders; substantially free means "without intentional addition" of zeolites and / or phosphates. Typical zeolite builders include zeolite A, zeolite P and zeolite MAP. A typical phosphate builder is sodium tripolyphosphate.

[0159] The builder and / or cobuilder may in particular be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and / or cobuilder known in the art for use in detergents may be used. Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium tripolyphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Hoechst), ethanolamines (e.g., 2-aminoethan-1-ol (MEA), iminodiethanol (DEA) and tris(2-hydroxyethyl)amine (TEA)), and carboxymethyl inulin (CMI), and combinations thereof.

[0160] The composition may include a cobuilder alone or in combination with a builder (such as a zeolite builder). Non-limiting examples of cobuilders include homopolymers or copolymers of polyacrylates, such as poly(acrylic acid) (PAA) or copoly(acrylic acid / maleic acid) (PAA / PMA). Additional non-limiting examples include citrates, chelating agents (such as aminocarboxylates, aminopolycarboxylates, and phosphonates), and alkyl succinates or alkenyl succinates. Further specific examples include nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic acid (IDS), ethylenediamine-N,N'-disuccinic acid (EDDS), methylglycine diacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diylbis(phosphonic acid) (HEDP), ethylenediaminetetra(methylene)tetrakis(phosphonic acid) (EDTMPA), diethylenetriaminepenta(methylene)pentakis(phosphonic acid) (DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-alanine-N,N-diacetic acid (α-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), sulfanilic acid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA), and sulfomethyl-N,N-diacetic acid (SMDA), N-(hydroxyethyl)-ethylenediaminetriacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Additional exemplary builders and / or cobuilders are described, for example, in WO 09 / 102854, US 5977053.

[0161] Chelating agent and crystal growth inhibitor

[0162] The composition of the present invention may further comprise a chelating agent and / or a crystal growth inhibitor. Suitable molecules include copper, ion and / or manganese chelating agents and mixtures thereof. Suitable molecules include DTPA (diethylenetriaminepentaacetic acid), HEDP (hydroxyethanediphosphonic acid), DTPMP (diethylenetriaminepenta(methylenephosphonic acid)), disodium 1,2-dihydroxybenzene-3,5-disulfonate hydrate, ethylenediamine, diethylenetriamine, ethylenediaminedisuccinic acid (EDDS), N-hydroxyethylethylenediaminetriacetic acid (HEDTA), triethylenetetraminehexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrapropionic acid (EDTP), carboxymethyl inulin, and 2-phosphonobutane 1,2,4-tricarboxylic acid (Bayhibit® AM) and its derivatives. Typically, the composition may comprise from 0.005 wt% to 15 wt%, or from 3.0 wt% to 10 wt% of a chelating agent or a crystal growth inhibitor.

[0163] Bleaching component

[0164] The composition of the present invention may further comprise a bleaching component. Suitable bleaching components for incorporation into the composition of the present invention or for use in the method of the present invention include a bleaching component or a mixture of more than one bleaching component. Suitable bleaching components include bleaching catalysts, photobleaches, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, and mixtures thereof. Generally, when a bleaching component is used, the composition of the present invention may comprise from 0 wt% to 30 wt%, from 0.00001 wt% to 90 wt%, 0.0001 wt% to 50 wt%, from 0.001 wt% to 25 wt%, or from 1 wt% to 20 wt%. Examples of suitable bleaching components include:

[0165] (1) Preformed peracids: Suitable preformed peracids include, but are not limited to, compounds selected from the group consisting of preformed peroxyacids or salts thereof, typically peroxycarboxylic acids or salts thereof, or peroxymonosulfuric acid or salts thereof.

[0166] The preformed peroxyacid or salt thereof is preferably a peroxycarboxylic acid or salt thereof, typically having a chemical structure corresponding to the following chemical formula:

[0167]

[0168] wherein: R 14 is selected from alkyl, aralkyl, cycloalkyl, aryl or heterocyclic groups; R 14 groups may be straight-chain or branched, substituted or unsubstituted; and Y is any suitable counterion that achieves charge neutrality, preferably, Y is selected from hydrogen, sodium or potassium. Preferably, R 14is a straight-chain or branched-chain, substituted or unsubstituted C 6-9 alkyl. Preferably, the peroxyacid or its salt is selected from peroxyhexanoic acid, peroxyheptanoic acid, peroxyoctanoic acid, peroxynonanoic acid, peroxydodecanoic acid, and their salts, or any combination thereof. A particularly preferred peroxyacid is phthalimido-peroxy-alkanoic acid, especially ε-phthalimidoperoxyhexanoic acid (PAP). Preferably, the peroxyacid or its salt has a melting point in the range from 30 °C to 60 °C.

[0169] The preformed peroxyacid or its salt can also be peroxymonosulfuric acid or its salt, typically having a chemical structure corresponding to the following chemical formula:

[0170]

[0171] wherein: R 15 is selected from alkyl, aralkyl, cycloalkyl, aryl or heterocyclic groups; R 15 groups can be straight-chain or branched-chain, substituted or unsubstituted; and Z is any suitable counterion to achieve charge neutrality, preferably, Z is selected from hydrogen, sodium or potassium. Preferably, R 15 is a straight-chain or branched-chain, substituted or unsubstituted C 6-9 alkyl. Preferably, such a bleaching component can be present in the composition of the present invention in an amount from 0.01 wt% to 50 wt% or from 0.1 wt% to 20 wt%.

[0172] (2) The hydrogen peroxide source includes, for example, inorganic hydrogen peroxide salt compounds, including alkali metal salts such as perborates (usually monohydrate or tetrahydrate), percarbonates, persulfates, perphosphates, sodium silicates and mixtures thereof. In one aspect of the present invention, the inorganic hydrogen peroxide salt compounds are, for example, those selected from the group consisting of: perborates, sodium percarbonates and mixtures thereof. When used, the inorganic hydrogen peroxide salt compounds are typically present in the overall composition in an amount of 0.05 wt% to 40 wt% or 1 wt% to 30 wt% and are typically incorporated into such a composition as crystalline solids that can be coated. Suitable coatings include inorganic salts such as alkali metal silicates, carbonates or borates or mixtures thereof, or organic materials such as water-soluble or water-dispersible polymers, waxes, oils or fatty soaps. Preferably, such a bleaching component can be present in the composition of the present invention in an amount of 0.01 wt% to 50 wt% or 0.1 wt% to 20 wt%.

[0173] (3) The term "bleaching activator" as used herein means a compound that reacts with hydrogen peroxide to form a peracid via a perhydrolysis reaction. The peracid thus formed constitutes an activated bleaching agent. Suitable bleaching activators to be used herein include those belonging to the classes of esters, amides, imides or acid anhydrides. Suitable bleaching activators are those having R-(C=O)-L, where R is an alkyl group (optionally branched), having from 6 to 14 carbon atoms or from 8 to 12 carbon atoms when the bleaching activator is hydrophobic, and having less than 6 carbon atoms or less than 4 carbon atoms when the bleaching activator is hydrophilic; and L is a leaving group. Examples of suitable leaving groups are benzoic acid and its derivatives - especially benzenesulfonates. Suitable bleaching activators include dodecanoyloxybenzenesulfonate, decanoyloxybenzenesulfonate, decanoyloxybenzoic acid or its salts, 3,5,5-trimethylhexanoyloxybenzenesulfonate, tetraacetylethylenediamine (TAED), sodium 4-[(3,5,5-trimethylhexanoyl)oxy]benzene-1-sulfonate (ISONOBS), 4-(dodecanoyloxy)benzene-1-sulfonate (LOBS), 4-(decanoyloxy)benzene-1-sulfonate, 4-(decanoyloxy)benzoate (DOBS or DOBA), 4-(nonanoyloxy)benzene-1-sulfonate (NOBS), and / or those disclosed in WO 98 / 17767. A family of bleaching activators is disclosed in EP 624154 and particularly preferred in that family is triethyl acetylcitrate (ATC). ATC or short-chain triglycerides such as triacetin have the advantage that they are environmentally friendly. Moreover, triethyl acetylcitrate and triacetin have good hydrolysis stability in the product during storage and are effective bleaching activators. Finally, ATC is multifunctional because the citrate released in the perhydrolysis reaction can act as a builder. Alternatively, the bleaching system can comprise, for example, peroxyacids of the amide, imide or sulfone type. The bleaching system can also comprise peracids such as 6-(phthalimido)perhexanoic acid (PAP). Suitable bleaching activators are also disclosed in WO 98 / 17767. Although any suitable bleaching activator can be employed, in one aspect of the present invention, the subject cleaning composition can comprise NOBS, TAED or a mixture thereof. When present, the peracid and / or bleaching activator is generally present in the composition in an amount of 0.1 wt% to 60 wt%, 0.5 wt% to 40 wt% or 0.6 wt% to 10 wt% based on the fabric and home care composition. One or more hydrophobic peracids or their precursors can be used in combination with one or more hydrophilic peracids or their precursors. Preferably, such bleaching components can be present in the composition of the present invention in an amount of 0.01 wt% to 50 wt% or 0.1 wt% to 20 wt%.

[0174] The amounts of hydrogen peroxide source and peracid or bleach activator may be selected so that the molar ratio of available oxygen (from the peroxide source) to peracid is from 1:1 to 35:1, or even 2:1 to 10:1.

[0175] (4) Diacyl Peroxides - Preferred diacyl peroxide bleaching species include those selected from the group consisting of diacyl peroxides having the general formula: R 1 -C(O)-OO-(O)CR 2 , where R 1 Indicates C6-C 18 An alkyl group, preferably a straight chain having at least 5 carbon atoms and optionally containing one or more substituents (e.g. -N + (CH3)3, -COOH or -CN) and / or one or more interrupting moieties (e.g., -CONH- or -CH=CH-) inserted between adjacent carbon atoms of the alkyl group. 12 alkyl group, and R 2 represents an aliphatic group that is compatible with the peroxide portion so that R 1 and R 2 Together, they contain a total of 8 to 30 carbon atoms. In a preferred aspect, R 1 and R 2 It is a straight chain unsubstituted C6-C 12 Most preferably, R 1 and R 2 are the same. Diacyl peroxide (where R 1 and R 2 All are C6-C 12 alkyl groups) are particularly preferred. Preferably, at least one of the R groups (R1 or R2), most preferably only one, does not contain a branched ring or a side group ring at the α position, or preferably does not contain a branched ring or a side group ring at either the α position or the β position, or most preferably does not contain a branched ring or a side group ring at either the α position, the β position, or the γ position. In a further preferred embodiment, the DAP may be asymmetric, such that the R1 acyl group preferably hydrolyzes rapidly to produce a peracid, but the R2 acyl group hydrolyzes slowly.

[0176] The tetraacyl peroxide bleaching species is preferably selected from tetraacyl peroxides of the general formula: R 3 -C(O)-OO-C(O)-(CH2)nC(O)-OO-C(O)-R 3 , where R 3 represents a C1-C9 alkyl group or a C3-C7 group, and n represents an integer from 2 to 12 or 4 to 10 both inclusive.

[0177] Preferably, the diacyl and / or tetraacyl peroxide bleaching species are present in an amount sufficient to provide at least 0.5 ppm, at least 10 ppm, or at least 50 ppm by weight of the wash liquor. In a preferred embodiment, the bleaching species are present in an amount sufficient to provide from 0.5 ppm to 300 ppm, from 30 ppm to 150 ppm by weight of the wash liquor.

[0178] Preferably, the bleaching composition comprises a bleaching catalyst (5 and 6).

[0179] (5) Preferred are organic (non-metallic) bleaching catalysts including bleaching catalysts capable of accepting an oxygen atom from a peroxyacid and / or its salt and transferring the oxygen atom to an oxidizable substrate. Suitable bleaching catalysts include, but are not limited to: iminium cations and polyions; iminium zwitterions; modified amines; modified amine oxides; N-sulfonylimines; N-phosphonylimines; N-acylimines; thiadiazole dioxides; perfluoroimines; cyclic glyoxals and mixtures thereof.

[0180] Suitable iminium cations and polyions include, but are not limited to, N-methyl-3,4-dihydroisoquinolinium tetrafluoroborate, prepared as described in Tetrahedron (1992), 49(2), 423-38 (e.g., compound 4, page 433); N-methyl-3,4-dihydroisoquinolinium p-toluenesulfonate, prepared as described in US 5360569 (e.g., column 11, example 1); and n-octyl-3,4-dihydroisoquinolinium p-toluenesulfonate, prepared as described in US 5360568 (e.g., column 10, example 3).

[0181] Suitable iminium zwitterions include, but are not limited to, N-(3-sulfopropyl)-3,4-dihydroisoquinolinium, inner salt, prepared as described in US 5576282 (e.g., column 31, example II); N-[2-(sulfonyloxy)dodecyl]-3,4-dihydroisoquinolinium, inner salt, prepared as described in US 5817614 (e.g., column 32, example V); 2-[3-[(2-ethylhexyl)oxy]-2-(sulfonyloxy)propyl]-3,4-dihydroisoquinolinium, inner salt, prepared as described in WO 05 / 047264 (e.g., page 18, example 8), and 2-[3-[(2-butyloctyl)oxy]-2-(sulfonyloxy)propyl]-3,4-dihydroisoquinolinium, inner salt.

[0182] Suitable modified amine oxygen transfer catalysts include, but are not limited to, 1,2,3,4-tetrahydro-2-methyl-1-isoquinolinol, which can be prepared according to the procedures described in Tetrahedron Letters (1987), 28(48), 6061-6064. Suitable modified amine oxide oxygen transfer catalysts include, but are not limited to, sodium 1-hydroxy-N-oxido-N-[2-(sulphonyloxy)decyl]-1,2,3,4-tetrahydroisoquinoline.

[0183] Suitable N-sulfonyl imine oxygen transfer catalysts include, but are not limited to, 3-methyl-1,2-benzisothiazole 1,1-dioxide, which is prepared according to the procedures described in Journal of Organic Chemistry (1990), 55(4), 1254-61.

[0184] Suitable N-phosphonyl imine oxygen transfer catalysts include, but are not limited to, [R-(E)]-N-[(2-chloro-5-nitrophenyl)methylene]-p-phenyl-p-(2,4,6-trimethylphenyl)phosphinic amide, which can be prepared according to the procedures described in Journal of the Chemical Society, Chemical Communications (1994),(22), 2569-70.

[0185] Suitable N-acyl imine oxygen transfer catalysts include, but are not limited to, [N(E)]-N-(phenylmethylene)acetamide, which can be prepared according to the procedures described in Polish Journal of Chemistry (2003), 77(5), 577-590.

[0186] Suitable thiadiazole dioxide oxygen transfer catalysts include, but are not limited to, 3-methyl-4-phenyl-1,2,5-thiadiazole 1,1-dioxide, which can be prepared according to the procedures described in US 5753599 (column 9, example 2).

[0187] Suitable perfluoro imine oxygen transfer catalysts include, but are not limited to, (Z)-2,2,3,3,4,4,4-heptafluoro-N-(nonafluorobutyl)butanimide fluoride, which can be prepared according to the procedures described in Tetrahedron Letters (1994), 35(34), 6329-30.

[0188] Suitable cyclic glyconate oxygen transfer catalysts include, but are not limited to, 1,2:4,5-di-O-isopropylidene-D-erythro-2,3-hexodiulose-2,6-pyranose (hexodiuro), as prepared in US 6649085 (column 12, example 1).

[0189] Preferably, the bleaching catalyst comprises an iminium ion and / or a carbonyl functional group, and typically is capable of forming an oxaziridinium and / or a dioxirane functional group after accepting an oxygen atom, especially from a peroxyacid and / or its salt. Preferably, the bleaching catalyst comprises an oxaziridinium functional group and / or is capable of forming an oxaziridinium functional group upon accepting an oxygen atom, especially upon accepting an oxygen atom from a peroxyacid and / or its salt. Preferably, the bleaching catalyst comprises a cyclic iminium ion functional group, preferably wherein the cyclic moiety has a ring size of from five to eight atoms (including the nitrogen atom), preferably six atoms. Preferably, the bleaching catalyst comprises an aryliminium ion functional group, preferably a bicyclic arylimine functional group, preferably a 3,4-dihydroisoquinolinium functional group. Typically, the imine functional group is a quaternary imine functional group and typically is capable of forming a quaternary oxaziridinium functional group upon accepting an oxygen atom, especially upon accepting an oxygen atom from a peroxyacid and / or its salt. In another aspect, the detergent composition comprises a bleaching component having a logP o / w not greater than 0, not greater than -0.5, not greater than -1.0, not greater than -1.5, not greater than -2.0, not greater than -2.5, not greater than -3.0, or not greater than -3.5. The method for determining logP o / w is described in more detail below.

[0190] Typically, the bleaching component is capable of generating a bleaching species having an X SO of from 0.01 to 0.30, from 0.05 to 0.25, or from 0.10 to 0.20. The method for determining X SO is described in more detail below. For example, a bleaching component having an isoquinolinium structure is capable of generating a bleaching species having an oxaziridinium structure. In this example, X SO is the X SO of the oxaziridinium bleaching species.

[0191] Preferably, the bleaching catalyst has a chemical structure corresponding to the following chemical formula:

[0192]

[0193] wherein: n and m are independently 0 to 4, preferably both n and m are 0; each R 1Independently selected from substituted or unsubstituted groups selected from the group consisting of: hydrogen, alkyl, cycloalkyl, aryl, fused aryl, heterocycle, fused heterocycle, nitro, halo, cyano, sulfonate, alkoxy, keto, carboxyl, and alkoxycarbonyl groups; and any two adjacent Rs 1 Substituents may combine to form a fused aryl, fused carbocycle, or fused heterocycle; each R 2 Independently selected from substituted or unsubstituted groups independently selected from the group consisting of: hydrogen, hydroxy, alkyl, cycloalkyl, alkaryl, aryl, aralkyl, alkylene, heterocycle, alkoxy, arylcarbonyl, carboxyalkyl, and amide groups; any R 2 May combine with any other R 2 To form part of a common ring; any geminal Rs 2 May combine to form a carbonyl; and any two Rs 2 May combine to form a substituted or unsubstituted fused unsaturated moiety; R 3 Is a C1 to C 20 Substituted or unsubstituted alkyl; R 4 Is hydrogen or the -A moiety of Q t , where: Q is branched or unbranched alkylene, t = 0 or 1, and A is an anionic group selected from the group consisting of OSO3 - , SO3 - , CO2 - , OCO2 - , OPO3 2- , OPO3H - And OPO2 - ; R 5 Is hydrogen or the moiety -CR 11 R 12 -Y-G b -Y c -[(CR 9 R 10 ) y -O] k -R 8 , where: each Y is independently selected from the group consisting of O, S, N-H, or N-R 8 ; and each R 8 Is independently selected from the group consisting of alkyl, aryl, and heteroaryl, the moiety being substituted or unsubstituted, and whether substituted or unsubstituted, the moiety has less than 21 carbons; each G is independently selected from the group consisting of CO, SO2, SO, PO, and PO2; R 9 And R 10 Are independently selected from the group consisting of H and C1-C4 alkyl; R 11 And R 12Independently selected from the group consisting of: H and alkyl, or when taken together can combine to form a carbonyl group; b = 0 or 1; c can = 0 or 1, but if b = 0, c must = 0; y is an integer from 1 to 6; k is an integer from 0 to 20; R 6 is H, or an alkyl, aryl or heteroaryl moiety; said moieties are substituted or unsubstituted; and if X is present, it is a suitable charge balancing counterion, preferably present when R 4 is hydrogen, suitable X includes but is not limited to: chloride, bromide, sulfate, methylsulfate, sulfonate, p-toluenesulfonate, tetrafluoroborate and phosphate.

[0194] In one embodiment of the present invention, the bleaching catalyst has a structure corresponding to the following general formula:

[0195]

[0196] wherein R 13 is a branched alkyl group containing from three to 24 carbon atoms (including branched carbon atoms) or a straight-chain alkyl group containing from one to 24 carbon atoms; preferably, R 13 is a branched alkyl group containing from eight to 18 carbon atoms or a straight-chain alkyl group containing from eight to eighteen carbon atoms; preferably, R 13 is selected from the group consisting of: 2-propylheptyl, 2-butyl octyl, 2-pentyl nonyl, 2-hexyl decyl, n-dodecyl, n-tetradecyl, n-hexadecyl, n-octadecyl, isononyl, isodecyl, isotridecyl and isopentadecyl; preferably, R 13 is selected from the group consisting of: 2-butyl octyl, 2-pentyl nonyl, 2-hexyl decyl, isotridecyl and isopentadecyl.

[0197] Preferably, in addition to the bleaching catalyst, especially the organic bleaching catalyst, the bleaching component further comprises a peracid source. The peracid source can be selected from (a) preformed peracids; (b) percarbonates, perborates or persulfates (hydrogen peroxide sources), preferably in combination with a bleach activator; and (c) perhydrolases and esters for in-situ formation of peracids in the presence of water in textile or hard surface treatment steps.

[0198] When present, based on the composition, the peracid and / or bleach activator is generally present in the composition in an amount from 0.1 wt% to 60 wt%, from 0.5 wt% to 40 wt% or from 0.6 wt% to 10 wt%. One or more hydrophobic peracids or their precursors can be used in combination with one or more hydrophilic peracids or their precursors.

[0199] The amounts of hydrogen peroxide source and peracid or bleach activator can be selected such that the molar ratio of available oxygen (from the peroxide source) to peracid is from 1:1 to 35:1, or 2:1 to 10:1.

[0200] (6) Metal-containing bleach catalysts - The bleaching component can be provided by a catalytic metal complex. One type of metal-containing bleach catalyst is a catalytic system that includes transition metal cations having a defined bleaching catalytic activity (such as copper, iron, titanium, ruthenium, tungsten, molybdenum, or manganese cations), auxiliary metal cations having little or no bleaching catalytic activity (such as zinc or aluminum cations), and a sequestering agent having a defined stability constant for the catalytic and auxiliary metal cations, in particular ethylenediaminetetraacetic acid, ethylenediamine tetra(methylenephosphonic acid), and their water-soluble salts. Such catalysts are disclosed in US 4430243. Preferred catalysts are described in WO 09 / 839406, US 6218351, and WO 00 / 012667. Particularly preferred are transition metal catalysts or ligands that are polydentate N-donor ligands as crosslinking bridges.

[0201] If desired, the compositions herein can be catalyzed by means of manganese compounds. Such compounds and levels of use are well known in the art and include, for example, the manganese-based catalysts disclosed in US 5576282.

[0202] Cobalt bleach catalysts useful herein are known and are described, for example, in US 5597936; US 5595967. Such cobalt catalysts can be readily prepared by known procedures, such as those taught in US 5597936 and US 5595967.

[0203] The compositions herein can also suitably include transition metal complexes of ligands, such as bispidone (US 7501389) and / or mostly polycyclic rigid ligands - abbreviated as "MRL". As a practical matter and not by way of limitation, the compositions and methods herein can be adjusted to provide at least about one part per hundred million of the active MRL species in an aqueous washing medium and will typically provide from 0.005 ppm to 25 ppm, from 0.05 ppm to 10 ppm, or from 0.1 ppm to 5 ppm of MRL in the wash liquor.

[0204] Suitable transition metals in the transition metal bleach catalysts of the present invention include, for example, manganese, iron, and chromium. Suitable MRLs include 5,12 - diethyl - 1,5,8,12 - tetraazabicyclo[6.6.2]hexadecane. Suitable transition metal MRLs can be readily prepared by known procedures, such as those taught in US 6225464 and WO 00 / 32601.

[0205] (7) Optical bleaches - Suitable optical bleaches include, for example, sulfonated zinc phthalocyanine, sulfonated aluminum phthalocyanine, xanthene dyes, and mixtures thereof. Preferred bleaching components for use in the compositions of the present invention comprise a hydrogen peroxide source, a bleach activator, and / or an organic peroxyacid, optionally generated in situ by the reaction of the hydrogen peroxide source and the bleach activator in combination with a bleach catalyst. Preferred bleaching components comprise a bleach catalyst, preferably an organic bleach catalyst as described above.

[0206] Particularly preferred bleaching components are bleach catalysts, especially organic bleach catalysts.

[0207] Exemplary bleaching systems are also described, for example, in WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259, and WO 2007 / 087242.

[0208] Fabric toner

[0209] The compositions of the present invention may also contain fabric colorants. Suitable fabric colorants include dyes, dye - clay conjugates, and pigments. Suitable dyes include small - molecule dyes and polymeric dyes. Suitable small - molecule dyes include small - molecule dyes selected from the group consisting of dyes belonging to the following Color Index (C.I.) classifications: direct blue, direct red, direct violet, acid blue, acid red, acid violet, basic blue, basic violet, and basic red, or mixtures thereof.

[0210] In another aspect, suitable small molecule dyes include small molecule dyes selected from the group consisting of: Color Index (Society of Dyers and Colorists, Bradford, UK) numbers Direct Violet 9, Direct Violet 35, Direct Violet 48, Direct Violet 51, Direct Violet 66, Direct Violet 99, Direct Blue 1, Direct Blue 71, Direct Blue 80, Direct Blue 279, Acid Red 17, Acid Red 73, Acid Red 88, Acid Red 150, Acid Violet 15, Acid Violet 17, Acid Violet 24, Acid Violet 43, Acid Red 52, Acid Violet 49, Acid Violet 50, Acid Blue 15, Acid Blue 17, Acid Blue 25, Acid Blue 29, Acid Blue 40, Acid Blue 45, Acid Blue 75, Acid Blue 80, Acid Blue 83, Acid Blue 90, and Acid Blue 113, Acid Black 1, Basic Violet 1, Basic Violet 3, Basic Violet 4, Basic Violet 10, Basic Violet 35, Basic Blue 3, Basic Blue 16, Basic Blue 22, Basic Blue 47, Basic Blue 66, Basic Blue 75, Basic Blue 159, and mixtures thereof. In another aspect, suitable small molecule dyes include small molecule dyes selected from the group consisting of: Color Index (Society of Dyers and Colorists, Bradford, UK) numbers Acid Violet 17, Acid Violet 43, Acid Red 52, Acid Red 73, Acid Red 88, Acid Red 150, Acid Blue 25, Acid Blue 29, Acid Blue 45, Acid Blue 113, Acid Black 1, Direct Blue 1, Direct Blue 71, Direct Violet 51, and mixtures thereof. In another aspect, suitable small molecule dyes include small molecule dyes selected from the group consisting of: Color Index (Society of Dyers and Colorists, Bradford, UK) numbers Acid Violet 17, Direct Blue 71, Direct Violet 51, Direct Blue 1, Acid Red 88, Acid Red 150, Acid Blue 29, Acid Blue 113, or mixtures thereof.

[0211] Suitable polymeric dyes include polymeric dyes selected from the group consisting of: polymers containing conjugated chromophores (dye-polymer conjugates) and polymers in which the chromophore is copolymerized into the polymer backbone, and mixtures thereof.

[0212] On the other hand, suitable polymeric dyes include polymeric dyes selected from the group consisting of: fabric substantive colorants sold under the name Liquitint® (Milliken), dye-polymer conjugates formed from at least one reactive dye and a polymer selected from the group consisting of: polymers containing moieties selected from the group consisting of hydroxyl moieties, primary amine moieties, secondary amine moieties, thiol moieties, and mixtures thereof. Still on the other hand, suitable polymeric dyes include polymeric dyes selected from the group consisting of: Liquitint® Purple CT, carboxymethyl cellulose (CMC) conjugated with a reactive blue, reactive violet, or reactive red dye (such as CMC conjugated with C.I. Reactive Blue 19 (sold by Megazyme, Co. Wicklow, Ireland under the product name AZO-CM-CELLULOSE production code S-ACMC)), alkoxylated triphenyl-methane polymeric colorants, alkoxylated thiophene polymeric colorants, and mixtures thereof.

[0213] Preferred toner dyes include the optical brighteners found in WO 08 / 87497. These optical brighteners can be characterized by the following structure (I):

[0214] (I)

[0215] wherein R1 and R2 can independently be selected from:

[0216] a) [(CH2CR'HO) x (CH2CR"HO) y H]

[0217] wherein R’ is selected from the group consisting of: H, CH3, CH2O(CH2CH2O) z H, and mixtures thereof; wherein R” is selected from the group consisting of: H, CH2O(CH2CH2O) z H, and mixtures thereof; wherein x + y ≤ 5; wherein y ≥ 1; and wherein z = 0 to 5;

[0218] b) R1 = alkyl, aryl, or arylalkyl, and R2 = [(CH2CR'HO) x (CH2CR"HO) y H]

[0219] wherein R’ is selected from the group consisting of: H, CH3, CH2O(CH2CH2O) z H, and mixtures thereof; wherein R” is selected from the group consisting of: H, CH2O(CH2CH2O) zH, and mixtures thereof; where x + y ≤ 10; where y ≥ 1; and where z = 0 to 5;

[0220] c) R1 = [CH2CH2(OR3)CH2OR4] and R2 = [CH2CH2(OR3)CH2OR4]

[0221] where R3 is selected from the group consisting of: H, (CH2CH2O) z H and mixtures thereof; and where z = 0 to 10;

[0222] where R4 is selected from the group consisting of: (C1-C 16 ) alkyl, aryl groups, and mixtures thereof; and

[0223] d) where R1 and R2 can independently be selected from the amino addition products of styrene oxide, glycidyl methyl ether, isobutyl glycidyl ether, isopropyl glycidyl ether, tert-butyl glycidyl ether, 2-ethylhexyl glycidyl ether, and cetyl glycidyl ether, followed by the addition of from 1 to 10 alkylene oxide units.

[0224] Preferred brighteners of the present invention can be characterized by the following structure (II):

[0225] (II)

[0226] where R' is selected from the group consisting of: H, CH3, CH2O(CH2CH2O) z H, and mixtures thereof; where R" is selected from the group consisting of: H, CH2O(CH2CH2O) z H, and mixtures thereof; where x + y ≤ 5; where y ≥ 1; and where z = 0 to 5.

[0227] Further preferred brighteners of the present invention can be characterized by the following structure (III):

[0228] (III)

[0229] Typically contains a mixture having a total of 5 EO groups. Suitable preferred molecules are those having the following side groups in "Part a" above in Structure I.

[0230] Table 1

[0231]

[0232] Additional brighteners used include those described in US 2008 / 34511 (Unilever). The preferred reagent is "Violet 13".

[0233] Suitable dye-clay conjugates include dye-clay conjugates selected from the group consisting of at least one cationic / basic dye and smectite clay and mixtures thereof. In another aspect, suitable dye-clay conjugates include dye-clay conjugates selected from the group consisting of: a cationic / basic dye selected from the group consisting of C.I. Basic Yellow 1 to 108, C.I. Basic Orange 1 to 69, C.I. Basic Red 1 to 118, C.I. Basic Violet 1 to 51, C.I. Basic Blue 1 to 164, C.I. Basic Green 1 to 14, C.I. Basic Brown 1 to 23, C.I. Basic Black 1 to 11; and a clay selected from the group consisting of montmorillonite clay, lithium montmorillonite clay, saponite clay, and mixtures thereof. In still another aspect, suitable dye-clay conjugates include dye-clay conjugates selected from the group consisting of: montmorillonite Basic Blue B7 C.I. 42595 conjugate, montmorillonite Basic Blue B9 C.I. 52015 conjugate, montmorillonite Basic Violet V3 C.I. 42555 conjugate, montmorillonite Basic Green G1 C.I. 42040 conjugate, montmorillonite Basic Red R1 C.I. 45160 conjugate, montmorillonite C.I. Basic Black 2 conjugate, lithium montmorillonite Basic Blue B7 C.I. 42595 conjugate, lithium montmorillonite Basic Blue B9 C.I. 52015 conjugate, lithium montmorillonite Basic Violet V3 C.I. 42555 conjugate, lithium montmorillonite Basic Green G1 C.I. 42040 conjugate, lithium montmorillonite Basic Red R1 C.I. 45160 conjugate, lithium montmorillonite C.I. Basic Black 2 conjugate, saponite Basic Blue B7 C.I. 42595 conjugate, saponite Basic Blue B9 C.I. 52015 conjugate, saponite Basic Violet V3 C.I. 42555 conjugate, saponite Basic Green G1 C.I. 42040 conjugate, saponite Basic Red R1 C.I. 45160 conjugate, saponite C.I. Basic Black 2 conjugate, and mixtures thereof.

[0234] Suitable pigments include pigments selected from the group consisting of: flavanthrone, indanthrone, chlorinated indanthrone containing from 1 to 4 chlorine atoms, perylene, dichloroperylene, monobromodichloroperylene, dibromodichloroperylene, tetrabromoperylene, naphthalene-3,4,9,10-tetracarboxylic diimide (wherein these imide groups may be unsubstituted or substituted with C1-C3-alkyl or phenyl or heterocyclic groups, and wherein the phenyl and heterocyclic groups may additionally carry substituents that do not confer solubility in water), anthrapyrimidinecarboxamide, anthrone violet, isoanthrone violet, dioxazine pigments, copper phthalocyanine that may contain up to 2 chlorine atoms per molecule, polychloro-copper phthalocyanine, or polybromochloro-copper phthalocyanine containing up to 14 bromine atoms per molecule, and mixtures thereof.

[0235] In another aspect, suitable pigments include pigments selected from the group consisting of: ultramarine blue (C.I. Pigment Blue 29), ultramarine violet (C.I. Pigment Violet 15), and mixtures thereof.

[0236] The fabric conditioners described above can be used in combination (any mixture of fabric conditioners can be used). Suitable conditioners are described in more detail in US 7208459. The preferred level of the dye in the compositions of the present invention is from 0.00001 wt% to 0.5 wt%, or from 0.0001 wt% to 0.25 wt%. The concentration of the dye preferably used in water for the treatment and / or cleaning step is from 1 ppb to 5 ppm, from 10 ppb to 5 ppm, or from 20 ppb to 5 ppm. In the preferred compositions, the concentration of the surfactant will be from 0.2 to 3 g / l.

[0237] Encapsulated material

[0238] The compositions of the present invention can comprise encapsulates, which comprise a core and a shell having an inner surface and an outer surface. The shell encapsulates the core.

[0239] In one aspect of the encapsulate, the core can comprise materials selected from the group consisting of: fragrances; brighteners; dyes; insect repellents; silicones; waxes; flavorants; vitamins; fabric softeners; skin care agents; in one aspect, paraffin wax; enzymes; antibacterial agents; bleaching agents; sensates; and mixtures thereof; and the shell can comprise materials selected from the group consisting of: polyethylene; polyamide; polyvinyl alcohol, optionally containing other comonomers; polystyrene; polyisoprene; polycarbonate; polyester; polyacrylate; aminoplastics, in one aspect, the aminoplastics can comprise polyureas, polyurethanes, and / or polyurea polyurethanes, in one aspect, the polyureas can comprise polyoxymethylene ureas and / or melamine formaldehyde; polyolefins; polysaccharides, in one aspect, the polysaccharides can comprise alginates and / or chitosan; gelatin; shellac; epoxy resins; vinyl polymers; water-insoluble inorganic substances; silicones; and mixtures thereof.

[0240] In one aspect of the encapsulate, the core can comprise a fragrance.

[0241] In one aspect of the encapsulate, the shell can comprise melamine formaldehyde and / or crosslinked melamine formaldehyde.

[0242] In one aspect, suitable encapsulates can comprise a core material and a shell, the shell at least partially surrounding the core material. At least 75%, 85% or 90% of the encapsulates can have a fracture strength ranging from 0.2 to 10 MPa, from 0.4 to 5 MPa, from 0.6 to 3.5 MPa or from 0.7 to 3 MPa; and have a beneficial reagent leakage ranging from 0% to 30%, from 0% to 20% or from 0% to 5%.

[0243] In one aspect, at least 75%, 85% or 90% of the encapsulates can have a particle size ranging from 1 to 80 microns, from 5 to 60 microns, from 10 to 50 microns or from 15 to 40 microns.

[0244] In one aspect, at least 75%, 85% or 90% of the encapsulates can have a particle wall thickness ranging from 30 to 250 nm, from 80 to 180 nm, or from 100 to 160 nm.

[0245] In one aspect, the core material of the encapsulates can comprise a material selected from the group consisting of fragrance raw materials, and / or optionally comprise a material selected from the group consisting of: vegetable oils, including pure vegetable oils and / or blended vegetable oils, including castor oil, coconut oil, cottonseed oil, grapeseed oil, rapeseed, soybean oil, corn oil, palm oil, linseed oil, safflower oil, olive oil, peanut oil, coconut oil, palm kernel oil, castor oil, lemon oil and mixtures thereof; esters of vegetable oils, esters, including dibutyl adipate, dibutyl phthalate, butyl benzyl adipate, octyl benzyl adipate, tricresyl phosphate, trioctyl phosphate and mixtures thereof; straight-chain or branched-chain hydrocarbons, including those having a boiling point above about 80°C; partially hydrogenated terphenyls, dialkyl phthalates, alkyl biphenyls (including monoisopropyl biphenyl), alkylated naphthalenes (including dipropyl naphthalene), petroleum spirits (including kerosene), mineral oils and mixtures thereof; aromatic solvents, including benzene, toluene and mixtures thereof; silicone oils; and mixtures thereof.

[0246] In one aspect, the wall material of the encapsulates can comprise a suitable resin, the resin comprising a reaction product of an aldehyde and an amine, suitable aldehydes including formaldehyde. Suitable amines include melamine, urea, benzoguanamine, glycoluril and mixtures thereof. Suitable melamines include hydroxymethyl melamine, methylated hydroxymethyl melamine, imino melamine and mixtures thereof. Suitable ureas include dimethylol urea, methylated dimethylol urea, urea-resorcinol and mixtures thereof.

[0247] In one aspect, suitable formaldehyde scavengers can be used with and / or added to the composition, such as the encapsulated material in a capsule slurry, before, during, or after adding the encapsulated material to the composition. Suitable capsules can be made according to the following teachings of US 2008 / 0305982 and / or US 2009 / 0247449.

[0248] In a preferred aspect, the composition may further comprise a deposition aid, preferably consisting of the group consisting of cationic or nonionic polymers. Suitable polymers include cationic starch, cationic hydroxyethyl cellulose, polyvinyl formal, locust bean gum, mannan, xyloglucan, tamarind gum, polyethylene terephthalate, and polymers containing dimethylaminoethyl methacrylate, optionally having one or monomers selected from the group consisting of acrylic acid and acrylamide.

[0249] Fragrance

[0250] In one aspect, the composition of the present invention further comprises a fragrance comprising one or more fragrance raw materials selected from the group consisting of: 1,1'-oxybis-2-propanol; diethyl 1,4-cyclohexanedicarboxylate; (ethoxymethoxy)cyclododecane; 1,3-nonanediol monoacetate; 2-propenyl (3-methylbutoxy)acetate; β-methylcyclododecaneethanol; 2-methyl-3-[(1,7,7-trimethylbicyclo[2.2.1]hept-2-yl)oxy]-1-propanol; oxacyclohexadecan-2-one; α-methyl-benzyl alcohol ester; trans-3-ethoxy-1,1,5-trimethylcyclohexane; 4-(1,1-dimethylethyl)cyclohexyl acetate; dodecahydro-3a,6,6,9a-tetramethylnaphtho[2,1-b]furan; β-methylphenylacetaldehyde; β-methyl-3-(1-methylethyl)phenylacetaldehyde; 4-phenyl-2-butanone; ethyl 2-methylbutyrate; benzaldehyde; 1-methylethyl 2-methylbutyrate; dihydro-5-pentyl-2(3H)furanone; (2E)-1-(2,6,6-trimethyl-2-cyclohexen-1-yl)-2-buten-1-one; dodecanal; undecanal; 2-ethyl-α,α-dimethylphenylacetaldehyde; decanal; α,α-dimethylphenethyl acetate; 2-(phenylmethylene)octanal; methyl 2-[[3-[4-(1,1-dimethylethyl)phenyl]-2-methylpropylidene]amino]benzoate; 1-(2,6,6-trimethyl-3-cyclohexen-1-yl)-2-buten-1-one; 2-pentylcyclopentanone; methyl 3-oxo-2-pentylcyclopentylacetate; 4-hydroxy-3-methoxybenzaldehyde; 3-ethoxy-4-hydroxybenzaldehyde; 2-heptylcyclopentanone; 1-(4-methylphenyl)ethanone; (3E)-4-(2,6,6-trimethyl-1-cyclohexen-1-yl)-3-buten-2-one; (3E)-4-(2,6,6-trimethyl-2-cyclohexen-1-yl)-3-buten-2-one; phenethyl alcohol; 2H-1-benzopyran-2-one; 4-methoxybenzaldehyde; 10-undecenal; benzyl propionate; β-methylphenylpentanol; 1,1-diethoxy-3,7-dimethyl-2,6-octadiene; α,α-dimethylphenethyl alcohol; (2E)-1-(2,6,6-trimethyl-1-cyclohexen-1-yl)-2-buten-1-one; benzyl acetate; 2-propenyl cyclohexanepropionate; 2-propenyl hexanoate; 1,2-dimethoxy-4-(2-propenyl)benzene; 1,5-dimethyl-bicyclo[3.2.1] Octan-8-one oxime; 4-(4-hydroxy-4-methylpentyl)-3-cyclohexene-1-carbaldehyde; 3-buten-2-ol; methyl 2-[[[2,4(or 3,5)-dimethyl-3-cyclohexen-1-yl]methylene]amino]benzoate; 8-cyclohexadecen-1-one; methyl ionone; 2,6-dimethyl-7-octen-2-ol; 2-methoxy-4-(2-propenyl)phenol; (2E)-3,7-dimethyl-2,6-octadien-1-ol; (3Z)-hex-3-en-1-yl 2-hydroxybenzoate; 2-tridecenenitrile; 4-(2,2-dimethyl-6-methylenecyclohexyl)-3-methylbut-3-en-2-one; tetrahydro-4-methyl-2-(2-methylprop-1-enyl)-2H-pyran; (2-methylbutoxy)prop-2-enyl acetate; 3-methylbutyl 2-hydroxybenzoate; (Z)-1-(2,6,6-trimethylcyclohex-1-en-1-yl)but-2-en-1-one; methyl 2-hexyl-3-oxocyclopentanecarboxylate; 4-ethyl-α,α-dimethylphenylacetaldehyde; 3-(4-hydroxy-4-methylpentyl)-3-cyclohexene-1-carbaldehyde; 1-(2,3,4,7,8,8a-hexahydro-3,6,8,8-tetramethyl-1H-3a,7-methanoazulen-5-yl)-[3R-(3α,3aβ,7β,8aα)]-ethanone; 6-butyltetrahydro-undecanal; 4-tert-butyl-α-methylphenylacetaldehyde; 5-heptyldihydro-2(3H)-furanone; methyl 2-[(7-hydroxy-3,7-dimethyloctylidene)amino]benzoate; benzyl 2-hydroxybenzoate; 2-methoxynaphthalene; 2-hexylcyclopent-2-en-1-one; 5-hexyldihydro-2(3H)-furanone; ethyl 3-methyl-3-phenyloxirane-2-carboxylate; 1,3,3-trimethyl-2-oxabicyclo[2.2.2]octane; phenylpentanol, γ-Methyl-; 3,7-dimethyl-3-octanol; 3,7-dimethyl-2,6-octadienenitrile; 3,7-dimethyl-6-octen-1-ol; terpinyl acetate; 2-methyl-6-methylene-7-octen-2-ol dihydro derivative; 3a,4,5,6,7,7a-hexahydro-4,7-methano-1H-inden-6-yl propionate; 3-methyl-2-buten-1-ol acetate; (Z)-3-hexen-1-ol acetate; 2-ethyl-4-(2,2,3-trimethyl-3-cyclopenten-1-yl)-2-buten-1-ol; 4-(octahydro-4,7-methano-5H-inden-5-ylidene)-butanal; 3-2,4-dimethyl-cyclohexene-1-carbaldehyde; 1-(1,2,3,4,5,6,7,8-octahydro-2,3,8,8-tetramethyl-2-naphthalenyl)-ethanone; methyl 2-hydroxybenzoate; hexyl 2-hydroxybenzoate; 2-phenoxy-ethanol; pentyl 2-hydroxybenzoate; 2,3-heptanedione; 2-hexen-1-ol; 2,6-dimethyl-6-octen-2-ol; damascenone (α, β, γ or δ or mixtures thereof), 3a,4,5,6,7,7a-hexahydro-4,7-methano-1H-inden-6-yl acetate; 9-undecenal; 8-undecenal; isocyclocitral; 1-(1,2,3,5,6,7,8,8a-octahydro-2,3,8,8-tetramethyl-2-naphthalenyl)-ethanone; 3,5-dimethyl-3-cyclohexene-1-carbaldehyde; 2,4-dimethyl-3-cyclohexene-1-carbaldehyde; 3,7-dimethyl-1,6-octadien-3-ol; 3,7-dimethyl-1,6-octadien-3-ol acetate; linalool oxide (p-t-Bucinal), and 2-[2-(4-methyl-3-cyclopenten-1-yl)propyl]-cyclopentanone and 1-methyl-4-(1-methylethenyl)cyclohexene and mixtures thereof.

[0251] In one aspect, the composition may comprise encapsulated fragrance particles that contain a water-soluble hydroxy compound or melamine-formaldehyde or modified polyvinyl alcohol. In one aspect, the encapsulate comprises (a) at least partially water-soluble solid matrix that contains one or more water-soluble hydroxy compounds, preferably starch; and (b) a fragrance oil encapsulated by the solid matrix.

[0252] In another aspect, the fragrance may be pre-complexed with a polyamine (preferably polyethyleneimine) to form a Schiff base.

[0253] Polymer

[0254] The compositions of the present invention may also contain one or more polymers. Examples are carboxymethyl cellulose, poly(vinyl-pyrrolidone), poly(ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide), poly(vinylimidazole), polycarboxylates (such as polyacrylates), maleic acid / acrylic acid copolymers, and lauryl methacrylate / acrylic acid copolymers.

[0255] The composition may contain one or more amphiphilic cleansing polymers, such as compounds having the following general structure: bis((C2H5O)(C2H4O)n)(CH3)-N + -C x H 2x -N + -(CH3)-bis((C2H5O)(C2H4O)n), where n = from 20 to 30, and x = from 3 to 8, or sulfated or sulfonated variants thereof.

[0256] The composition may contain amphiphilic alkoxylated oil cleansing polymers that have balanced hydrophilic and hydrophobic properties such that they remove oil particles from fabrics and surfaces. Specific examples of the amphiphilic alkoxylated oil cleansing polymers of the present invention contain a core structure and a plurality of alkoxylated groups attached to that core structure. These may include alkoxylated polyalkylenimines, preferably having an inner poly(ethylene oxide) block and an outer poly(propylene oxide) block.

[0257] Alkoxylated polycarboxylates (such as those prepared from polyacrylates) may be used herein to provide additional oil removal performance. Such materials are described in WO 91 / 08281 and PCT90 / 01815. Chemically, these materials include polyacrylates having an ethoxy side chain for every 7-8 acrylate units. The side chain has the formula -(CH2CH2O) m (CH2) n CH3, where m is 2-3 and n is 6-12. The side chain is ester-linked to the polyacrylate "backbone" to provide a "comb-like" polymer type structure. The molecular weight may vary, but typically ranges from 2000 to 50,000. Such alkoxylated polycarboxylates may be included in the compositions herein from 0.05 wt% to 10 wt%.

[0258] The isoprenoid-derived surfactants of the present invention, and mixtures formed with other co-surfactants and other auxiliary components are particularly suitable for use with amphiphilic graft copolymers, preferably the amphiphilic graft copolymer comprises (i) a polyethylene glycol main chain; and (ii) at least one side chain moiety selected from polyvinyl acetate, polyvinyl alcohol, and mixtures thereof. A preferred amphiphilic graft copolymer is Sokalan HP22 supplied by BASF. Suitable polymers include random graft copolymers, preferably polyvinyl acetate-grafted polyethylene oxide copolymers having a polyethylene oxide main chain and multiple polyvinyl acetate side chains. The molecular weight of the polyethylene oxide main chain is preferably 6000, and the weight ratio of polyethylene oxide to polyvinyl acetate is 40 to 60, and there is no more than 1 graft point per 50 ethylene oxide units.

[0259] Carboxylate polymer

[0260] The compositions of the present invention may include one or more carboxylic ester polymers, such as maleate / acrylate random copolymers or polyacrylate homopolymers. In one aspect, the carboxylic ester polymer is a polyacrylate homopolymer having a molecular weight from 4,000 to 9,000 Da or from 6,000 to 9,000 Da.

[0261] Dirt release polymer

[0262] The compositions of the present invention may further include one or more soil release polymers having a structure defined by one of the following structures (I), (II), or (III):

[0263] (I) - [(OCHR 1 -CHR 2 ) a -O-OC-Ar-CO-] d

[0264] (II) - [(OCHR 3 -CHR 4 ) b -O-OC-sAr-CO-] e

[0265] (III) - [(OCHR 5 -CHR 6 ) c -OR 7 f

[0266] Wherein:

[0267] a, b, and c are from 1 to 200; ​

[0268] d, e, and f are from 1 to 50;

[0269] Ar is a 1,4-substituted phenylene;

[0270] sAr is a 1,3-substituted phenylene substituted with SO3Me at the 5-position;

[0271] Me is Li, K, Mg / 2, Ca / 2, Al / 3, ammonium, monoalkylammonium, dialkylammonium, trialkylammonium or tetraalkylammonium, where the alkyl group is C1-C 18 alkyl or C2-C 10 hydroxyalkyl, or a mixture thereof;

[0272] R 1 、R 2 、R 3 、R 4 、R 5 and R 6 are independently selected from H or C1-C 18 n-alkyl or iso-alkyl; and

[0273] R 7 is a straight-chain or branched C1-C 18 alkyl, or a straight-chain or branched C2-C 30 alkenyl, or a cycloalkyl having 5 to 9 carbon atoms, or a C8-C 30 aryl, or a C6-C 30 arylalkyl.

[0274] Suitable soil-release polymers are polyester soil-release polymers such as Repel-o-tex polymers, including Repel-o-tex, SF-2 and SRP6, supplied by Rhodia. Other suitable soil-release polymers include Texcare polymers, including Texcare SRA100, SRA300, SRN100, SRN170, SRN240, SRN300 and SRN325, supplied by Clariant. Other suitable soil-release polymers are Marloquest polymers such as Marloquest SL, supplied by Sasol.

[0275] Cellulosic polymer

[0276] The composition of the present invention may further comprise one or more cellulose polymers, which include those selected from alkyl celluloses, alkyl alkoxyalkyl celluloses, carboxyalkyl celluloses, and alkyl carboxyalkyl celluloses. In one aspect, the cellulose polymers are selected from the group consisting of carboxymethyl cellulose, methyl cellulose, methyl hydroxyethyl cellulose, methyl carboxymethyl cellulose, and mixtures thereof. In one aspect, the carboxymethyl cellulose has a degree of carboxymethyl substitution from 0.5 to 0.9 and a molecular weight from 100,000 Da to 300,000 Da.

[0277] Dye transfer inhibitor

[0278] The composition of the present invention may further comprise one or more dye transfer inhibitors. Suitable polymeric dye transfer inhibitors include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyl oxazolidone, and polyvinyl imidazole or mixtures thereof. When present in the composition, the dye transfer inhibitor may be present at a level from 0.0001 wt% to 10 wt%, from 0.01 wt% to 5 wt%, or from 0.1 wt% to 3 wt%.

[0279] Brightener

[0280] The composition of the present invention may also contain additional components that can color the article being cleaned, such as fluorescent brighteners.

[0281] The composition may comprise C.I. Fluorescent Brightener 260 in the α-crystalline form having the following structure:

[0282]

[0283] In one aspect, the brightener is a cold water-soluble brightener, such as C.I. Fluorescent Brightener 260 in the α-crystalline form. In one aspect, the brightener is predominantly in the α-crystalline form, meaning that typically at least 50 wt%, at least 75 wt%, at least 90 wt%, at least 99 wt%, or even substantially all of the C.I. Fluorescent Brightener 260 is in the α-crystalline form.

[0284] The brightener is typically in the form of micronized particles having a weighted average primary particle size from 3 to 30 microns, from 3 microns to 20 microns, or from 3 to 10 microns.

[0285] The composition may comprise C.I. Fluorescent Brightener 260 in the β-crystalline form, and the weight ratio of (i) C.I. Fluorescent Brightener 260 in the α-crystalline form to (ii) C.I. Fluorescent Brightener 260 in the β-crystalline form may be at least 0.1 or at least 0.6. BE680847 relates to a process for obtaining C.I. Fluorescent Brightener 260 in the α-crystalline form.

[0286] The commercial optical brighteners that can be used in the present invention can be divided into several subgroups, including but not limited to: stilbenes, pyrazolines, coumarins, carboxylic acids, polymethine cyanines, dibenzothiophene-5,5-dioxides, azoles, derivatives of 5- and 6-membered heterocycles, and other miscellaneous agents. Examples of such brighteners are disclosed in “The Production and Application of Fluorescent Brightening Agents”, M. Zahradnik, published by John Wiley & Sons, New York (1982). Specific non-limiting examples of optical brighteners that can be used in the compositions of the present invention are those identified in US 4790856 and US 3646015.

[0287] Other suitable brighteners have the following structures:

[0288]

[0289] Suitable levels of fluorescent brighteners include lower levels from 0.01 wt%, from 0.05 wt%, from 0.1 wt% or from 0.2 wt% to higher levels of 0.5 wt% or 0.75 wt%.

[0290] In one aspect, the brightener may be loaded on clay to form particles. Silicates - The compositions of the present invention may also contain silicates, such as sodium silicate or potassium silicate. The composition may comprise from 0 wt% to less than 10 wt% of silicate, up to 9 wt%, or up to 8 wt%, or up to 7 wt%, or up to 6 wt%, or up to 5 wt%, or up to 4 wt%, or up to 3 wt%, or even up to 2 wt%, and from above 0 wt%, or from 0.5 wt%, or from 1 wt% of silicate. A suitable silicate is sodium silicate.

[0291] Dispersant

[0292] The compositions of the present invention may also contain a dispersant. Suitable water-soluble organic materials include homopolymeric or copolymeric acids or their salts, wherein the polycarboxylic acid contains at least two carboxyl groups separated from each other by no more than two carbon atoms.

[0293] Enzyme stabilizer

[0294] Enzymes for use in a composition can be stabilized by various techniques. The enzymes used herein can be stabilized by the presence of a water-soluble source of calcium and / or magnesium ions. Examples of conventional stabilizers are, for example, polyols such as propylene glycol or glycerol, sugars or sugar alcohols, peptide aldehydes, lactic acid, boric acid or boric acid derivatives such as aromatic borates, or phenylboric acid derivatives such as 4-formylphenylboric acid, and the composition can be formulated as described, for example, in WO 92 / 19709 and WO 92 / 19708. In the case of an aqueous composition containing a protease, a reversible protease inhibitor can be added to further improve stability, such reversible protease inhibitor being, for example, a boron compound including borates, 4-formylphenylboric acid, phenylboric acid and its derivatives; or a compound such as calcium formate, sodium formate and 1,2-propanediol. The peptide aldehyde can have the formula B2-B1-B0-R, where: R is hydrogen, CH3, CX3, CHX2 or CH2X, where X is a halogen atom; B0 is a phenylalanine residue having OH substituents at the para position and / or at the meta position; B1 is a single amino acid residue; and B2 is composed of one or more amino acid residues, optionally containing an N-terminal protecting group. Preferred peptide aldehydes include, but are not limited to: Z-RAY-H, Ac-GAY-H, Z-GAY-H, Z-GAL-H, Z-GAF-H, Z-GAV-H, Z-RVY-H, Z-LVY-H, Ac-LGAY-H (SEQ ID NO: 5), Ac-FGAY-H (SEQ ID NO: 6), Ac-YGAY-H (SEQ ID NO: 7), Ac-FGVY-H (SEQ ID NO: 8) or Ac-WLVY-H (SEQ ID NO: 9), where Z is benzyloxycarbonyl and Ac is acetyl.

[0295] Solvent

[0296] Suitable solvents include water and other solvents such as lipophilic fluids. Examples of suitable lipophilic fluids include siloxanes, other silicones, hydrocarbons, ethylene glycol ethers, glycerol derivatives (such as glycerol ethers), perfluorinated amines, perfluorinated and hydrofluoroether solvents, low volatility non-fluorinated organic solvents, diol solvents, other environmentally friendly solvents and mixtures thereof.

[0297] Structurant / thickener

[0298] Structured liquids can be structured internally, where the structure is formed by a primary component (e.g., surfactant material), and / or structured externally by providing a three-dimensional matrix structure using a secondary component (e.g., polymers, clays, and / or silicate materials). The composition can contain from 0.01 wt% to 5 wt%, or from 0.1 wt% to 2.0 wt% of a structuring agent. Structuring agents are typically selected from the group consisting of: diglycerides and triglycerides, ethylene glycol distearate, microcrystalline cellulose, cellulose-based materials, microfibrillated cellulose, hydrophobically modified alkali swellable emulsions (e.g., Polygel W30 (3V Sigma)), biopolymers, xanthan gum, gellan gum, and mixtures thereof. Suitable structuring agents include hydrogenated castor oil and its non-ethoxylated derivatives. Suitable structuring agents are disclosed in US 6855680. Such structuring agents have a thread-like structuring system that has a range of aspect ratios. Other suitable structuring agents and methods for making them are described in WO 10 / 034736.

[0299] Modulator

[0300] The compositions of the present invention can include high melting point fatty compounds. High melting point fatty compounds useful herein have a melting point of 25°C or higher and are selected from the group consisting of: fatty alcohols, fatty acids, fatty alcohol derivatives, fatty acid derivatives, and mixtures thereof. Compounds having a low melting point are not intended to be included in this section. Non-limiting examples of high melting point compounds are found in International Cosmetic Ingredient Dictionary, 5th Edition, 1993, and CTFA Cosmetic Ingredient Handbook, 2nd Edition, 1992.

[0301] In view of providing improved conditioning benefits (e.g., slipperiness, softness during application to wet hair, and moisturizing to dry hair), the high melting point fatty compounds are included in the composition at levels from 0.1 wt% to 40 wt%, from 1 wt% to 30 wt%, from 1.5 wt% to 16 wt%, from 1.5 wt% to 8 wt%.

[0302] The compositions of the present invention can contain a cationic polymer. The concentration of the cationic polymer in the composition typically ranges from 0.05 wt% to 3 wt%, from 0.075 wt% to 2.0 wt%, or from 0.1 wt% to 1.0 wt%. At the pH at which the composition is intended to be used, suitable cationic polymers will have a cationic charge density of at least 0.5 meq / gm, at least 0.9 meq / gm, at least 1.2 meq / gm, at least 1.5 meq / gm, or less than 7 meq / gm, and less than 5 meq / gm, and the pH will generally range from pH 3 to pH 9, or between pH 4 and pH 8. Herein, the "cationic charge density" of a polymer refers to the ratio of the number of positive charges on the polymer to the molecular weight of the polymer. The average molecular weight of such suitable cationic polymers will generally be between 10,000 and 10,000,000, between 50,000 and 5,000,000, or between 100,000 and 3,000,000.

[0303] Suitable cationic polymers for use in the compositions of the present invention contain cationic nitrogenous moieties, such as quaternary ammonium or cationically protonated amino moieties. Any anionic counterion can be used in association with the cationic polymer, provided that the polymer remains soluble in water, in the composition, or in the condensed phase of the composition, and provided that the counterion is physically and chemically compatible with the major components of the composition or otherwise does not unduly impair the performance, stability, or aesthetic of the composition. Non-limiting examples of such counterions include halides (e.g., chloride, fluoride, bromide, iodide), sulfate, and methyl sulfate.

[0304] Non-limiting examples of such polymers are described in the CTFA Cosmetic Ingredient Dictionary, 3rd Edition, edited by Estrin, Crosley, and Haynes (The Cosmetic, Toiletry, and Fragrance Association, Inc., Washington, D.C. (1982)).

[0305] Other suitable cationic polymers for use in the composition include polysaccharide polymers, cationic guar derivatives, quaternary nitrogen-containing cellulose ethers, synthetic polymers, copolymers of etherified cellulose, guar gum and starch. When used, the cationic polymers herein can be dissolved in the composition or in the coacervate phase dissolved in the composition, which coacervate phase is formed from the cationic polymers and anionic, amphoteric and / or zwitterionic surfactant components described above. Complex coacervates of the cationic polymers can also be formed with other charged materials in the composition. Suitable cationic polymers are described in US 3962418; US 3958581; and US 2007 / 0207109.

[0306] The compositions of the present invention can include nonionic polymers as modifiers. Polyalkylene glycols having a molecular weight greater than 1000 are useful herein. Those having the following general formula are useful:

[0307]

[0308] wherein R 95 is selected from the group consisting of: H, methyl and mixtures thereof. Modifiers, and in particular silicones, can be included in the composition. Modifiers for use in the compositions of the present invention typically comprise water-insoluble, water-dispersible, non-volatile liquids that form emulsified liquid particles. Suitable modifiers for use in the composition are those modifiers that are generally characterized as: silicones (e.g., silicone oils, cationic silicones, silicone gums, high refractive index silicones, and silicone resins), organic conditioning oils (e.g., hydrocarbon oils, polyolefins, and fatty esters) or combinations thereof, or those modifiers that otherwise form liquid dispersion particles in the aqueous surfactant matrix herein. Such modifiers should be physically and chemically compatible with the major components of the composition and should not otherwise unduly impair the stability, aesthetics or performance of the composition.

[0309] The concentration of the modifier in the composition should be sufficient to provide the desired conditioning benefit. This concentration can vary with the modifier, the desired conditioning performance, the average size of the modifier particles, the type and concentration of other components, and other similar factors.

[0310] The concentration range of the silicone modifier is typically from 0.01 wt% to 10 wt%. Non-limiting examples of suitable silicone modifiers and optional suspending agents for the silicone are described in U.S. Reissue Patent No. 34,584; US5104646; US5106609; US4152416; US2826551; US3964500; US4364837; US6607717; US6482969; US5807956; US5981681; US6207782; US7465439; US7041767; US7217777; US2007 / 0286837A1; US2005 / 0048549A1; US2007 / 0041929A1; GB849433; DE10036533, all of which are incorporated herein by reference; Chemistry and Technology of Silicones, New York: Academic Press (1968); General Electric Silicone Rubber Product Data Sheets SE 30, SE 33, SE 54 and SE76; Silicone Compounds, Petrarch Systems, Inc. (1984); and Encyclopedia of Polymer Science and Engineering, Volume 15, 2nd Edition, pages 204-308, John Wiley & Sons, Inc. (1989).

[0311] The composition of the present invention may also comprise from 0.05 wt% to 3 wt% of at least one organic regulating oil as a modifier, alone or in combination with other modifiers such as silicone (described herein). Suitable regulating oils include hydrocarbon oils, polyolefins, and fatty esters. Also suitable for use in the compositions herein are the modifiers described in US 5674478 and US 5750122 or in US4529586; US 4507280; US 4663158; US 4197865; US 4217914; US 4381919; and US 4422853.

[0312] Hygiene and malodor

[0313] The composition of the present invention may also comprise one or more of thymol, quaternary ammonium salts (such as Bardac®) and their zinc complexes, silver and silver compounds (especially those designed to slowly release Ag + or those which are silver nano-dispersions).

[0314] Probiotic

[0315] The composition may comprise probiotics, such as those described in WO 09 / 043709.

[0316] Foam booster

[0317] If high foaming is desired, foam boosters (such as C 10 -C 16 alkanolamides or C 10 -C 14 alkyl sulfates) may typically be incorporated into the composition at levels from 1 wt% to 10 wt%. C 10 -C 14 Monoethanol and diethanol amides illustrate typical classes of such foam boosters. Such foam boosters are also advantageously used in combination with high-foaming co-surfactants such as, for example, the amine oxides, betaines, and sultaines mentioned above. If desired, water-soluble magnesium and / or calcium salts (such as MgCl2, MgSO4, CaCl2, CaSO4, etc.) may typically be added at levels from 0.1 wt% to 2 wt% to provide additional foam and to enhance grease removal performance.

[0318] Foam inhibitor

[0319] Compounds for reducing or suppressing foam formation may be incorporated into the compositions of the present invention. Foam suppression may be particularly important in so-called "high-concentration cleaning processes" as described in US 4489455 and US 4489574 and in front-loading-style washing machines. A variety of materials may be used as foam inhibitors, and foam inhibitors are well known to those skilled in the art. See, for example, Kirk Othmer Encyclopedia of Chemical Technology, 3rd Edition, Volume 7, pages 430-447 (John Wiley & Sons, Inc., 1979). Examples of foam inhibitors include monocarboxylic fatty acids and soluble salts thereof, high molecular weight hydrocarbons such as paraffin waxes, fatty acid esters (such as fatty acid triglycerides), fatty acid esters of monohydric alcohols, aliphatic C 18 -C 40Ketones (e.g., stearone), N-alkylated aminotriazines, preferably wax hydrocarbons having a melting point below about 100 °C, silicone foam inhibitors, and secondary alcohols. The foam inhibitors are described in US 2954347; US4265779; US 4265779; US 3455839; US 3933672; US 4652392; US 4978471; US 4983316; US5288431; US 4639489; US 4749740; US 4798679; US 4075118; EP 89307851.9; EP 150872; and DOS 2,124,526.

[0320] Lipase

[0321] The compositions of the present invention comprise lipase in addition to peptides (as defined herein). Furthermore, the enzyme products of the present invention that can be used in the compositions of the present invention comprise lipase in addition to peptides (as defined herein). The lipase can be any lipase. In an embodiment, the lipase is of microbial origin. In an embodiment, the lipase is of bacterial origin. In a preferred embodiment, the lipase is of fungal origin, such as from filamentous fungi or yeast.

[0322] Examples of preferred fungal lipases include lipases from Thermomyces (e.g., from Thermomyces lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP 305216), cutinases from Humicola (e.g., Humicola insolens) (WO 96 / 13580), lipases from Absidia reflexa disclosed in US 2009 / 0221033 A1 (SEQ ID NO: 3), and lipase (GCL 1) from Geotrichum candidum shown in SEQ ID NO: 4 herein (or SEQ ID NO: 1 in WO 2022 / 162043 – which is hereby incorporated by reference).

[0323] Other examples of lipases are those from bacteria such as Pseudomonas (some of these are now renamed Burkholderia), e.g., Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes (EP 218272), Pseudomonas cepacia (EP331376), Pseudomonas sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), lipases from Pseudomonas wisconsinensis (WO 96 / 12012); GDSL-type lipases from Streptomyces (WO10 / 065455); cutinases from Magnaporthe grisea (WO 10 / 107560); cutinases from Pseudomonas mendocina (US 5,389,536); lipases from Thermobifida fusca (WO 11 / 084412, WO 13 / 033318); Geobacillus stearothermophilus lipases (WO 11 / 084417); lipases from Bacillus subtilis (WO 11 / 084599); and lipases from Streptomyces griseus (WO 11 / 150157) and Streptomyces pristinaespiralis (WO12 / 137147) (all references are incorporated by reference).

[0324] Other examples are lipase variants such as those described in EP 407225, WO 92 / 05249, WO 94 / 01541, WO 94 / 25578, WO 95 / 14783, WO 95 / 30744, WO 95 / 35381, WO 95 / 22615, WO 96 / 00292, WO 97 / 04079, WO97 / 07202, WO 00 / 34450, WO 00 / 60063, WO 01 / 92502, WO 07 / 87508 and WO 09 / 109500 (all documents are hereby incorporated by reference).

[0325] Other examples are lipases sometimes referred to as acyltransferases or perhydrolases, such as acyltransferases homologous to Candida antarctica lipase A (WO 10 / 111143), acyltransferases from Mycobacterium smegmatis (WO 05 / 56782), perhydrolases from the CE 7 family (WO 09 / 67279), and variants of Mycobacterium smegmatis perhydrolases (in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd) (WO 10 / 100028).

[0326] Preferred commercial lipase products include Lipolase TM 、Lipex™、Lipolex TM 、Lipoclean TM 、LipexEvity 100L、Lipex Evity 105T、Lipex Evity 200L (Novozymes), Lumafast (from Genencor), Preferenz L100 (Danisco US Inc.), and Lipomax (from Gist-Brocades).

[0327] Lipase of SEQ ID NO: 1 - Thermomyces lanuginosus lipase (TLL)

[0328] In a preferred embodiment, the enzyme product of the present invention or the (detergent) composition of the present invention comprises a lipase or a variant thereof derived from a strain of the genus Thermomyces, particularly Thermomyces lanuginosus (synonym: Humicola lanuginosa).

[0329] In a particular embodiment, the lipase is the lipase shown in SEQ ID NO: 1 or a variant thereof.

[0330] In an embodiment, the lipase is:[[]]

[0331] i) a lipase that has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 1;

[0332] ii) A parental lipase variant having lipase activity, which variant has at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% but less than 100% sequence identity with the lipase shown in SEQ ID NO: 1;

[0333] iii) A fragment of the lipase in i) or ii) that has lipase activity,

[0334] wherein optionally the variant comprises substitutions at positions corresponding to T231R + N233R of SEQ ID NO: 1, and at least one or more (e.g., several) of D96E, D111A, D254S, G163K, P256T, G91T, and G38A.

[0335] In a particular embodiment, the lipase used in the enzyme product or composition of the present invention is a variant of the parental lipase, wherein the variant has lipase activity, has at least 60%, particularly at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity with SEQ ID NO: 1, and comprises substitutions selected from the group consisting of:

[0336] D96E + T231R + N233R;

[0337] N33Q + D96E + T231R + N233R;

[0338] N33Q + D111A + T231R + N233R;

[0339] N33Q + T231R + N233R + P256T;

[0340] N33Q + G38A + G91T + G163K + T231R + N233R + D254S;

[0341] N33Q + G38A + G91T + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0342] D27R + N33Q + G38A + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0343] D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+P256T;

[0344] D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S;

[0345] D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0346] D96E+T231R+N233R+D254S;

[0347] T231R+N233R+D254S+P256T;

[0348] G163K+T231R+N233R+D254S;

[0349] D27R+N33Q+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;

[0350] D27R+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0351] D96E+G163K+T231R+N233R+D254S;

[0352] D27R+G163K+T231R+N233R+D254S;

[0353] D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S;

[0354] D27R+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;

[0355] D27R+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0356] D27R+D96E+G163K+T231R+N233R+D254S;

[0357] D27R+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0358] D27R + G38A + D96E + G163K + T231R + N233R + D254S + P256T

[0359] D111A + G163K + T231R + N233R + D254S + P256T;

[0360] D111A + T231R + N233R;

[0361] D111A + T231R + N233R + D254S + P256T;

[0362] D27R + D96E + D111A + G163K + T231R + N233R;

[0363] D27R + D96E + D111A + T231R + N233R;

[0364] D27R + N33Q + G38A + D96E + D111A + T231R + N233R + D254S + P256T;

[0365] D27R + G38A + D96E + D111A + G163K + E210Q + T231R + N233R + D254S + P256T;

[0366] D27R + T231R + N233R + D254S + P256T;

[0367] D96E + D111A + G163K + T231R + N233R;

[0368] D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0369] D96E + D111A + G163K + T231R + N233R + P256T;

[0370] D96E + D111A + T231R + N233R;

[0371] D96E + D111A + T231R + N233R + D254S;

[0372] D96E + D111A + T231R + N233R + D254S + P256T

[0373] D96E + D111A + T231R + N233R + P256T;

[0374] D96E + G163K + T231R + N233R + D254S + P256T;

[0375] D96E + T231R + N233R + D254S + P256T;

[0376] D96E + T231R + N233R + P256T;

[0377] G38A + D96E + D111A + T231R + N233R;

[0378] G91T + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0379] G91T + D96E + D111A + T231R + N233R;

[0380] G91T + D96E + T231R + N233R;

[0381] G91T + T231R + N233R + D254S + P256T;

[0382] N33Q + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0383] T231R + N233R + D254S + P256T;

[0384] T231R + N233R + P256T.

[0385] In another embodiment, the lipase is a variant of the parent lipase, wherein the variant

[0386] (a) contains a modification at at least one position corresponding to positions E1, V2, N33, F51, E56, L69, K98, V176, H198, E210, Y220, L227 and K237 of SEQ ID NO: 1; and optionally further contains a modification at at least one position corresponding to positions D27, G38, D96, D111, G163, T231, N233, D254 and P256 of SEQ ID NO: 1;

[0387] (b) has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity with SEQ ID NO: 1;

[0388] (c) has lipase activity.

[0389] In an embodiment, the lipase is a variant of a parental lipase, where the parental lipase is selected from the group consisting of:

[0390] a) a polypeptide that has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 1;

[0391] b) a fragment of the polypeptide of SEQ ID NO: 1.

[0392] In an embodiment, the lipase is a variant having lipase activity, and the variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100% sequence identity with SEQ ID NO: 1.

[0393] In an embodiment, the lipase variant contains a modification in at least one of the following positions corresponding to: E1, V2, D27, N33, G38, F51, E56, L69, D96, K98, D111, G163, V176, H198, E210, Y220, L227, T231, N233, K237, D254, and P256, numbered according to SEQ ID NO: 1. More preferably, the lipase variant contains at least one of the following modifications corresponding to: E1C, V2Y, D27R, N33K, N33Q, G38A, F51V, E56K, L69R, D96E, D96L, K98I, K98Q, D111A, G163K, V176L, H198S, E210K, Y220F, L227G, T231R, N233R, N233C, K237C, D254S, and P256T, numbered according to SEQ ID NO: 1.

[0394] In an embodiment, the lipase variant further contains one of the substitutions selected from the group: S54T, S83T, G91A, A150G, I255A, and E239C.

[0395] In a preferred embodiment, the lipase variant contains the substitutions corresponding to E1C+N233C in SEQ ID NO: 1 and optionally one or more additional substitutions.

[0396] In certain embodiments, the variant has lipase activity and has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity to SEQ ID NO: 1, and contains a substitution corresponding to or consisting of one of the following sets of substitutions (numbered using SEQ ID NO: 1):

[0397]

[0398]

[0399]

[0400] In an embodiment, the lipase is a variant of a parental lipase, the variant having lipase activity and having at least 60% but less than 100% sequence identity to SEQ ID NO: 1, and containing one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, E56R, D57N, V60E,K, K98I, N101D, R118F, G163S, Y220F, T231R, N233R, T244E, and P256T (numbered using SEQ ID NO: 1). The lipase variant may contain substitutions at positions corresponding to T231R+N233R, as well as one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, E56R, D57N, V60E,K, K98I, N101D, R118F, G163S, Y220F, T244E, and P256T.

[0401] In a preferred embodiment, the lipase is a variant that contains a substitution corresponding to any of the following sets of substitutions (numbered using SEQ ID NO: 1):

[0402] G23S+T231R+N233R

[0403] D27N+T231R+N233R

[0404] A40I+T231R+N233R

[0405] F51I+T231R+N233R

[0406] F51L+T231R+N233R

[0407] E56R+T231R+N233R

[0408] D57N + T231R + N233R

[0409] V60E + T231R + N233R

[0410] V60K + T231R + N233R

[0411] K98I + T231R + N233R

[0412] N101D + T231R + N233R

[0413] R118F + T231R + N233R

[0414] G163S + T231R + N233R

[0415] Y220F + T231R + N233R

[0416] T231R + N233R + T244E

[0417] T231R + N233R + P256T (numbered using SEQ ID NO: 1)

[0418] In an embodiment, the lipase is a lipase variant that contains substitutions corresponding to E56R + T231R + N233R, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, D57N, V60E,K, K98I, N101D, R118F, G163S, Y220F, T244E, and P256T.

[0419] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to R118F + T231R + N233R, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, E56R, D57N, V60E,K, K98I, N101D, G163S, Y220F, T244E, and P256T.

[0420] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to E56R + R118F + T231R + N233R, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, D57N, V60E,K, K98I, N101D, G163S, Y220F, T244E, and P256T.

[0421] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to E56R+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, D57N, V60E,K, K98I, N101D, G163S, Y220F, and T244E.

[0422] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I,L+E56R+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, D57N, V60E,K, K98I, N101D, G163S, Y220F, and T244E.

[0423] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to G23S+F51I,L+E56R+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to D27N, A40I, D57N, V60E,K, K98I, N101D, G163S, Y220F, and T244E.

[0424] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to D27N+F51I,L+E56R+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, A40I, D57N, V60E,K, K98I, N101D, G163S, Y220F, and T244E.

[0425] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to A40I+F51I,L+E56R+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, D57N, V60E,K, K98I, N101D, G163S, Y220F, and T244E.

[0426] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, V60E,K, K98I, N101D, G163S, Y220F, and T244E.

[0427] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+K98I+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, V60E,K, N101D, G163S, Y220F, and T244E.

[0428] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+K98I+R118F+G163S+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, V60E,K, N101D, Y220F, and T244E.

[0429] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+K98I+R118F+G163S+T231R+N233R+T244E+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, V60E,K, N101D, and Y220F.

[0430] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+V60E,K+K98I+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, N101D, G163S, Y220F, and T244E.

[0431] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+N101D+K98I+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, V60E,K, N101D, G163S, Y220F, and T244E.

[0432] In an embodiment, the lipase is a lipase variant that contains substitutions at positions corresponding to F51I, L+E56R+D57N+V60E,K+K98I+N101D+R118F+T231R+N233R+P256T, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, G163S, Y220F, and T244E.

[0433] In an embodiment, the lipase is a lipase variant that consists of or contains substitutions corresponding to the following (numbered using SEQ ID NO: 1):

[0434]

[0435] In an embodiment, the lipase is a variant of a parental lipase selected from:

[0436] a) a polypeptide that has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99% or 100% sequence identity to SEQ ID NO: 1; and

[0437] b) a fragment of the polypeptide of SEQ ID NO: 1.

[0438] In an embodiment, the lipase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99% but less than 100% sequence identity to SEQ ID NO: 1.

[0439] Lipase of SEQ ID NO: 4 - Geotrichum candidum lipase (GCL 1)

[0440] In another preferred embodiment, the composition of the present invention or the enzyme product of the present invention comprises a lipase or an analogue thereof (e.g., an analogue disclosed in WO 2022 / 162043) as shown in SEQ ID NO: 4 (also as disclosed in SEQ ID NO: 1 in WO 2022 / 162043, which is hereby incorporated by reference).

[0441] Thus, in a preferred embodiment, the lipase used according to the present invention is:

[0442] i) a lipase that has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 4;

[0443] ii) a fragment of the lipase in i) that has lipase activity.

[0444] Other lipases

[0445] Other lipases contemplated according to the present invention are those lipases disclosed in the following applications: WO 2019 / 038164, WO 2019 / 121585, WO 2019 / 138121, WO 2019 / 155789, WO 2019 / 155790, WO 2019 / 185519, WO 2019 / 185610, WO 2019 / 185612, WO 2019 / 201636, WO 2019 / 206994, WO 2019 / 215078, WO 2019 / 219903, and WO 2019 / 243312 (all hereby incorporated by reference).

[0446] Additional enzymes

[0447] In addition to lipases and peptides, the composition of the present invention may comprise one or more additional enzymes that provide cleaning performance and / or fabric care benefits. Examples of suitable enzymes include, but are not limited to, proteases, α - amylases, cellulases, phospholipases, cutinases, pectinases, mannanases, pectin lyases, nucleases (e.g., DNases, RNases), or mixtures thereof. A typical combination is an enzyme mixture that may comprise, for example, a protease and a lipase together with α - amylase, phospholipase, cutinase, pectinase, mannanase, pectin lyase, nuclease (e.g., DNase, RNase), xanthanase, dispersase, or mixtures thereof.

[0448] When present in the composition, the foregoing additional enzyme(s) may be present at a level of from 0.00001 wt% to 2 wt%, from 0.0001 wt% to 1 wt% or from 0.001 wt% to 0.5 wt% enzyme protein, based on the weight of the composition.

[0449] Generally, the properties of the one or more enzymes selected should be compatible with the selected detergent (i.e., optimum pH, compatibility with other enzyme and non-enzyme ingredients, etc.), and the one or more enzymes should be present in an effective amount.

[0450] Protease: In one aspect, preferred additional enzymes are proteases. Suitable proteases include those from bacterial, fungal, plant, viral or animal sources, such as plant or microbial sources. Microbial-source proteases are preferred. Include chemically modified mutants or protein-engineered mutants. It can be an alkaline protease, such as a serine protease or a metalloprotease. The serine protease can be, for example, of the S1 family (such as trypsin) or of the S8 family (such as subtilisin). The metalloprotease can be, for example, thermolysin from the M4 family, for example, or other metalloproteases, such as those from the M5, M7 or M8 families.

[0451] The term "subtilase" refers to a subgroup of serine proteases according to Siezen et al., Protein Engng. [Protein Engineering] 4 (1991) 719-737 and Siezen et al., Protein Science [Protein Science] 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site that forms a covalent adduct with the substrate. Subtilases can be divided into 6 subclasses, namely, the subtilisin family, the thermitase family, the proteinase K family, the lantibiotic peptidase family, the kexin family and the pyrolysin family.

[0452] Examples of subtilisins are those derived from the genus Bacillus, such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii as described in US 7262042 and WO 09 / 021867; and subtilisin amylosacchariticus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 as described in WO 89 / 06279 and protease PD138 as described in (WO 93 / 18140). Other useful proteases can be those described in WO 92 / 175177, WO 01 / 016285, WO 02 / 026024 and WO 02 / 016547. Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin) and Fusarium proteases (described in WO 89 / 06270, WO 94 / 25583 and WO 05 / 040372), and chymotrypsin derived from Cellumonas (described in WO 05 / 052161 and WO 05 / 052146).

[0453] Another preferred protease is the alkaline protease from Bacillus lentus DSM 5483 (as described in, for example, WO95 / 23221) and its variants (described in WO 92 / 21760, WO 95 / 23221, EP 1921147 and EP 1921148).

[0454] Examples of metalloproteases are the neutral metalloproteases as described in WO 07 / 044993 (Genencor International Inc.), for example those derived from Bacillus amyloliquefaciens.

[0455] Examples of useful proteases are variants described in the following: WO 92 / 19729, WO 96 / 034946, WO98 / 20115, WO 98 / 20116, WO 99 / 011768, WO 01 / 44452, WO 03 / 006602, WO 04 / 03186, WO 04 / 041979, WO 07 / 006305, WO 11 / 036263, WO 11 / 036264, especially variants having substitutions at one or more of the following positions: 3, 4, 9, 15, 27, 36, 57, 68, 76, 87, 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 274, numbered using BPN'. More preferably, the subtilisin variants may comprise the following mutations: S3T, V4I, S9R, A15T, K27R, *36D, V68A, N76D, N87S,R, *97E, A98S, S99G,D,A, S99AD, S101G,M,R S103A, V104I,Y,N, S106A, G118V,R, H120D,N, N123S, S128L, P129Q, S130A, G160D, Y167A, R170S, A194P, G195E, V199M, V205I, L217D, N218D, M222S, A232V, K235L, Q236H, Q245R, N252K, T274A (numbered using BPN').

[0456] Suitable commercially available proteases include those sold under the following trade names: Alcalase®, Blaze®; Duralase Tm 、Durazym Tm, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase® and Esperase®, all of which are available as Ultra® or Evity® (Novozymes A / S); those sold under the following trade names: Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect Prime®, Preferenz Tm , Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, Effectenz Tm , FN2®, FN3®, FN4®, Excellase®, Opticlean® and Optimase® (Danisco / DuPont), Axapem TM (Gist-Brocases N.V.), BLAP (the sequence of which is shown in FIG. 29 of US 5352604) and its variants (Henkel AG) and KAP (Bacillus alkalophilus subtilisin) from Kao Corporation

[0457] Amylase: In one aspect, a preferred additional enzyme is an amylase. Suitable amylases can be α-amylase or glucoamylase and can be of bacterial or fungal origin. This includes chemically modified mutants or protein-engineered mutants. Amylases include, for example, α-amylases obtained from the genus Bacillus, such as the α-amylase of a specific strain of Bacillus licheniformis more particularly described in GB 1296839

[0458] Suitable amylases include the amylase having SEQ ID NO: 3 in WO 95 / 10603 or variants thereof having 90% sequence identity with SEQ ID NO: 3. Preferred variants are described in SEQ ID NO: 4 of WO 94 / 02597, WO 94 / 18314, WO 97 / 43424, and WO 99 / 019467, such as variants having substitutions at one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181, 188, 190, 197, 201, 202, 207, 208, 209, 211, 243, 264, 304, 305, 391, 408, and 444.

[0459] Different suitable amylases include the amylase having SEQ ID NO: 6 in WO 02 / 010355 or variants thereof having 90% sequence identity with SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having deletions at positions 181 and 182 and a substitution at position 193.

[0460] Other suitable amylases are hybrid α - amylases comprising residues 1 - 33 of an α - amylase from Bacillus amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36 - 483 of a Bacillus licheniformis α - amylase shown in SEQ ID NO: 4 of WO 2006 / 066594 or variants thereof having 90% sequence identity. Preferred variants of the hybrid α - amylase are those having substitutions, deletions, or insertions at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, I201, A209, and Q264. The most preferred variants of the hybrid α - amylase comprising residues 1 - 33 of an α - amylase from Bacillus amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36 - 483 of SEQ ID NO: 4 are those having the following substitutions:

[0461] M197T;

[0462] H156Y + A181T + N190F + A209V + Q264S; or

[0463] G48A + T49I + G107A + H156Y + A181T + N190F + I201F + A209V + Q264S.

[0464] Another suitable amylase is the amylase having SEQ ID NO: 6 in WO 99 / 019467 or a variant thereof having 90% sequence identity with SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having a substitution, deletion, or insertion at one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269. Particularly preferred amylases are those having a deletion at position R181 and G182, or at position H183 and G184.

[0465] Other amylases that can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2, or SEQ ID NO: 7 in WO 96 / 023873 or a variant thereof having 90% sequence identity with SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 7. Preferred variants of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 7 are those having a substitution, deletion, or insertion at one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304, and 476. More preferred variants are those having a deletion at position 181 and 182 or at position 183 and 184. The most preferred amylase variants of SEQ ID NO: 1, SEQ ID NO: 2, or SEQ ID NO: 7 are those having a deletion at position 183 and 184 and a substitution at one or more of the following positions: 140, 195, 206, 243, 260, 304, and 476.

[0466] Other amylases that can be used are the amylase having SEQ ID NO: 2 in WO 08 / 153815, SEQ ID NO: 10 in WO 01 / 66712 or a variant thereof having 90% sequence identity with SEQ ID NO: 2 in WO 08 / 153815 or 90% sequence identity with SEQ ID NO: 10 in WO 01 / 66712. Preferred variants of SEQ ID NO: 10 in WO 01 / 66712 are those having a substitution, deletion, or insertion at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264.

[0467] Other suitable amylases are the amylase having SEQ ID NO: 2 of WO 09 / 061380 or variants thereof having 90% sequence identity to SEQ ID NO: 2. Preferred variants of SEQ ID NO: 2 are those having a C-terminal truncation, and / or substitution, deletion, or insertion at one or more of the following positions: Q87, Q98, S125, N128, T131, T165, K178, R180, S181, T182, G183, M201, F202, N225, S243, N272, N282, Y305, R309, D319, Q320, Q359, K444, and G475. More preferred variants of SEQ ID NO: 2 are those having a substitution at one or more of the following positions: Q87E,R, Q98R, S125A, N128C, T131I, T165I, K178L, T182G, M201L, F202Y, N225E,R, N272E,R, S243Q,A,E,D, Y305R, R309A, Q320R, Q359E, K444E, and G475K, and / or those having a deletion at position R180 and / or S181 or T182 and / or G183. The most preferred amylase variants of SEQ ID NO: 2 are those having the following substitutions:

[0468] N128C + K178L + T182G + Y305R + G475K;

[0469] N128C + K178L + T182G + F202Y + Y305R + D319T + G475K;

[0470] S125A + N128C + K178L + T182G + Y305R + G475K; or

[0471] S125A + N128C + T131I + T165I + K178L + T182G + Y305R + G475K, wherein these variants are C-terminal truncated and optionally further comprise a substitution at position 243 and / or a deletion at position 180 and / or position 181.

[0472] Other suitable amylases are the α - amylase having SEQ ID NO: 12 in WO 01 / 66712 or variants having at least 90% sequence identity with SEQ ID NO: 12. Preferred amylase variants are those having substitutions, deletions or insertions at one or more of the following positions in SEQ ID NO: 12 in WO 01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having deletions of D183 and G184 and having substitutions R118K, N195F, R320K and R458K, and variants having substitutions at one or more positions selected from the group consisting of: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345, and A339, most preferably variants having substitutions at all of these positions.

[0473] Other examples are amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078 and WO 2013 / 001087.

[0474] Commercially available amylases are Duramyl TM 、Termamyl TM 、Termamyl Ultra TM、 Fungamyl TM 、BAN TM 、Stainzyme TM 、Stainzyme Plus TM 、Amplify®、Amplify® Prime、Achieve® Choice、Achieve® Advance、Supramyl TM 、Natalase TM 、Liquozyme X and BAN TM (from Novozymes A / S), KEMZYM® AT9000 (Biozym Biotech Trading GmbH, Wehlistrasse 27b A - 1200 Wien Austria), and Rapidase TM, Purastar TM / Effectenz TM , Powerase, Preferenz S100, Preferenx S110, Preferenz S210, ENZYSIZE®, OPTISIZE HT PLUS®, and PURASTAR OXAM® (Danisco / DuPont) and KAM® (Kao Corporation).

[0475] Cellulase: In one aspect, preferred additional enzymes include cellulases. Suitable cellulases include those of bacterial or fungal origin. Include chemically modified mutants or protein-engineered mutants. Suitable cellulases include cellulases from the following genera: Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, such as the fungal cellulases produced by Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4435307, US 5648263, US 5691178, US 5776757, and WO 89 / 09259.

[0476] Particularly suitable cellulases are alkaline or neutral cellulases with color care benefits. Examples of such cellulases are those described in EP 0495257, EP 0531372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are cellulase variants such as those described in WO 94 / 07998, EP 0531315, US 5457046, US 5686593, US 5763254, WO 95 / 24471, WO 98 / 12307, and PCT / DK98 / 00299.

[0477] Commercially available cellulases include Celluzyme TM , and Carezyme TM (Novozymes), Clazinase TM , and Puradax HA TM (Genencor International), and KAC-500(B) TM (Kao Corporation).

[0478] In one aspect, other preferred enzymes include endoglucanases (EC 3.2.1.4) of microbial origin that exhibit endo-β-1,4-glucanase activity, including bacterial polypeptides endogenous to members of the genus Bacillus (polypeptides having a sequence with at least 90%, 94%, 97%, or 99% identity to amino acid sequence SEQ ID NO: 2 in US 7141403) and mixtures thereof. Suitable endoglucanases are sold under the trade names Celluclean® and Whitezyme® (Novozymes).

[0479] Pectate lyase, mannanase, DNase: The compositions of the present invention may additionally contain other preferred enzymes, which include pectate lyases, for example, pectate lyases sold under the trade names Pectawash®, Pectaway®, or Xpect®; and mannanases, for example, mannanases sold under the trade names Mannaway® (Novozymes) and Purabrite® (Danisco / DuPont). Finally, the compositions may also contain deoxyribonucleases (DNases).

[0480] DNase (deoxyribonuclease): In one aspect, a preferred additional enzyme is a DNase. The term "DNase" means a polypeptide having DNase activity that catalyzes the hydrolytic cleavage of phosphodiester bonds in the DNA backbone, thereby degrading DNA.

[0481] One or more detergent enzymes can be incorporated into the detergent composition by adding a separate additive containing one or more enzymes, or by adding a combined additive containing all of these enzymes. The detergent additives of the present invention, i.e., the separate additives or the combined additives, can be formulated, for example, as granules, liquids, slurries, etc. Preferred detergent additive formulations are granules, especially dust-free granules; liquids, especially stabilized liquids; or slurries.

[0482] Dust-free particles can be produced as disclosed, for example, in US 4106991 and US 4661452, and can optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycol, PEG) with an average molecular weight of 1000 to 20000; ethoxylated nonylphenols having 16 to 50 ethylene oxide units; ethoxylated fatty alcohols, where the alcohol contains 12 to 20 carbon atoms and where there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and monoglycerides, diglycerides, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluidized bed techniques are given in GB 1483591. Liquid enzyme preparations can be stabilized, for example, by adding polyols (such as propylene glycol), sugars or sugar alcohols, lactic acid or boric acid according to established methods. Protected enzymes can be prepared according to the method disclosed in EP 238216.

[0483] For any detergent composition to be used in an automatic washing machine, foam should not form to the extent that it overflows the washing machine. When in use, the foam inhibitor is preferably present in a "foam-inhibiting amount". "Foam-inhibiting amount" means that the formulator of the composition can choose the amount of this foam control agent that will adequately control the foam to result in a low-foaming laundry detergent for use in an automatic washing machine.

[0484] The compositions herein will generally contain from 0 wt% to 10 wt% of a foam inhibitor. When used as a foam inhibitor, monocarboxylic fatty acids and salts thereof will typically be present in amounts up to 5 wt%. Preferably, a fatty monocarboxylate foam inhibitor is used in an amount from 0.5 wt% to 3 wt%. Silicone foam inhibitors are typically used in amounts up to 2.0 wt%, although higher amounts can be used. Monostearyl phosphate foam inhibitors are generally used in amounts ranging from 0.1 wt% to 2 wt%. Hydrocarbon foam inhibitors are typically used in amounts ranging from 0.01 wt% to 5.0 wt%, although higher levels can be used. Alcohol foam inhibitors are typically used in amounts from 0.2 wt% to 3 wt%.

[0485] The compositions herein can have cleaning activity over a wide range of pH. In certain embodiments, the composition has cleaning activity from pH 4 to pH 11.5. In other embodiments, the composition has activity from pH 6 to pH 11, from pH 7 to pH 11, from pH 8 to pH 11, from pH 9 to pH 11, or from pH 10 to pH 11.5.

[0486] The compositions of the present invention can have cleaning activity within a wide range of temperatures (e.g., from 10 °C or lower to 90 °C). Preferably, the temperature will be below 50 °C or 40 °C or even 30 °C. In certain embodiments, the optimal temperature range for the compositions is from 10 °C to 20 °C, from 15 °C to 25 °C, from 15 °C to 30 °C, from 20 °C to 30 °C, from 25 °C to 35 °C, from 30 °C to 40 °C, from 35 °C to 45 °C, or from 40 °C to 50 °C.

[0487] Peptides that enhance / enhance the fat removal performance / activity of lipase

[0488] According to the present invention, the compositions of the present invention and the enzyme products of the present invention contain peptides (as defined herein) in addition to lipase. The peptides enhance / enhance the fat removal performance / activity of lipase.

[0489] According to the present invention, the compositions of the present invention and the enzyme products of the present invention contain one or more peptides selected from the group consisting of:

[0490] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2; and

[0491] ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10), a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or KNLRRIIRKGIHIKKYF (SEQ ID NO: 10).

[0492] Form of the composition

[0493] The compositions of the present invention are for cleaning or washing, especially for clothing. The compositions of the present invention are particularly liquid detergent compositions, but can also be solid or powder compositions.

[0494] In one aspect, the present invention relates to a composition, wherein the form of the composition is selected from the group consisting of: regular, compressed or concentrated liquid; gel; paste; soap bar; regular or compressed powder; granular solid; homogeneous or multi-layered tablet having two or more layers (same or different phases); pouch having one or more chambers; single or multiple chamber unit dosage form; or any combination thereof.

[0495] The form of the composition can physically separate the components from each other in multiple chambers (such as water-soluble pouches) or in different layers of the tablet. Thus, adverse storage interactions between the components can be avoided. In the washing solution, the different dissolution profiles of each chamber can also cause delayed dissolution of the selected components.

[0496] The pouch can be configured as a single chamber or multiple chambers. It can have any form, shape and material suitable for holding the composition, for example, before contact with water, it does not allow the composition to be released from the pouch. The pouch is made of a water-soluble film, which contains an internal volume. The internal volume can be divided into chambers of the pouch. Preferred films are polymer materials, preferably polymers forming films or sheets. Preferred polymers, copolymers or their derivatives are selected from polyacrylates, water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylate, most preferably polyvinyl alcohol copolymers and hydroxypropylmethylcellulose (HPMC). Preferably, the level of the polymer in the film such as PVA is at least about 60%. The preferred average molecular weight will typically be about 20,000 to about 150,000. The film can also be a blend composition, which contains a hydrolyzable and water-soluble polymer blend, such as polylactic acid and polyvinyl alcohol (known under trade reference number M8630, sold by MonoSol LLC, Indiana, USA) plus plasticizers, such as glycerol, ethylene glycol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain a solid laundry cleaning composition or partial components and / or a liquid cleaning composition or partial components separated by a water-soluble film. The chambers for the liquid components can be different in composition from the chambers containing solids (US 2009 / 0011970 A1).

[0497] Water - soluble film- The composition of the present invention can also be encapsulated within a water-soluble film. Preferably, the preferred film material is a polymeric material. The film material can be obtained, for example, by casting, blow molding, extrusion, or blown extrusion of the polymeric material, as known in the art. Preferred polymers, copolymers, or derivatives thereof suitable for use as bag materials are selected from polyvinyl alcohol, polyvinylpyrrolidone, polyalkylene oxides, acrylamide, acrylic acid, cellulose, cellulose ethers, cellulose esters, cellulose amides, polyvinyl acetate, polycarboxylic acids and salts, polyamino acids or peptides, polyamides, polyacrylamides, copolymers of maleic acid / acrylic acid, polysaccharides (including starch and gelatin), natural gums (such as xanthum gum and carragum gum). More preferred polymers are selected from polyacrylates and water-soluble acrylate copolymers, methylcellulose, sodium carboxymethylcellulose, dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, and most preferably from polyvinyl alcohol, polyvinyl alcohol copolymers, and hydroxypropylmethylcellulose (HPMC), and combinations thereof. Preferably, the level of the polymer (e.g., PVA polymer) in the bag material is at least 60 wt%. The polymer can have any weight average molecular weight, preferably from about 1,000 to 1,000,000, from about 10,000 to 300,000, from about 20,000 to 150,000. Mixtures of polymers can also be used as bag materials.

[0498] Naturally, different film materials and / or films of different thicknesses can be used to make the chambers of the present invention. The benefit in selecting different films is that the resulting chambers can exhibit different solubility or release characteristics.

[0499] Preferred film materials are PVA films known under the MonoSol trade names M8630, M8900, H8779, and those described in US 6166117 and US 6787512, and PVA films having corresponding solubility and deformation characteristics.

[0500] The film materials herein can also include one or more additive components. For example, it can be beneficial to add plasticizers such as glycerol, ethylene glycol, diethylene glycol, propylene glycol, sorbitol, and mixtures thereof. Other additives include functional detergent additives to be delivered to the wash water, such as organic polymer dispersants, etc.

[0501] In a preferred embodiment, the parent lipase is Thermomyces lanuginosus lipase (TLL), for example, especially the lipase shown in SEQ ID NO: 1.

[0502] It should be understood that for the foregoing species, the present invention encompasses the perfect and imperfect stages as well as other taxonomic equivalents, such as anamorphs, regardless of their known species names. Those skilled in the art will readily recognize the identity of appropriate equivalents.

[0503] Strains of these species are readily available to the public in many culture collections, such as the American Type Culture Collection (ATCC), the Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ), the Centraalbureau Voor Schimmelcultures (CBS), and the Agricultural Research Service Patent Culture Collection, Northern Regional Research Center (NRRL).

[0504] The foregoing probes can be used to identify the parental lipase and obtain the same from other sources, including microorganisms isolated from nature (e.g., soil, compost, water, etc.), or directly obtain a DNA sample from natural materials (e.g., soil, compost, water, etc.). Techniques for directly isolating microorganisms and DNA from natural habitats are well known in the art. The polynucleotide encoding the parent can then be obtained by similarly screening a genomic DNA or cDNA library or a mixed DNA sample of another microorganism. Once the polynucleotide encoding the parent has been detected with one or more probes, the polynucleotide can be isolated or cloned by utilizing techniques known to those of ordinary skill in the art (see, e.g., Sambrook et al., 1989, supra).

[0505] Enzyme products

[0506] In one aspect, the present invention relates to enzyme products comprising:

[0507] (a) one or more lipases; and

[0508] (b) one or more peptides selected from the group consisting of:

[0509] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 2; and

[0510] ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or 10, respectively.

[0511] The enzyme product of the present invention can be incorporated into the compositions of the present invention. The enzyme product of the present invention can be formulated in any suitable manner, and in particular can be in the form of a liquid or solid formulation.

[0512] In a preferred embodiment, the enzyme product comprises an enzyme stabilizer, such as those disclosed in the "enzyme stabilizer" section herein.

[0513] Liquid enzyme product formulation

[0514] The enzyme product of the present invention can be formulated into a liquid enzyme formulation, which is generally a pourable composition, although it may also have a high viscosity. The physical appearance and properties of the liquid enzyme product formulation can vary widely - for example, they may have different viscosities (from gel-like to watery), colored, uncolored, transparent, turbid, and even have solid particles (such as in slurries and suspensions). The minimum components are lipase, peptides (as defined herein), and a solvent system (to make it liquid). In addition to lipase and peptides, the liquid enzyme formulation can also contain other enzyme activities, such as protease, amylase, cellulase, phospholipase, cutinase, pectinase, mannanase, pectin lyase, nuclease (such as DNase, RNase) activity, or a mixture thereof.

[0515] The solvent system can comprise water, polyols (such as glycerol, (mono-, di- or tri-) propylene glycol, (mono-, di- or tri-) ethylene glycol, sugar alcohols (e.g., sorbitol, mannitol, erythritol, galactitol, inositol, xylitol or ribitol), polypropylene glycol, and / or polyethylene glycol), ethanol, sugars, and salts. Typically, the solvent system also includes preservatives and / or other stabilizers.

[0516] A liquid enzyme product formulation can be prepared by mixing a solvent system with an enzyme concentrate of desired purity (or enzyme particles to obtain a slurry / suspension).

[0517] In an embodiment, the liquid enzyme product comprises:

[0518] (a) at least 0.01% w / w lipase,

[0519] (b) one or more peptides as defined herein,

[0520] (c) at least 0.5% w / w polyol,

[0521] (d) water, and

[0522] (e) optionally a preservative.

[0523] The lipase in the liquid enzyme product of the present invention can be stabilized using conventional stabilizers. Examples of stabilizers include but are not limited to sugars such as glucose, fructose, sucrose, or trehalose; addition of salts to increase ionic strength; divalent cations (e.g., Ca2+ or Mg2+); and enzyme inhibitors, enzyme substrates, or various polymers (e.g., PVP). Selecting the optimal pH for the formulation can be very important for enzyme stability. The optimal pH depends on the specific enzyme but typically ranges from pH 4 - 9. In some cases, surfactants such as nonionic surfactants (e.g., alcohol ethoxylates) can improve the physical stability of the enzyme formulation.

[0524] One embodiment of the present invention relates to a composition comprising the enzyme product of the present invention, the composition further comprising:

[0525] (i) a polyol, preferably selected from glycerol, (mono-, di- or tri-) propylene glycol, (mono-, di- or tri-) ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, galactitol, inositol, xylitol, and ribitol;

[0526] (ii) optionally an additional enzyme, preferably selected from proteases and amylases,

[0527] (iii) optionally a surfactant, preferably selected from anionic and nonionic surfactants,

[0528] (iv) optionally a divalent cation, polymer, or enzyme inhibitor;

[0529] (v) optionally having a pH in the range of pH 4 - 9; and

[0530] (vi) water.

[0531] Slurries or dispersants of enzymes are typically prepared by dispersing small particles of the enzyme (e.g., spray-dried particles) in a liquid medium in which the enzyme is slightly soluble (e.g., a liquid non-ionic surfactant or a liquid polyethylene glycol). Powders can also be added in an amount to an aqueous system such that not all of it goes into solution (above the solubility limit). Another form is a crystal suspension, which can also be an aqueous liquid (see, e.g., WO 2019 / 002356). Another method of preparing such a dispersant is by preparing a water-in-oil emulsion, where the enzyme is in the aqueous phase and water is evaporated from the droplets. Such slurries / suspensions can be physically stabilized (to reduce or avoid sedimentation) by adding a rheology modifier such as fumed silica or xanthan gum, typically to achieve shear-thinning rheology.

[0532] Solid / granular enzyme formulations

[0533] The enzyme products of the present invention can also be formulated as solid / granular enzyme formulations. Dust-free granules can be produced as disclosed, for example, in US 4,106,991 and US 4,661,452, and can optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycol, PEG) with an average molecular weight of 1000 to 20000; ethoxylated nonylphenols with 16 to 50 ethylene oxide units; ethoxylated fatty alcohols, where the alcohol contains 12 to 20 carbon atoms and where there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and glycerol monoesters, and glycerol di-esters, and glycerol triesters of fatty acids. Examples of film-forming coating materials suitable for application by fluidized bed techniques are given in GB1483591.

[0534] The enzyme products of the present invention can be formulated as granules, for example, as co-granules combining one or more enzymes or beneficial reagents such as MnTACN or other bleaching components. Examples of such additional enzymes include proteases, amylases, cellulases, phospholipases, cutinases, pectinases, mannanases, pectin lyases, nucleases (e.g., DNases, RNases), or mixtures thereof. Then, each enzyme will be present in multiple granules, which ensures a more uniform distribution of the enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0535] Embodiments of the present invention relate to enzyme product particles / pellets comprising a lipase and a peptide as defined herein.

[0536] The granule consists of a core and optionally one or more coatings (outer layers) surrounding the core. Typically, the granule / particle size of the granule (measured as the equivalent spherical diameter (volume-based average particle size)) is 20 - 2000 µm, in particular 50 - 1500 µm, 100 - 1500 µm or 250 - 1200 µm.

[0537] The core can include additional materials such as fillers, fibrous materials (cellulose or synthetic fibers), stabilizers, solubilizers, suspending agents, viscosity modifiers, light spheres, plasticizers, salts, lubricants, and fragrances. The core can include binders such as synthetic polymers, waxes, fats, or carbohydrates. The core typically can contain salts of polyvalent cations, reducing agents, antioxidants, peroxide decomposition catalysts, and / or acidic buffer components as a homogeneous blend. The core can consist of inert particles, where the enzyme is adsorbed within the inert particles or applied (e.g., by fluidized bed coating) to the surface of the inert particles. The diameter of the core can be 20 - 2000 µm, in particular 50 - 1500 µm, 100 - 1500 µm or 250 - 1200 µm. The core can be prepared by blending granulating ingredients, for example by methods including granulation techniques such as crystallization, precipitation, pan-coating, fluidized bed coating, fluidized bed agglomeration, rotary atomization, extrusion, prilling, spheronization, particle size reduction methods, drum granulation, and / or high shear granulation. Methods for preparing the core can be found in Handbook of Powder Technology; Particle size enlargement by C. E. Capes; Volume 1; 1980; Elsevier. These methods are well known in the art and have also been described in International Patent Application WO2015 / 028567, pages 3 - 5, which is incorporated by reference.

[0538] The core of the enzyme granule / particle can be surrounded by at least one coating, for example, to improve storage stability, to reduce dust formation during handling, or for coloring the granule. Optional one or more coatings can include salt coatings or other suitable coating materials such as polyethylene glycol (PEG), methylhydroxypropylcellulose (MHPC), and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are shown in WO 93 / 07263 and WO 97 / 23606.

[0539] Such coatings are well known in the art and have been previously described, for example, in WO 00 / 01793, WO 2001 / 025412 and WO 2015 / 028567, which are incorporated herein by reference.

[0540] In one aspect, the present invention provides granules comprising:

[0541] (a) a core comprising at least a lipase and a peptide as defined herein; and

[0542] (b) optionally a (salt) coating consisting of one or more layers surrounding the core.

[0543] Another aspect of the present invention relates to layered granules comprising:

[0544] (a) a (non-enzyme) core;

[0545] (b) a coating surrounding the core, wherein the coating comprises a lipase and a peptide as defined herein; and

[0546] (c) optionally a (salt) coating consisting of one or more layers surrounding the coating containing the lipase and the peptide.

[0547] Encapsulated enzyme formulations

[0548] The enzyme products of the present invention can also be formulated as encapsulated enzyme formulations ("capsule products"). This is particularly useful for separating the enzyme and optionally the peptide from other ingredients when the enzyme is added to, for example, a (liquid) cleaning composition (such as the detergent compositions described below).

[0549] Physical separation can be used to address incompatibilities between one or more enzymes, and peptides as defined herein, and other components. Incompatibilities can occur if the other components react with the enzyme and / or peptide, or if the other components are substrates of the enzyme. Other enzymes can be substrates of, for example, proteases.

[0550] The enzyme and optionally the peptide as defined herein can be encapsulated in a matrix, preferably a water-soluble or water-dispersible matrix (such as water-soluble polymer particles), for example as described in WO 2016 / 023685. Examples of water-soluble polymer matrices are matrix compositions comprising polyvinyl alcohol. Such compositions are also used to encapsulate detergent compositions in unit dose formats.

[0551] The enzyme and optionally the peptide as defined herein can also be encapsulated in core-shell microcapsules, for example as described in WO 2015 / 144784 or as described in IP.com disclosure IPCOM000239419D.

[0552] Such core-shell capsules can be prepared using a variety of techniques known in the art, for example, interfacial polymerization using water-in-oil or oil-in-water emulsions, where the polymer crosslinks at the surface of the droplets in the emulsion (the interface between water and oil), thus forming a wall / membrane around each droplet / capsule.

[0553] Purification of enzymes in the formulation

[0554] The enzymes and peptides used in the above enzyme product formulations can be purified to any desired purity. This includes high levels of purification, for example, achieved by using crystallization methods, but also includes no purification or low levels of purification, for example, achieved by using a crude fermentation broth, as described in WO 2001 / 025411 or WO 2009 / 152176.

[0555] The peptides of the present invention

[0556] In one aspect, the present invention relates to peptides suitable for use in the compositions of the present invention. These peptides are capable of enhancing / enhancing the fat-removing performance / activity of lipases (especially the lipases disclosed herein). In a preferred embodiment, these peptides do not have enzyme activity, such as lipase activity.

[0557] In an embodiment, the peptide of the present invention is a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2.

[0558] In an embodiment, these peptides have a high K (Lys) content and / or a high R (Arg) content.

[0559] In an embodiment, the peptides defined above have K (Lys) at positions corresponding to position 2 and / or position 18 (numbered using SEQ ID NO: 2).

[0560] In an embodiment, the peptides defined above have R (Arg) at positions corresponding to position 6 and / or position 7 and / or position 10 and / or position 13 (numbered using SEQ ID NO: 2).

[0561] In an embodiment, the peptides defined above have at least 2 Ks, such as 3 Ks, such as 4 Ks, such as 5 Ks.

[0562] In an embodiment, the peptides defined above have at least 4 Rs, such as 5 Rs, such as 6 Rs, such as 7 Rs, or 8 Rs.

[0563] In embodiments, these peptides as defined above have at least 20% R (Arg), such as at least 25% R (Arg), particularly at least 30% R (Arg).

[0564] In embodiments, these peptides as defined above have at least 10% K (Lys), such as at least 15% K (Lys), particularly at least 20% K (Lys).

[0565] In embodiments, these peptides as defined above consist of 15 to 25 amino acids, such as 17 amino acids and 23 amino acids, such as 15 amino acids, such as 16 amino acids, such as at least 17 amino acids, such as 18 amino acids, particularly 19 amino acids, such as 20 amino acids, such as 21 amino acids, such as 22 amino acids, such as 23 amino acids, such as 24 amino acids, such as 25 amino acids.

[0566] In preferred embodiments, these peptides as defined above contain 19 amino acids or consist of 19 amino acids.

[0567] In one aspect, the peptides of the invention are peptides having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or are peptides having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10, respectively.

[0568] In embodiments, the peptides of the invention as defined above have a high K (Lys) content and / or a high R (Arg) content.

[0569] In embodiments, these peptides as defined above have K at the position corresponding to position 1 and / or position 9 and / or position 14 and / or position 15 (numbered using SEQ ID NO: 3), or have K at the position corresponding to position 1 and / or position 9 and / or position 15 and / or position 16 (numbered using SEQ ID NO: 10).

[0570] In embodiments, these peptides as defined above have R (Arg) at the position corresponding to position 4 and / or position 5 and / or position 8.

[0571] In embodiments, these peptides as defined above have at least 4 Ks, such as 5 Ks, such as 6 Ks, such as 7 Ks.

[0572] In an embodiment, these peptides defined above have at least 3 Rs, such as 4 Rs, such as 5 Rs, such as 6 Rs, or such as 8 Rs.

[0573] In an embodiment, these peptides defined above have at least 15% R (Arg), such as at least 20% R (Arg), particularly at least 25% R (Arg).

[0574] In an embodiment, these peptides defined above have at least 20% K (Lys), such as at least 25% K (Lys), particularly at least 3 Ks (Lys).

[0575] In an embodiment, these peptides defined above consist of 13 to 23 amino acids, such as 15 - 21 amino acids, such as 13 amino acids, such as 14 amino acids, such as 15 amino acids, such as 17 amino acids, particularly 17 amino acids, such as 18 amino acids, such as 19 amino acids, such as 20 amino acids, such as at least 21 amino acids, such as 22 amino acids, such as at least 23 amino acids.

[0576] In a preferred embodiment, these peptides defined above contain 17 or 18 amino acids or consist of 17 or 18 amino acids.

[0577] The present invention is described in the following paragraphs:

[0578] 1. A composition, the composition comprising:

[0579] (a) one or more lipases; and

[0580] (b) one or more peptides selected from the group consisting of:

[0581] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2; and / or

[0582] ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10, respectively.

[0583] 2. The composition as described in paragraph 1, wherein the composition comprises a surfactant or a surfactant system.

[0584] 3. The composition as described in paragraph 2, wherein the surfactant or the surfactant system is present at a level of from 0.1 wt% to 60 wt%, from 0.2 wt% to 40 wt%, from 0.5 wt% to 30 wt%, from 1 wt% to 50 wt%, from 1 wt% to 40 wt%, from 1 wt% to 30 wt%, from 1 wt% to 20 wt%, from 3 wt% to 10 wt%, from 3 wt% to 5 wt%, from 5 wt% to 40 wt%, from 5 wt% to 30 wt%, from 5 wt% to 15 wt%, from 3 wt% to 20 wt%, from 3 wt% to 10 wt%, from 8 wt% to 12 wt%, from 10 wt% to 12 wt%, from 20 wt% to 25 wt% or from 25 wt% - 60 wt%.

[0585] 4. The composition as described in any one of paragraphs 1 - 3, wherein the composition comprises a surfactant or a surfactant system, and the surfactant is selected from nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof.

[0586] 5. The composition as described in any one of paragraphs 1 - 4, wherein the composition comprises one or more anionic surfactants and / or one or more nonionic surfactants.

[0587] 6. The composition as described in any one of paragraphs 1 - 5, wherein the composition comprises one or more anionic surfactants, preferably linear alkylbenzene sulfonic acid (LAS), alcohol ether sulfate (AEOS) and / or alkyl sulfate (AS), especially sodium lauryl sulfate (SLS) or sodium laureth sulfate (SLES).

[0588] 7. The composition as described in any one of paragraphs 1 - 6, wherein the composition comprises one or more nonionic surfactants, preferably alcohol ethoxylate (AEO), especially linear alcohol (C12 - 15) ethoxylate.

[0589] 8. The composition as described in any one of paragraphs 1 - 7, wherein the composition comprises one or more anionic surfactants and one or more nonionic surfactants.

[0590] 9. The composition according to any one of paragraphs 1 - 8, wherein the composition comprises an anionic surfactant linear alkylbenzene sulfonic acid (LAS) and a nonionic surfactant alcohol ethoxylate (AEO).

[0591] 10. The composition according to any one of paragraphs 2 - 9, wherein the surfactant system comprises LAS, SLES, AS, and AEO.

[0592] 11. The composition according to any one of paragraphs 1 - 10, wherein the composition further comprises one or more components selected from the group consisting of: builders, chelating agents, dye transfer inhibitors, dispersants, enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, pre - formed peracids, polymeric dispersants, clay removal / anti - redeposition agents, brighteners, foam inhibitors, dyes, color - correcting dyes, fragrances, fragrance delivery systems, fabric softeners, carriers, hydrotropes, processing aids, solvents, and / or pigments.

[0593] 12. The composition according to any one of paragraphs 1 - 11, wherein the composition provides increased fat removal compared to when there is no peptide according to any one of the preceding paragraphs, particularly no peptide of SEQ ID NO: 2 and / or SEQ ID NO: 3 or SEQ ID NO: 10, especially when used for cleaning or washing, particularly when used for washing laundry.

[0594] 13. The composition according to any one of paragraphs 1 - 12, wherein the composition is formulated as a regular, compressed, or concentrated liquid; gel; paste; bar soap; regular or compressed powder; granular solid; homogeneous or multi - layer tablet having two or more layers (same or different phases); pouch having one or more chambers; single or multiple chamber unit dosage form; or any combination thereof.

[0595] 14. The composition according to any one of paragraphs 1 - 13, wherein the lipase is of microbial origin, particularly of fungal or bacterial origin.

[0596] 15. The composition according to any one of paragraphs 1 - 14, wherein the composition comprises a fungal lipase derived from a strain of Thermomyces lanuginosus (synonym: Humicola lanuginosa), particularly the lipase shown in SEQ ID NO: 1 or a variant thereof.

[0597] 16. The composition according to any one of paragraphs 1 - 15, wherein the lipase is

[0598] i) a lipase that has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 1;

[0599] ii) a parental lipase variant having lipase activity, which variant has at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% but less than 100% sequence identity with the lipase as shown in SEQ ID NO: 1;

[0600] iii) a fragment of the lipase in i) or ii) that has lipase activity.

[0601] 17. The composition according to any one of paragraphs 1 - 16, wherein the lipase is a variant that comprises substitutions at positions corresponding to T231R + N233R of SEQ ID NO: 1 and optionally at least one or more (e.g., several) of D96E, D111A, D254S, G163K, P256T, G91T, and G38A.

[0602] 18. The composition according to any one of paragraphs 1 - 17, wherein the lipase is a variant of a parental lipase, wherein the variant has lipase activity, has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity with SEQ ID NO: 1, and comprises substitutions at positions corresponding to T231R + N233R of SEQ ID NO: 1 and at least one or more (e.g., several) of D96E, D111A, D254S, G163K, P256T, G91T, and G38A, and these positions are selected from the group consisting of:

[0603] a. D96E + T231R + N233R;

[0604] b. N33Q + D96E + T231R + N233R;

[0605] c. N33Q + D111A + T231R + N233R;

[0606] d. N33Q + T231R + N233R + P256T;

[0607] e.N33Q + G38A + G91T + G163K + T231R + N233R + D254S;

[0608] f.N33Q + G38A + G91T + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0609] g.D27R + N33Q + G38A + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0610] h.D27R + N33Q + G38A + G91T + D96E + D111A + G163K + T231R + N233R + P256T;

[0611] i.D27R + N33Q + G38A + G91T + D96E + D111A + G163K + T231R + N233R + D254S;

[0612] j.D27R + G38A + G91T + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0613] k.D96E + T231R + N233R + D254S;

[0614] l.T231R + N233R + D254S + P256T;

[0615] m.G163K + T231R + N233R + D254S;

[0616] n.D27R + N33Q + G38A + G91T + D96E + G163K + T231R + N233R + D254S + P256T;

[0617] o.D27R + G91T + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0618] p.D96E + G163K + T231R + N233R + D254S;

[0619] q.D27R + G163K + T231R + N233R + D254S;

[0620] r.D27R + G38A + G91T + D96E + D111A + G163K + T231R + N233R + D254S;

[0621] s.D27R+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;

[0622] t.D27R+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0623] u.D27R+D96E+G163K+T231R+N233R+D254S;

[0624] v.D27R+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0625] w.D27R+G38A+D96E+G163K+T231R+N233R+D254S+P256T

[0626] x.D111A+G163K+T231R+N233R+D254S+P256T;

[0627] y.D111A+T231R+N233R;

[0628] z.D111A+T231R+N233R+D254S+P256T;

[0629] aa.D27R+D96E+D111A+G163K+T231R+N233R;

[0630] bb.D27R+D96E+D111A+T231R+N233R;

[0631] cc.D27R+N33Q+G38A+D96E+D111A+T231R+N233R+D254S+P256T;

[0632] dd.D27R+G38A+D96E+D111A+G163K+E210Q+T231R+N233R+D254S+P256T;

[0633] ee.D27R+T231R+N233R+D254S+P256T;

[0634] ff.D96E+D111A+G163K+T231R+N233R;

[0635] gg.D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0636] hh. D96E + D111A + G163K + T231R + N233R + P256T;

[0637] ii. D96E + D111A + T231R + N233R;

[0638] jj. D96E + D111A + T231R + N233R + D254S;

[0639] kk. D96E + D111A + T231R + N233R + D254S + P256T

[0640] ll. D96E + D111A + T231R + N233R + P256T;

[0641] mm. D96E + G163K + T231R + N233R + D254S + P256T;

[0642] nn. D96E + T231R + N233R + D254S + P256T;

[0643] oo. D96E + T231R + N233R + P256T;

[0644] pp. G38A + D96E + D111A + T231R + N233R;

[0645] qq. G91T + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0646] rr. G91T + D96E + D111A + T231R + N233R;

[0647] ss. G91T + D96E + T231R + N233R;

[0648] tt. G91T + T231R + N233R + D254S + P256T;

[0649] uu. N33Q + D96E + D111A + G163K + T231R + N233R + D254S + P256T;

[0650] vv. T231R + N233R + D254S + P256T;

[0651] ww. T231R + N233R + P256T.

[0652] 19. A composition according to any one of paragraphs 1 - 18, wherein the lipase is a variant of a parental lipase, wherein the variant

[0653] (a) Comprising a modification at at least one position corresponding to positions E1, V2, N33, F51, E56, L69, K98, V176, H198, E210, Y220, L227, and K237 of SEQ ID NO: 1; and optionally further comprising a modification at at least one position corresponding to positions D27, G38, D96, D111, G163, T231, N233, D254, and P256 of SEQ ID NO: 1;

[0654] (b) Having at least 60% but less than 100% sequence identity with SEQ ID NO: 1;

[0655] (c) Having lipase activity.

[0656] 20. The composition according to any one of paragraphs 1-19, wherein the lipase variant comprises a modification in at least one of the following positions: E1, V2, D27, N33, G38, F51, E56, L69, D96, K98, D111, G163, V176, H198, E210, Y220, L227, T231, N233, K237, D254, and P256, numbered according to SEQ ID NO: 1.

[0657] 21. The composition according to any one of paragraphs 19 or 20, wherein the lipase variant comprises at least one of the following modifications: E1C, V2Y, D27R, N33K, N33Q, G38A, F51V, E56K, L69R, D96E, D96L, K98I, K98Q, D111A, G163K, V176L, H198S, E210K, Y220F, L227G, T231R, N233R, N233C, K237C, D254S, and P256T, numbered according to SEQ ID NO: 1.

[0658] 22. The composition according to any one of paragraphs 19-21, wherein the lipase variant further comprises one substitution selected from the group consisting of: S54T, S83T, G91A, A150G, I255A, and E239C, numbered according to SEQ ID NO: 1.

[0659] 23. The composition according to any one of paragraphs 19-22, wherein the lipase variant comprises the substitution E1C+N233C and one or more additional substitutions, numbered according to SEQ ID NO: 1.

[0660] 24. A composition as described in any one of paragraphs 19 - 23, wherein the variant has lipase activity, has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity with SEQ ID NO: 1, and comprises or consists of substitutions corresponding to one of the following sets of substitutions numbered using SEQ ID NO: 1:

[0661]

[0662]

[0663]

[0664]

[0665] 25. A composition as described in any one of paragraphs 1 - 24, wherein the lipase is a lipase variant of a parental lipase, the variant has lipase activity, has at least 60% but less than 100% sequence identity with SEQ ID NO: 1, and comprises one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, E56R, D57N, V60E,K, K98I, N101D, R118F, G163S, Y220F, T231R, N233R, T244E, and P256T.

[0666] 26. A composition as described in any one of paragraphs 1 - 25, wherein the lipase is a lipase variant that comprises substitutions at positions corresponding to T231R + N233R, and one or more (e.g., several) substitutions at positions corresponding to G23S, D27N, A40I, F51I,L, E56R, D57N, V60E,K, K98I, N101D, R118F, G163S, Y220F, T244E, and P256T.

[0667] 27. A composition as described in any one of paragraphs 1 - 26, wherein the lipase is a lipase variant that comprises substitutions corresponding to any of the following sets of substitutions (numbered using SEQ ID NO: 1):

[0668]

[0669] 28. A composition as described in any one of paragraphs 1 - 27, wherein the lipase is a lipase variant that comprises substitutions corresponding to any of the following sets of substitutions (numbered using SEQ ID NO: 1):

[0670]

[0671] 28. A composition according to any one of paragraphs 1-27, wherein the lipase variant is selected from the group consisting of:

[0672] a) a polypeptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or 100% sequence identity to SEQ ID NO: 1; and

[0673] b) a fragment of the polypeptide of SEQ ID NO: 1.

[0674] 29. A composition according to any one of paragraphs 1-28, wherein the lipase variant has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% but less than 100% sequence identity to SEQ ID NO: 1.

[0675] 30. A composition according to paragraphs 1-14, wherein the lipase is

[0676] i) a lipase having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or 100% sequence identity to SEQ ID NO: 4;

[0677] ii) a fragment of the lipase in i) having lipase activity.

[0678] 31. A composition according to paragraph 30, wherein the composition comprises or consists of Geotrichum candidum lipase 1 (GCL 1) as shown in SEQ ID NO: 4.

[0679] 32. A composition according to any one of paragraphs 1-31, the composition further comprising one or more enzymes selected from: α-amylase, protease, cellulase, phospholipase, cutinase, pectinase, mannanase, pectin lyase, nuclease (e.g., DNase, RNase) activity, or a mixture thereof.

[0680] 33. A composition as described in any one of paragraphs 1-32, the composition comprising a lipase, in particular the Thermomyces lanuginosus lipase (TLL) or a variant thereof disclosed in SEQ ID NO: 1 herein, in particular a variant disclosed herein, or the Geotrichum candidum lipase 1 (GCL 1) disclosed in SEQ ID NO: 4 herein, a peptide of SEQ ID NO: 2 or 3, and a DNase and / or a protease.

[0681] 34. A composition as described in any one of paragraphs 1-33, wherein the combination of the lipase and the peptide as defined in any one of paragraphs 1-33 enhances the fat removal performance / activity of the lipase.

[0682] 35. A method for cleaning or washing laundry, the method comprising contacting the laundry with a composition as described in any one of paragraphs 1-34.

[0683] 36. The method as described in paragraph 35, wherein the laundry includes textiles, clothes, linen, etc., and the laundry can be made of any material, the material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile materials, fabrics made of these materials and products made of these fabrics (e.g., clothing and other articles).

[0684] 37. The method as described in paragraph 35 or 36, wherein the laundry is in the form of knitted fabric, woven fabric, denim, non-woven fabric, felt, yarn, and terry cloth.

[0685] 38. The method as described in any one of paragraphs 35-37, wherein the laundry is cellulose-based, such as natural cellulose products, including cotton, linen / flax, jute, ramie, sisal or coir fiber, or man-made cellulose products (e.g., derived from wood pulp), including viscose fiber / rayon, cellulose acetate fiber (triacetate), lyocell fiber or blends thereof, or wherein the laundry is non-cellulose-based, such as natural polyamides, including wool, camel hair, cashmere, mohair, rabbit hair and silk, or synthetic polymers such as nylon, aramid, polyester, acrylate, polypropylene and spandex / elastane, or blends thereof and blends of cellulose-based fibers and non-cellulose-based fibers, particularly wherein the blend is a blend of cotton and / or rayon / viscose fiber with one or more accompanying materials, the accompanying materials such as wool, synthetic fibers (e.g., polyamide fiber, acrylic fiber, polyester fiber, polyvinyl chloride fiber, polyurethane fiber, polyurea fiber, aramid fiber) and / or cellulose-containing fibers (e.g., rayon / viscose fiber, ramie, linen / flax, jute, cellulose acetate fiber, lyocell fiber).

[0686] 39. The method according to any one of paragraphs 35 - 38, wherein the article of clothing is a conventional washable article of clothing, such as a household article of clothing with stains.

[0687] 40. The method according to any one of paragraphs 35 - 39, wherein the lipase is administered at a concentration of 0.001 - 5 ppm, in particular 0.01 - 1 ppm.

[0688] 41. The method according to any one of paragraphs 35 - 40, wherein the peptide is administered at a concentration of 0.001 - 100 ppm, in particular 0.01 - 50 ppm.

[0689] 42. An enzyme product, comprising:

[0690] (a) one or more lipases, in particular lipases as defined in any one of the preceding paragraphs; and

[0691] (b) one or more peptides selected from the group consisting of:

[0692] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2; and

[0693] ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10, respectively.

[0694] 43. The enzyme product according to paragraph 42, wherein the product is formulated as a liquid enzyme formulation.

[0695] 44. The enzyme product according to paragraph 42 or 43, wherein the product further comprises a solvent system to make it liquid.

[0696] 45. An enzyme product as described in any one of paragraphs 42 - 44, wherein the enzyme product comprises a solvent selected from the group consisting of water, polyols (such as glycerol, (mono-, di- or tri-) propylene glycol, (mono-, di- or tri-) ethylene glycol, sugar alcohols (e.g., sorbitol, mannitol, erythritol, galactitol, inositol, xylitol or ribitol), polypropylene glycol, and / or polyethylene glycol), ethanol, sugars, and salts.

[0697] 46. An enzyme product as described in any one of paragraphs 42 - 45, wherein the enzyme product comprises a preservative and / or other stabilizers, such as sugars including glucose, fructose, sucrose, or trehalose; salts to increase ionic strength; divalent cations (e.g., Ca2+ or Mg2+); and enzyme inhibitors, enzyme substrates, or polymers (e.g., PVP).

[0698] 47. An enzyme product as described in any one of paragraphs 42 - 46, wherein the product further comprises other enzyme activities, such as protease, amylase, cellulase, phospholipase, cutinase, pectinase, mannanase, pectin lyase, nuclease (e.g., DNase, RNase) activity, or a mixture thereof.

[0699] 48. An enzyme product as described in any one of paragraphs 42 - 47, the enzyme product comprising:

[0700] (a) at least 0.01% w / w lipase, particularly a lipase as defined in any one of paragraphs 1 - 34;

[0701] (b) one or more peptides selected from the group consisting of:

[0702] i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2; and

[0703] ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10, respectively,

[0704] (c) at least 0.5% w / w polyol,

[0705] (d) water, and

[0706] (e) optionally a preservative.

[0707] 49. An enzyme product as described in any one of paragraphs 42 - 48, wherein the pH is in the range of pH 4 - 9.

[0708] 50. An enzyme product as described in any one of paragraphs 42 - 49, wherein the enzyme product further comprises:

[0709] (i) a polyol, preferably selected from glycerol, (mono-, di- or tri-) propylene glycol, (mono-, di- or tri-) ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, galactitol, inositol, xylitol and ribitol;

[0710] (ii) optionally an additional enzyme, preferably selected from proteases, DNases and / or amylases;

[0711] (iii) optionally a surfactant, preferably selected from anionic and nonionic surfactants;

[0712] (iv) optionally a divalent cation, a polymer, or an enzyme inhibitor;

[0713] (v) optionally having a pH in the range of pH 4 - 9; and

[0714] (vi) water.

[0715] 51. An enzyme product as described in any one of paragraphs 42 - 50, wherein the product is formulated as a solid / granular enzyme formulation.

[0716] 52. An enzyme product as described in any one of paragraphs 42 - 51, wherein the product comprises a waxy coating material, such as a poly(ethylene oxide) product (polyethylene glycol, PEG) with an average molar mass of 1000 to 20000; ethoxylated nonylphenol having 16 to 50 ethylene oxide units; ethoxylated fatty alcohols, wherein the alcohol contains 12 to 20 carbon atoms and wherein there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and glycerol monoesters, and glycerol di-esters, and glycerol tri-esters of fatty acids.

[0717] 53. An enzyme product as described in any one of paragraphs 42 - 52, wherein the enzyme product is formulated as a granule, such as a co-granule formulated by combining one or more enzymes or beneficial reagents (such as MnTACN or other bleaching components).

[0718] 54. An enzyme product as described in any one of paragraphs 42 - 53, wherein the enzyme product further comprises an enzyme from the group consisting of protease, amylase, cellulase, phospholipase, cutinase, pectinase, mannanase, pectin lyase, nuclease (such as DNase, RNase), or a mixture thereof.

[0719] 55. An enzyme product as described in any one of paragraphs 42 - 54, wherein the particle consists of a core and optionally one or more coatings (outer layers) surrounding the core.

[0720] 56. An enzyme product as described in any one of paragraphs 42 - 55, wherein the particle size / granularity of the particle, measured as equivalent spherical diameter (volume - based average particle size), is 20 - 2000 µm, particularly 50 - 1500 µm, 100 - 1500 µm or 250 - 1200 µm.

[0721] 57. An enzyme product as described in any one of paragraphs 42 - 56, wherein the core comprises additional materials such as fillers, fibrous materials (cellulose or synthetic fibers), stabilizers, solubilizers, suspending agents, viscosity modifiers, light spheres, plasticizers, salts, lubricants and fragrances.

[0722] 58. An enzyme product as described in any one of paragraphs 42 - 57, wherein the core comprises a binder, such as a synthetic polymer, wax, fat, or carbohydrate. The core typically may contain salts of polyvalent cations, reducing agents, antioxidants, peroxide - decomposing catalysts and / or acidic buffer components as a homogeneous blend. The core may consist of inert particles, wherein the enzyme is adsorbed within the inert particles or is applied (e.g., by fluidized - bed coating) onto the surface of the inert particles.

[0723] 59. An enzyme product as described in any one of paragraphs 42 - 58, wherein the diameter of the core is 20 - 2000 µm, particularly 50 - 1500 µm, 100 - 1500 µm or 250 - 1200 µm.

[0724] 60. An enzyme product as described in any one of paragraphs 42 - 59, wherein the core is surrounded by at least one coating (e.g., a salt coating), or other suitable coating materials (e.g., polyethylene glycol (PEG), methyl hydroxy - propyl cellulose (MHPC) and polyvinyl alcohol (PVA)).

[0725] 61. An enzyme product as described in any one of paragraphs 42 - 60, wherein the product comprises particles, and the particles comprise:

[0726] (a) A core, the core comprising at least lipase and a peptide selected from the group consisting of:

[0727] (i) A peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 2; and

[0728] (ii) A peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or 10, respectively; and

[0729] (b) An optional (salt) coating consisting of one or more layers surrounding the core.

[0730] 62. The enzyme product according to any one of paragraphs 42 - 61, wherein the product is a layered granule, the granule comprising:

[0731] (a) A (non - enzyme) core;

[0732] (b) A coating surrounding the core, wherein the coating comprises a lipase and a peptide selected from the group consisting of:

[0733] (i) A peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 2; and

[0734] (ii) A peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or 10, respectively; and

[0735] (c) An optional (salt) coating consisting of one or more layers surrounding the enzyme-containing coating.

[0736] 63. An enzyme product as described in any one of paragraphs 42 - 62, wherein the product is formulated as an encapsulated enzyme formulation ("capsulized").

[0737] 64. A peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 2.

[0738] 65. A peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity with SEQ ID NO: 3 or 10 respectively.

[0739] 66. Use of the peptide as described in paragraph 64 or 65 for enhancing the fat removal performance / activity of lipase.

[0740] The present invention is further described by the following examples, which should not be construed as limiting the scope of the present invention.

[0741] Materials and Methods

[0742] Lipase LIP1: Thermomyces lanuginosus lipase (TLL) shown in SEQ ID NO: 1, which has the following substitutions: T231R + N233R (available from Novozymes A / S, Denmark).

[0743] Determination of lipase activity by p - nitrophenyl (pNP) assay

[0744] The hydrolytic activity of lipase can be determined by kinetic assays using p-nitrophenyl acyl esters as substrates. A 100 mM stock solution of each of the following substrates in DMSO can be diluted to a final concentration of 1 mM - 25 mM in assay buffer (50 mM Tris; pH 7.7; 0.4% Triton X-100): p-nitrophenyl butyrate (C4), p-nitrophenyl caproate (C6), p-nitrophenyl decanoate (C10), p-nitrophenyl laurate (C12), and p-nitrophenyl palmitate (C16) (all from Sigma-Aldrich Danmark A / S, Kirkebjerg Allé 84, 2605 Brøndby; catalogue numbers: C3: N-9876, C6: N-0502, C10: N-0252, C12: N-2002, C16: N-2752). Lipase in 50 mM Hepes (pH 8.0); 10 ppm Triton X-100; + / - 20 mM CaCl2 can be added to the substrate solution in a 96-well NUNC plate (catalogue number: 260836, Kamstrupvej 90, DK-4000, Roskilde) at the following final protein concentrations: 0.01 mg / ml; 5 × 10 -3 mg / ml; 2.5 × 10 -4 mg / ml and 1.25 × 10 -4 mg / ml. p-Nitrophenol released by p-nitrophenyl acyl hydrolysis can be monitored at 405 nm at 10-second intervals for 5 minutes on a Spectra max 190 (Molecular Devices GmbH, Bismarckring 39, 88400 Biberach an der Riss, Germany).

[0745] Construction of variants by site - directed mutagenesis

[0746] Site-directed variants can be constructed by traditional DNA fragment cloning using PCR together with correctly designed mutagenic oligonucleotides that introduce the desired mutations in the resulting sequence (Sambrook et al., Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor, 1989).

[0747] Design mutagenic oligonucleotides corresponding to the DNA sequences flanking one or more desired mutation sites, separated by DNA base pairs defining the insertion / deletion / substitution, and purchased from oligonucleotide suppliers such as Life Technologies.

[0748] To test these variants, the mutant DNA encoding the variants was integrated into a competent Aspergillus oryzae strain by homologous recombination, fermented using a standard protocol (yeast extract-based medium, 3 - 4 days, 30 °C), and purified by chromatography.

[0749] Examples

[0750] Example 1

[0751] Washing experiment with lipase and peptide X (SEQ ID NO: 2)

[0752] Prepare a standard detergent J washing solution by dissolving 0.8 g / l of standard detergent J containing 5% LAS, 10% SLES, 5% AS, 5% AEO (Biosoft N25 - 7 (NI)), 1% soap (all percentages are w / w) in water with a hardness of 6° dH.

[0753] Add 40 mL to a 50 mL test tube containing 10 5 mm steel balls. Prepare a cloth sample by melting coconut oil (100%) and taking 25 µL and adding it to a 2 cm diameter disc of WFK80A textile. Heat the cloth sample at 100 °C for 20 minutes and cool, then measure the weight using a precision balance (Mettler Toledo).

[0754] After adding 4 prepared coconut oil cloth samples to the liquid mixture, add the following combination of peptide X (5 ppm) and purified lipase LIP1 (0.15 ppm) to the corresponding test tubes, and then continuously stir at 40 rpm at 25 °C for 30 minutes. The peptide X sequence is as follows: PKGLLRRFLRALRILVPKD.

[0755] Rinse under cold water in a beaker for 5 minutes, then dry on filter paper. First, heat the cloth sample to be weighed at 100 °C for 20 minutes and cool for 1 - 2 hours, then weigh it.

[0756]

[0757] Example 2

[0758] Washing experiment with lipase and peptide Y (SEQ ID NO: 10)

[0759] The standard detergent J washing solution was prepared by dissolving 0.8 g / l of standard detergent J containing 5% LAS, 10% SLES, 5% AS, 5% AEO (Biosoft N25-7 (NI)), and 1% soap (all percentages are w / w) in water with a water hardness of 6° dH.

[0760] 40 mL was added to a 50 mL test tube containing 10 5-mm steel balls. The coconut oil cloth sample was prepared by melting coconut oil (100%) and taking 25 μL and adding it to a 2-cm diameter disc of WFK80A textile. The cloth sample was heated at 100 °C for 20 minutes and then cooled, and then weighed using a precision balance (Mettler Toledo).

[0761] After adding 4 prepared cloth samples to the liquid mixture, the following combination of peptide Y (5 ppm) and purified lipase LIP1 (0.15 ppm) was added to the corresponding test tubes, and then continuously stirred at 25 °C at 40 rpm for 30 minutes. The peptide Y sequence is as follows: KNLRRIIRKGIHIKKYF.

[0762] Rinse under the tap with cold water in a beaker for 5 minutes, and then dry on filter paper. First, heat the coconut oil cloth sample to be weighed at 100 °C for 20 minutes and then cool for 1 - 2 hours, and then weigh it.

[0763]

[0764] The invention described and claimed herein is not limited to the scope of the specific aspects disclosed herein, as these aspects are intended to be illustrative of several aspects of the invention. Any equivalent aspects are intended to be within the scope of the invention. Indeed, various modifications of the invention, in addition to those shown and described herein, will become apparent to those skilled in the art from the foregoing description. Such modifications are also intended to fall within the scope of the appended claims. In case of conflict, the present disclosure, including the definitions, shall prevail.

Claims

1. A composition, the composition comprising: (a) one or more lipases; and (b) one or more peptides selected from the group consisting of: i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 2; and / or ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or 10, respectively.

2. The composition according to claim 1, wherein the composition comprises a surfactant or a surfactant system, wherein the surfactant is selected from nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof.

3. The composition according to claim 1 or 2, wherein the composition provides increased fat removal compared to when no peptide as defined in any of the preceding claims is present, especially SEQ ID NO: 2 and / or SEQ ID NO: 3 or SEQ ID NO: 10, especially when used for cleaning or washing, especially when used for washing laundry.

4. The composition according to any one of claims 1 - 3, the composition further comprising one or more enzymes selected from the group consisting of: α - amylase, protease, cellulase, phospholipase, cutinase, pectinase, mannanase, pectin lyase, nuclease (e.g., DNase, RNase) activity, or mixtures thereof.

5. A method for cleaning or washing laundry, the method comprising contacting the laundry with the composition according to any one of claims 1 - 4.

6. An enzyme product, the enzyme product comprising: (a) one or more lipases, especially a lipase as defined in any one of the preceding claims; and (b) one or more peptides selected from the group consisting of: i) a peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 2; and ii) a peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10), or a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or SEQ ID NO: 10, respectively.

7. A peptide having the sequence PKGLLRRFLRALRILVPKD (SEQ ID NO: 2) or having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:

2.

8. A peptide having the sequence KNLRRIIRKGIHIKKYF (SEQ ID NO: 3) or KNLRRIIRKGIHIIKKYF (SEQ ID NO: 10), a peptide having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 3 or SEQ ID NO: 10, respectively.

9. Use of the peptide according to claim 7 or 8 for enhancing the fat-removing performance / activity of lipase.

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