Hard surface cleaning compositions and cleaning methods

Abstract

1. A hard surface cleaning composition comprising: (a) 0.1 to 60% by weight of a surfactant system; (b) 0.1 to 40% by weight of a solvent selected from the group consisting of lower alkanols, benzyl alcohols, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, linear alcohol ethoxylates, branched alcohols, oxoalcohol ethoxylates, and combinations thereof; and (c) optionally 0.001 to 10% by weight of a lipase.

Description

[Technical Field]

[0001] Sequence Listing Reference This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference.

[0002] The present invention relates to a cleaning composition for removing stains, especially fatty or grease-containing soils, from hard surfaces, such as the surfaces of dishes or kitchen benches. The present invention also relates to a method for cleaning hard surfaces and to a ready-to-use article comprising said composition. [Background technology]

[0003] Hard surface cleaning compositions are useful for various surfaces, such as industrial surfaces and household surfaces (e.g., kitchen surfaces). Between cleanings, various stains, such as greasy stains, dust, and even biofilms, quickly accumulate on these surfaces and become difficult to remove. To facilitate cleaning, conventional hard surface cleaners have a high pH (usually above pH 10). However, high pH cleaners are harsh on the skin of hands and the environment. High pH can also damage surface materials, such as coatings, resulting in a rough surface, which in turn makes stain removal even more difficult. In addition, the cleaning performance of conventional detergents with high pH may not be good enough for tough stains, such as oily kitchen stains, in some cases. Summary of the Invention [Problem to be solved by the invention]

[0004] Therefore, there is a need to develop hard surface cleaning compositions with milder pH and improved cleaning performance compared to that of conventional cleaning compositions with high pH.

[0005] On the other hand, lipases have not been shown to satisfy cleaning performance boosting in some current detergent formulations, which limits their application, for example, in hard surface cleaning detergents. Therefore, it is essential to develop detergent formulations that allow lipases to perform meaningfully and consistently to promote the removal of greasy soils, such as oily kitchen stains. [Means for solving the problem]

[0006] The present invention: (a) 0.1 to 60 wt. % of a surfactant system; (b) 0.1 to 40 wt. % of a solvent selected from the group consisting of lower alkanols, benzyl alcohol, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, e.g., linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10% by weight of lipase; The present invention relates to a hard surface cleaning composition comprising:

[0007] The cleaning compositions of the present invention may further comprise one or more ingredients selected from the group of builders, chelating agents, dispersants, enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric dispersants, suds suppressors, dyes, fragrances, structural plasticizers, carriers, hydrotropes, processing aids, pigments, and / or additional enzymes.

[0008] In a preferred embodiment, the cleaning composition of the present invention comprises one or more lipases set forth in any one of SEQ ID NOs: 1, 2, 3, 4, 5, 6, or 7, or variants thereof.

[0009] In one embodiment, the cleaning composition of the present invention comprises a commercially available lipase product selected from the group of Lipolase™, Lipex™; Lipolex™, Lipoclean™, Lipex Evity 100L, Lipex Evity 105T, Lipex Evity 200L (manufactured by Novozymes), Lumafast (originally manufactured by Genencor), Preferenz L100 (Danisco US Inc.), and Lipomax (originally manufactured by Gist-Brocades).

[0010] In one embodiment, the cleaning composition of the present invention comprises ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene-propylene glycol ethers, ethylene glycol phenyl ether, propylene glycol phenyl ether, propylene glycol methyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, tripropylene glycol butyl ether, tripropylene glycol methyl ether, ethylene glycol butyl ether, diethylene glycol methyl ether, diethylene glycol butyl ether, ethylene glycol dimethyl ether, ethylene glycol propyl ether, diethylene glycol ethyl ether, triethylene glycol The solvent may be selected from glycol methyl ether, triethylene glycol ethyl ether, triethylene glycol butyl ether, ethylene glycol monobutyl ether, diethylene glycol monobutyl ether, triethylene glycol monobutyl ether, dipropylene glycol monobutyl ether, diethylene glycol monobutyl ether, hexyl ethoxylates (e.g., ethylene glycol monohexyl ether), 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, and combinations thereof, such as a combination of ethanol and diethylene glycol monobutyl ether, glycol ether, propylene glycol, or dipropylene glycol.

[0011] The present invention also relates to a method of cleaning a hard surface comprising contacting the surface with the hard surface cleaning composition of the present invention.

[0012] The present invention further relates to a ready-to-use article (eg, a wipe or sponge) for cleaning hard surfaces, which article comprises the hard surface cleaning composition of the present invention.

[0013] Array Overview SEQ ID NO: 1 is the wild-type Thermomyces lanuginosus lipase (synonym Humicola lanuginosa DSM 4109 lipase), often simply referred to as "TLL." SEQ ID NO:2 is a variant of the Thermomyces lanuginosus lipase disclosed as SEQ ID NO:2 in WO 2019 / 154952. SEQ ID NO: 3 is a lipase from Geotrichum candidum. SEQ ID NO: 4 is a lipase from Geotrichum candidum. SEQ ID NO: 5 is a lipase from Geotrichum candidum. SEQ ID NO: 6 is a lipase from Geotrichum candidum. SEQ ID NO: 7 is a lipase from Geotrichum candidum.

[0014] The present invention will now be described in more detail with reference to the accompanying drawings, which show exemplary embodiments of the invention. [Brief explanation of the drawings]

[0015] [Figure 1] DM-90 stained tiles washed under various washing conditions are shown. [Figure 2] Figure 1 shows the cleaning performance of model detergent V2 (pH 8) with and without lipase on mixed oil and fat stains at a 15 minute soak time. DETAILED DESCRIPTION OF THE INVENTION

[0016] definition As used herein, the singular forms "a," "an," and "the" are intended to include the plural forms as well, unless the context clearly indicates otherwise.

[0017] Unless otherwise indicated, all references to percentages with respect to the disclosed compositions relate to weight percent based on the total weight of the respective composition.

[0018] Lipase: The terms "lipase," "lipase enzyme," "lipolytic enzyme," "lipid esterase," "lipolytic polypeptide," and "lipolytic protein" refer to enzymes in class EC 3.1.1 as defined by enzyme nomenclature. These 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 purposes of the present invention, lipase activity (i.e., the hydrolytic activity of a lipase) may be determined by the pNP assay using substrates of various chain lengths, as described in Assay I in the Examples section.

[0019] Fragment: The term "fragment" refers to a polypeptide having one or more (e.g., several) amino acids located away from the amino and / or carboxyl termini of the 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%, but less than 100%, of the number of amino acids 1 to 269 of SEQ ID NO: 1 or 2.

[0020] Parent or Parent Lipase: The term "parent" or "parent lipase" refers to a lipase that is altered to produce an enzyme variant. A parent lipase can be a naturally occurring (wild-type) polypeptide, but can also be a variant and / or fragment thereof. In a preferred embodiment, the parent lipase can be that set forth in SEQ ID NO: 1, 2, 3, 4, 5, 6, or 7.

[0021] Wild-type lipase: The term "wild-type" lipase refers to a lipase expressed by a naturally occurring microorganism, such as a bacterium, yeast, or filamentous fungus, as found in nature. In one embodiment, the wild-type lipase can be that set forth in SEQ ID NO: 1, which is derived from Thermomyces lanuginosus DSM 4109 (synonym Humicola lanuginosa DSM 4109) or the Absidia sp. lipase set forth in SEQ ID NO: 3 of WO 2021 / 001400.

[0022] Cleaning Ingredients: The term "cleaning ingredient" is defined herein to mean a class of chemicals that can be used in cleaning compositions. Examples of cleaning ingredients include alkalis, surfactants, solvents, hydrotropes, builders, co-builders, chelators or chelating agents, bleaching systems or components, polymers, suds boosters, suds suppressors, dispersants, dye transfer inhibitors, fragrances, bactericides, fungicides, corrosion inhibitors, soil suspending agents, soil release polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, preservatives, solvents, and solubilizers.

[0023] Cleaning composition: The term "cleaning composition" (which may also be referred to as "detergent composition") refers to a composition used to remove unwanted compounds from an item to be cleaned, such as a hard surface. Cleaning compositions may be used, for example, for household cleaning and commercial cleaning. The term encompasses all materials / compounds selected for the particular type of cleaning composition desired and product form (e.g., liquid, gel, powder, granule, paste, or spray composition). In addition to containing a lipase of the present invention, the cleaning compositions of the present invention may contain one or more additional enzymes (e.g., amylase, protease, cellulase, mannanase, hemicellulase, peroxidase, xylanase, phospholipase, esterase, cutinase, keratinase, reductase, oxidase, phenoloxidase, lipoxygenase, ligninase, pullulanase, malanase, β-glucanase, arabinosidase, hyaluronidase, laccase, deoxyribonuclease (DNase), hexosaminidase, and peroxidase, or any mixture thereof) and / or cleaning ingredients described above.

[0024] Alkyl: The term "alkyl" refers to a monovalent hydrocarbon radical having the specified number of carbon atoms, either straight or branched. Alkyl groups can be unsubstituted or substituted with substituents that do not interfere with the intended function of the composition, and can be substituted one to two times with the same or different groups. Substituents can include, for example, alkoxy, hydroxy, mercapto, amino, alkyl-substituted amino, nitro, carboxy, carbanyl, carbanyloxy, cyano, methylsulfonylamino, or halogen. Examples of "alkyl" include, but are not limited to, methyl, ethyl, n-propyl, isopropyl, n-butyl, s-butyl, t-butyl, n-pentyl, n-hexyl, 3-methylpentyl, and the like.

[0025] Sequence identity: The relationship between two amino acid sequences or two nucleotide sequences is described by the parameter "sequence identity." For purposes of the present invention, the sequence identity between two amino acid sequences is determined as the "longest identity" output using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16:276-277), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and an EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In order for the Needle program to report the longest identity, the nobrief option must be specified on the command line. The Needle output labeled "longest identity" is calculated as follows: (identical residues × 100) / (length of alignment−total number of gaps in the alignment).

[0026] Variant: The term "variant" refers to a polypeptide / enzyme that has the same activity as a parent enzyme, but contains alterations, i.e., substitutions, insertions, and / or deletions, at one or more (e.g., several) positions. A substitution refers to the replacement of an amino acid occupying a position with a different amino acid; a deletion refers to the removal of an amino acid occupying a position; and an insertion refers to the addition of an amino acid adjacent to and immediately after the amino acid occupying a position. In the context of the present invention, a specified lipase variant has the enzymatic activity of the parent. In one embodiment, the lipase activity of the variant is increased compared to the parent lipase, for example, an enzyme comprising or consisting of the amino acid sequence of SEQ ID NO: 1 or the amino acid sequence set forth in SEQ ID NO: 2.

[0027] Hard Surface: The term "hard surface" includes household surfaces such as showers, sinks, toilets, bathtubs, countertops, windows, mirrors, floors, etc., and industrial surfaces such as transport vehicles, storage tanks, bioreactors, fermenters, mixing tubes, pipelines, bottling line equipment, and other equipment used in biotech manufacturing, e.g., pharmaceutical manufacturing, food and beverage manufacturing. The term may also include surfaces of medical or dental devices that come into contact with a patient, whether the patient is human or an animal. Exemplary hard surfaces may be surfaces of steel, rubber, plastic, glass, ceramic, melamine, wood, coated surfaces, cement countertops, kitchen countertops, endoscopes, orthoscopic scalpels, hemostats, Kocher forceps, tracheotomy instruments, etc.

[0028] Rules for naming variants For purposes of the present invention, the lipase disclosed as SEQ ID NO: 1 is used to determine corresponding amino acid residues in another lipase. The amino acid sequence of another lipase is aligned with SEQ ID NO: 1, and based on the alignment, the amino acid position number corresponding to every amino acid residue in the polypeptide disclosed in SEQ ID NO: 1 is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48:443-453) as implemented in the Needle program of the EMBOSS 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 (EMBOSS version of BLOSUM62) substitution matrix.

[0029] The identification of corresponding amino acid residues in other lipases can be determined by alignment of multiple polypeptide sequences using several computer programs using their respective default parameters, including, but not limited to, MUSCLE (multiple sequence comparison with logarithmic prediction; 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 employing ClustalW (1.83 or later; Thompson et al., 1994, Nucleic Acids Research 22:4673-4680).

[0030] Other pairwise sequence comparison algorithms can be used if other enzymes diverge from the lipase of SEQ ID NO: 1, such that traditional sequence-based comparisons do not detect their relationship (Lindahl and Elofsson, 2000, J. Mol. Biol. 295:613-615). Greater sensitivity in sequence-based searches can be achieved using search programs that utilize probabilistic representations of polypeptide families (profiles) to search databases. For example, the PSI-BLAST program generates profiles through an iterative database search process to detect distant homologs (Atschul et al., 1997, Nucleic Acids Res. 25:3389-3402). Even greater sensitivity can be achieved if a polypeptide family or superfamily has more than one representative in a protein structure database. Programs such as GenTHREADER (Jones, 1999, J. Mol. Biol. 287:797-815; McGuffin and Jones, 2003, Bioinformatics 19:874-881) utilize information from a variety of sources (PSI-BLAST, secondary structure prediction, structural alignment profiles, and solvation potential) as input to a neural network that predicts the structural fold for 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 with superfamily models present in the SCOP database. These alignments can then be used to generate homology models for the polypeptide, and such models can be assessed for accuracy using a variety of tools developed for this purpose.

[0031] Several tools and resources are available for searching and generating structural alignments for proteins with known structures. For example, proteins of the SCOP superfamily have been structurally aligned, and this alignment can be accessed and downloaded. Two or more protein structures can be aligned using various algorithms, such as distance alignment matrices (Holm and Sander, 1998, Proteins 33:88-96) or combinatorial extension (Shindyalov and Bourne, 1998, Protein Engineering 11:739-747), and implementations of these algorithms can additionally be used to search structural databases with a structure of interest to find possible structural homologs (e.g., Holm and Park, 2000, Bioinformatics 16:566-567).

[0032] In describing variants used in connection with the present invention, the following nomenclature has been adapted for ease of reference: Accepted IUPAC single-letter or three-letter amino acid abbreviations are used.

[0033] Substitutions: For amino acid substitutions, the following nomenclature is used: original amino acid, position, substituted amino acid. Thus, a substitution of threonine at position 226 with alanine is designated "Thr226Ala" or "T226A." Multiple mutations are separated by additional markers ("+"), e.g., "Gly205Arg+Ser411Phe" or "G205R+S411F" represent substitutions of glycine (G) with arginine (R) and serine (S) with phenylalanine (F) at positions 205 and 411, respectively.

[0034] Deletions: For amino acid deletions, the following nomenclature is used: original amino acid, position, *. Thus, a deletion of glycine at position 195 is designated "Gly195*" or "G195*". Multiple deletions are separated by additional markers ("+"), for example, "Gly195*+Ser411*" or "G195*+S411*".

[0035] Insertions: For amino acid insertions, the following nomenclature is used: original amino acid, position, original amino acid, inserted amino acid. Thus, an insertion of lysine after glycine at position 195 is designated as "Gly195GlyLys" or "G195GK." Multiple amino acid insertions are designated as [original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2, etc.]. For example, an insertion of lysine and alanine after glycine at position 195 is designated as "Gly195GlyLysAla" or "G195GKA."

[0036] In such cases, the inserted amino acid residue is numbered by adding a lower case letter to the position number of the amino acid residue preceding the inserted amino acid residue. In the above example, the sequence would thus become:

[0037] [Table 1]

[0038] Multiple changes: Variants containing multiple changes are separated by additional marks ("+"), for example, "Arg170Tyr+Gly195Glu" or "R170Y+G195E" represent substitutions of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively.

[0039] Differential modifications. When different modifications can be introduced at a position, the different modifications are separated by commas, for example, "Arg170Tyr,Glu" or "R170Y,E" represents a substitution of arginine at position 170 with tyrosine or glutamic acid. Thus, "Tyr167Gly,Ala+Arg170Gly,Ala" represents the following variant: "Tyr167Gly+Arg170Gly", "Tyr167Gly+Arg170Ala", "Tyr167Ala+Arg170Gly", and "Tyr167Ala+Arg170Ala" are shown.

[0040] The inventors have surprisingly found that the inclusion of a lipase together with a solvent in a hard surface cleaning composition can achieve enhanced cleaning effectiveness and improved cleaning efficiency, especially for removing oily or greasy stains. As a result, compared with conventional high-pH hard surface cleaning detergents, the cleaning composition of the present invention can not only achieve better cleaning effectiveness, but also save time and labor costs. In addition, the pH of the cleaning composition can be lowered, for example, from pH 11 to a milder pH (e.g., less than pH 9 or neutral pH) without compromising cleaning effectiveness / cleaning performance.

[0041] Cleaning Compositions of the Present Invention A first aspect of the present invention comprises: (a) 0.1 to 60 wt. % of a surfactant system; (b) 0.1 to 40 wt. % of a solvent selected from the group consisting of lower alkanols, benzyl alcohol, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, e.g., linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10% by weight of lipase; The present invention relates to a hard surface cleaning composition comprising:

[0042] The compositions of the present invention may be formulated as ready-to-use detergents or as concentrates (e.g., 2x, 5x, 10x concentrated) that can be diluted on-site before application. Enzymes (e.g., lipases) may be added when formulating the concentrates or may be added to the diluted versions on-site.

[0043] composition ingredients The non-limiting list of composition ingredients illustrated below are suitable for use in the compositions and methods of the present invention and may desirably be incorporated in certain embodiments of the present invention to promote or enhance cleaning performance, for example, for treatment of the hard surface to be cleaned, or to modify the aesthetics of the composition in the case of fragrances, colorants, dyes, etc. The exact nature of these ingredients, and their level of incorporation, will depend on the physical form of the composition and the nature of the cleaning operation for which it is to be used. The ingredients set forth below are categorized by general headings according to specific functionality, but this should not be construed as limiting, as ingredients may include additional functionality, as will be well understood by those skilled in the art.

[0044] Suitable ingredient 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, soil removers, suds suppressors, dyes, perfumes, perfume delivery systems, carriers, hydrotropes, processing aids, and solvents. In addition to the disclosure below, suitable examples of such other ingredients and usage levels can be found in U.S. Patent Nos. 5,576,282, 6,306,812, and 6,326,348, which are incorporated herein by reference.

[0045] surfactant or surfactant system The detergent or cleaning compositions of the present invention comprise a surfactant or surfactant system, a lipase, and a solvate. In one embodiment, the surfactant system comprises at least one surfactant selected from nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof.

[0046] The surfactant is typically present at a level of 0.1 to 60 wt%, 0.2 to 40 wt%, 0.5 to 30 wt%, 1 to 50 wt%, 1 to 40 wt%, 1 to 30 wt%, 1 to 20 wt%, 3 to 10 wt%, 3 to 5 wt%, 5 to 40 wt%, 5 to 30 wt%, 5 to 15 wt%, 2 to 20 wt%, 3 to 6 wt%, 8 to 12 wt%, 10 to 12 wt%, 20 to 25 wt%, or 25 to 60 wt%.

[0047] Suitable anionic surfactants include sulfate and sulfonate detergent surfactants.

[0048] Suitable sulfonate surfactants include alkyl benzene sulfonates, in one aspect, C 10~13 Suitable alkylbenzene sulfonates (LAS) can be obtained by sulfonating commercially available linear alkylbenzenes (LAB); suitable LABs include lower 2-phenyl LABs such as Isochem® or Petrelab®, while other suitable LABs include higher 2-phenyl LABs such as Hyblene®. Suitable anionic detersive surfactants include alkylbenzene sulfonates obtained by the DETAL catalytic process, although other synthetic routes, such as HF, may also be suitable. In one embodiment, the magnesium salt of LAS is used.

[0049] Suitable sulfate surfactants include alkyl sulfates, in one aspect, C 8~18 Alkyl sulfate or mainly C 12 Alkyl sulfates are included.

[0050] Other suitable sulfate surfactants include alkyl alkoxylated sulfates, in one aspect alkyl ethoxylated sulfates, and in one aspect C 8~18 Alkyl alkoxylated sulfates, in another embodiment C 8~18 The alkyl ethoxylated sulfates are typically alkyl alkoxylated sulfates having an average degree of alkoxylation of 0.5 to 20 or 0.5 to 10, and typically alkyl alkoxylated sulfates having an average degree of ethoxylation of 0.5 to 10, 0.5 to 7, 0.5 to 5, or 0.5 to 3. 8~18 It is an alkyl ethoxylated sulfate.

[0051] The alkyl sulfates, alkyl alkoxylated sulfates, and alkyl benzene sulfonates may be linear or branched, and may be substituted or unsubstituted.

[0052] The surfactant may 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 a mid-chain branched alkyl benzene sulfonate, such as a mid-chain branched alkyl sulfate. In one aspect, the mid-chain branched alkyl 1~4 Alkyl groups, typically methyl and / or ethyl groups.

[0053] Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular linear alkylbenzene sulfonates (LAS), LAS isomers, branched alkylbenzene sulfonates (BABS), phenylalkane sulfonates, alpha-olefin sulfonates (AOS), olefin sulfonates, alkenesulfonates, alkane-2,3-diylbis(sulfonates), 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, Examples of suitable surfactants include alpha-sulfofatty acids (alpha-SFMe or SES), alkyl- or alkenyl succinic acids, dodecenyl / tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid, or soaps, and combinations thereof.

[0054] The anionic surfactant may be present at a level of 0.2 to 30%, 0.5 to 25%, 1 to 20%, 2 to 15%, 3 to 12%, 4 to 10%, 5 to 15%, or 6 to 8% by weight.

[0055] Suitable nonionic surfactants are: C8-C 18 Alkyl ethoxylates, such as NEODOL®; C-C alkyl alkoxylates, where the alkoxylate units can be ethyleneoxy units, propyleneoxy units, or mixtures thereof. 12 Alkylphenol alkoxylate; C with ethylene oxide / propylene oxide block polymer 12 ~C 18 Alcohol and C6-C 12Condensates with alkylphenols, e.g., Pluronic®; 14 ~C 22 Medium-chain branched alcohols; typically with an average degree of alkoxylation of 1 to 30, C 14 ~C 22 The surfactant is selected from the group consisting of: medium-chain branched alkyl alkoxylates; alkyl polysaccharides, and in one aspect, alkyl polyglycosides; polyhydroxy fatty acid amides; ether-terminated poly(oxyalkylated) alcohol surfactants; and mixtures thereof.

[0056] Suitable non-ionic cleansing surfactants include alkyl polyglucosides and / or alkyl alkoxylated alcohols.

[0057] In one embodiment, the nonionic detersive surfactant is an alkyl alkoxylated alcohol, in one embodiment C 8~18 Alkyl alkoxylated alcohols, such as C 8~18 Included are alkyl ethoxylated alcohols, and the average degree of alkoxylation of the alkyl alkoxylated alcohols can be from 1 to 50, from 1 to 30, from 1 to 20, or from 1 to 10. In one embodiment, the alkyl alkoxylated alcohols are C alkoxylated alcohols having an average degree of ethoxylation of from 1 to 10, from 1 to 7, or even from 1 to 5 or from 3 to 7. 8~18 The alkyl alkoxylated alcohol may be an alkyl ethoxylated alcohol. The alkyl alkoxylated alcohol may be linear or branched, and may be substituted or unsubstituted. Suitable nonionic surfactants include Lutensol®.

[0058] Non-limiting examples of nonionic surfactants include alcohol ethoxylates (AE or AEO), such as linear alcohol (C12-15) ethoxylates (LAE), alcohol propoxylates, propoxylated fatty alcohols (PFAs), 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.

[0059] Suitable cationic cleansing surfactants include alkyl pyridinium compounds, alkyl quaternary ammonium compounds, alkyl quaternary phosphonium compounds, alkyl tertiary sulfonium compounds, and mixtures thereof.

[0060] Suitable cationic detersive surfactants have the general formula: (R)(R1)(R2)(R3)N + X - wherein R is a linear or branched, substituted or unsubstituted C 6~18 R1 and R2 are independently selected from methyl or ethyl moieties; R3 is a hydroxyl, hydroxymethyl, or hydroxyethyl moiety; and X is an anion that provides charge neutrality. Suitable anions include halides, such as chloride; sulfate; and sulfonate. Suitable cationic cleansing surfactants include mono C 6~18 Alkyl monohydroxyethyl dimethyl quaternary ammonium chlorides are highly suitable cationic cleaning surfactants, such as mono C 8~10Alkylmonohydroxyethyldimethyl quaternary ammonium chloride, mono C 10~12 Alkyl monohydroxyethyl dimethyl quaternary ammonium chloride, and mono C 10 Alkyl monohydroxyethyl dimethyl quaternary ammonium chlorides are available.

[0061] Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quaternary salts (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quaternary salts, and combinations thereof.

[0062] Suitable zwitterionic surfactants include amine oxides and betaines, such as alkyldimethylbetaines, sulfobetaines, or combinations thereof. Amine-neutralized anionic surfactants—The anionic surfactants and auxiliary anionic co-surfactants can exist in acid form, which can be neutralized to form surfactant salts desirable for use in the detergent compositions. Typical neutralizing agents include metal counterion bases such as hydroxides, e.g., NaOH or KOH. Further preferred agents for neutralizing the anionic surfactants and auxiliary anionic surfactants or co-surfactants of the present invention in their acid form include ammonia, amines, or alkanolamines. Alkanolamines are preferred. Suitable non-limiting examples include monoethanolamine, diethanolamine, triethanolamine, and other linear or branched alkanolamines known in the art, such as highly preferred alkanolamines, such as 2-amino-1-propanol, 1-aminopropanol, monoisopropanolamine, or 1-amino-3-propanol. Neutralization with an amine can be carried out to a total or partial extent; for example, a portion of the anionic surfactant mixture can be neutralized with sodium or potassium, or a portion of the anionic surfactant mixture can be neutralized with an amine or alkanolamine.

[0063] Non-limiting examples of semi-polar surfactants include amine oxides (AOs), such as alkyldimethylamine oxides.

[0064] The surfactant system of the present invention may comprise at least one surfactant selected from the group consisting of nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof. A preferred weight ratio of anionic surfactant to nonionic surfactant is at least 2:1 or at least 1:1 to 1:10.

[0065] In one embodiment, the composition of the present invention comprises one or more anionic surfactants and / or one or more nonionic surfactants.

[0066] In a preferred embodiment, the compositions of the present invention comprise one or more anionic surfactants, preferably from the group of the linear alkylbenzene sulfonic acids (LAS), alcohol ether sulfates (AEOS), and / or alkyl sulfates (AS), in particular sodium lauryl sulfate (SLS) and sodium laureth sulfate (SLES).

[0067] In one embodiment, the compositions of the present invention comprise one or more non-ionic surfactants, preferably alcohol ethoxylates (AEOs), in particular linear alcohols (C 12~15 ) Ethoxylate (LAE).

[0068] In one embodiment, the composition of the present invention comprises the anionic surfactant linear alkylbenzene sulfonate (LAS) and the nonionic surfactant alcohol ethoxylate (AEO).

[0069] In one embodiment, the compositions of the present invention comprise the anionic surfactant sodium laureth sulfate (SLES) and the nonionic surfactant alcohol ethoxylate (AEO).

[0070] The nonionic surfactant may be present at a level of 0.2 to 30%, 0.5 to 25%, 1 to 20%, 2 to 15%, 3 to 12%, 4 to 10%, or 6 to 8% by weight.

[0071] In one embodiment, the ratio of anionic surfactant to nonionic surfactant is in the range of 1:10 to 10:1, for example, 1:5 to 5:1 or 1:3 to 2:1.

[0072] In a specific embodiment, the composition comprises a surfactant system as set forth in Table 1 below.

[0073] solvent The cleaning compositions of the present invention may contain a solvent, for example, to improve soil removal properties or to adjust the viscosity of the final composition. Suitable solvents useful in the present invention include, but are not limited to, lower alkanols, benzyl alcohol, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, such as linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates.

[0074] Exemplary solvents include, but are not limited to, ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene-propylene glycol ethers, ethylene glycol phenyl ether, propylene glycol phenyl ether, propylene glycol methyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, tripropylene glycol butyl ether, tripropylene glycol methyl ether, ethylene glycol butyl ether, diethylene glycol methyl ether, diethylene glycol butyl ether, ethylene glycol dimethyl ether, ethylene glycol propyl ether, diethylene glycol ethyl ether, triethylene glycol methyl ether, glycol methyl ether, triethylene glycol ethyl ether, triethylene glycol butyl ether, ethylene glycol monobutyl ether, diethylene glycol monobutyl ether, triethylene glycol monobutyl ether, dipropylene glycol monobutyl ether, diethylene glycol monobutyl ether, hexyl ethoxylates (e.g., ethylene glycol monohexyl ether), 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, and combinations thereof, such as combinations of ethanol and diethylene glycol monobutyl ether, glycol ether, propylene glycol, or dipropylene glycol.

[0075] Suitable alcohol ethoxylates are linear (preferably C 4~10) alcohol ethoxylates, branched alcohols, and oxo alcohol ethoxylates. The ethoxylation number may preferably be 1, 2, 3, 4, 5, 6, 7, or 8. In one embodiment, a suitable solvent of the present invention comprises at least one alcohol ethoxylate, such as hexyl ethoxylate (e.g., 2-(hexyloxy)ethanol), 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, and the like.

[0076] The solvent may be present at a level of 0.1 to 40%, 0.2 to 35%, 0.5 to 30%, 1 to 25%, 2 to 20%, 3 to 15%, 4 to 12%, 5 to 10%, or 6 to 8% by weight.

[0077] In one embodiment, two or more solvents are combined, for example, ethanol and diethylene glycol monobutyl ether, ethanol, diethylene glycol monobutyl ether and propylene glycol, ethanol and propylene glycol, or isopropanol and dipropylene glycol.

[0078] In one embodiment, the cleaning composition comprises one or more alcohol ethoxylates. For example, the cleaning composition comprises a hexyl ethoxylate (e.g., 2-(hexyloxy)ethanol) and further comprises one or more other solvents selected from dipropylene glycol monobutyl ether, diethylene glycol ethyl ether, triethylene glycol methyl ether, triethylene glycol ethyl ether, triethylene glycol butyl ether, ethylene glycol monobutyl ether, diethylene glycol monobutyl ether, triethylene glycol monobutyl ether, dipropylene glycol monobutyl ether, diethylene glycol monobutyl ether, 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, and dipropylene glycol.

[0079] In one embodiment, the cleaning composition comprises one or more lower alkyl glycol ether solvents. For example, the cleaning composition comprises ethylene glycol monohexyl ether (CEO) and further comprises one or more ester solvents selected from dipropylene glycol monobutyl ether, diethylene glycol ethyl ether, triethylene glycol methyl ether, triethylene glycol ethyl ether, triethylene glycol butyl ether, ethylene glycol monobutyl ether, diethylene glycol monobutyl ether, triethylene glycol monobutyl ether, dipropylene glycol monobutyl ether, diethylene glycol monobutyl ether, 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, and phenoxyethanol.

[0080] In one embodiment, the cleaning composition comprises two solvents: ethylene glycol monohexyl ether (CEO) and dipropylene glycol monobutyl ether (DPGBE), preferably in a weight ratio of 1:10 to 10:1, such as 1:5 to 5:1, 1:2 to 3:1, for example about 1:1.

[0081] stabilizers Stabilizers that can be used in the cleaning composition include, but are not limited to, primary aliphatic amines, betaine, borate, calcium ions, sodium citrate, citric acid, sodium formate, glycerin, malonic acid, organic diacids, polyols, propylene glycol, and mixtures thereof. Exemplary ranges of the stabilizer can be 0 to 20% by weight, e.g., about 0.5% to about 15% by weight, about 2% to about 10% by weight. In one embodiment, the stabilizer is sodium citrate or sodium carbonate.

[0082] In one embodiment of the cleaning composition, the amount of stabilizer is preferably from about 0.01% to about 5% by weight; more preferably from about 0.05% to about 2.5% by weight; most preferably from about 0.1% to about 1% by weight.

[0083] soap The compositions of the present invention may also contain soap. Without being limited by theory, it may be desirable to include soap to act partially as a surfactant and partially as a builder, and may be useful for suds suppression. Any soap known in the art for use in laundry detergents may be utilized. In one embodiment, the composition contains 0% to 20%, 0.5% to 20%, 4% to 10%, or 4% to 7% by weight of soap.

[0084] Examples of soaps useful herein include oleic acid soap, palmitic acid soap, palm kernel fatty acid soap, and mixtures thereof.Typical soaps are in the form of a mixture of fatty acid soaps with different chain lengths and degrees of substitution.One such mixture is topped palm kernel fatty acid.

[0085] In a preferred embodiment, the composition comprises coconut fatty acids. Other suitable fatty acids include saturated and / or unsaturated fatty acids, which 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, beef and fish oils, fats and oils, and mixtures thereof), or can be prepared synthetically (e.g., via oxidation of petroleum or by hydrogenation of carbon monoxide via the Fischer-Tropsch process).

[0086] Hydrotrope The compositions of the present invention may also contain one or more hydrotropes. Hydrotropes are compounds that solubilize hydrophobic compounds in aqueous solutions (or substances of opposite polarity in a nonpolar environment). Typically, hydrotropes possess both hydrophilic and hydrophobic properties (so-called amphiphilicity, as known from 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 occurs, as is found for surfactants and lipids that form micellar, lamellar, or other well-defined mesophases. Instead, many hydrotropes exhibit a continuous aggregation process in which the size of the aggregates increases with increasing concentration. However, many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing polar and nonpolar substances, including mixtures of water, oil, surfactants, and polymers. The use of hydrotropes in detergent or cleaning compositions allows for more concentrated formulations of surfactants (such as by processes that concentrate liquid detergents by removing water) without inducing undesirable phenomena such as phase separation or high viscosity.

[0087] The detergent compositions of the present invention may contain 0 to 10% by weight of a hydrotrope, for example, 0 to 5% by weight, 0.5 to 5% by weight, or 3 to 5% by weight. Any hydrotrope known in the art for use in detergents may 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 polyglycol ethers, sodium hydroxynaphthoate, sodium hydroxynaphthalenesulfonate, sodium ethylhexyl sulfate, and combinations thereof.

[0088] Builders and co-builders The compositions of the present invention may also include one or more builders, co-builders, builder systems, or mixtures thereof. When builders are used, cleaning compositions will typically include 0-60 wt. %, at least 1 wt. %, 2-60 wt. %, or 5-10 wt. % of builder. In dishwashing cleaning compositions, builder levels are typically, for example, 5-45 wt. % or 10-35 wt. The compositions may be substantially free of builders; by substantially free, it is meant that zeolite and / or phosphate are "not intentionally added." Typical zeolite builders include zeolite A, zeolite P, and zeolite MAP. Typical phosphate builders include sodium tripolyphosphate.

[0089] The builder and / or co-builder may be, in particular, a chelating agent that forms a water-soluble complex with Ca and Mg. Any builder and / or co-builder known in the art for use in detergents may be utilized. Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 manufactured by Hoechst), ethanolamines such as 2-aminoethan-1-ol (MEA), iminodiethanol (DEA), and 2,2',2"-nitrilotriethanol (TEA), and carboxymethyl inulin (CMI), and combinations thereof.

[0090] The composition may contain a co-builder alone or in combination with a builder, such as a zeolite builder. Non-limiting examples of co-builders include polyacrylate homopolymers or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid / maleic acid) (PAA / PMA). Further non-limiting examples include citrates, chelating agents such as aminocarboxylates, aminopolycarboxylates, and phosphonates, and alkyl or alkenyl succinic acids.As additional specific examples, 2,2’,2’’-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodiacetic acid (IDS), ethylenediamine-N,N’-disuccinic acid (EDDS), methylglycinediacetic acid (MGDA), glutamic acid-N,N-diacetic acid (GLDA), 1-hydroxyethane-1,1-diylbis(phosphonic acid) (HEDP), ethylenediaminetetrakis(methylene)tetrakis(phosphonic acid) (EDTMPA), diethylenetriaminepentakis(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), iminodiacetic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfethyl)aspartic acid (SEAS), N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfethyl)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)-ethylenediaminetriacetate (HEDTA), diethanolglycine (DEG), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP), aminotris(methylenephosphonic acid) (ATMP), and combinations and salts thereof may be mentioned. Further exemplary builders and / or cobuilders are described, for example, in WO 09 / 102854 pamphlet, US Patent No. 5977053 specification.

[0091] Chelating agent and crystal growth inhibitor The compositions of the present invention may also contain chelating agents and / or crystal growth inhibitors. Suitable molecules include chelating agents for copper, iron, and / or manganese, and mixtures thereof. Suitable molecules include DTPA (diethylenetriaminepentaacetic acid), HEDP (hydroxyethanediphosphonic acid), DTPMP (diethylenetriaminepenta(methylenephosphonic acid), 1,2-dihydroxybenzene-3,5-disulfonic acid disodium salt hydrate, ethylenediamine, diethylenetriamine, ethylenediaminedisuccinic acid (EDDS), N-hydroxyethylethylenediaminetriacetic acid (HEDTA), triethylenetetraaminehexaacetic acid (TTHA), N-hydroxyethyliminodiacetic acid (HEIDA), dihydroxyethylglycine (DHEG), ethylenediaminetetrapropionic acid (EDTP), carboxymethyl inulin, and 2-phosphonobutane 1,2,4-tricarboxylic acid (Bayhibit® AM), and derivatives thereof. Typically, the composition may contain 0.005 to 15% by weight or 3.0 to 10% by weight of a chelating agent or crystal growth inhibitor.

[0092] bleaching ingredients The compositions of the present invention may also include a bleaching component. Bleaching components suitable for incorporation into the compositions of the present invention or use in the methods of the present invention include one bleaching component or a mixture of two or more bleaching components. Suitable bleaching components include bleach catalysts, photobleaches, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, and mixtures thereof. Generally, when a bleaching component is used, the compositions of the present invention may include 0-30 wt.%, 0.00001-90 wt.%, 0.0001-50 wt.%, 0.001-25 wt.%, or 1-20 wt.%. Examples of suitable bleaching components include: (1) Preformed Peracids: Suitable preformed peracids include, but are not limited to, preformed peroxyacids or salts thereof, typically compounds selected from the group consisting of either peroxycarboxylic acids or salts thereof, or peroxysulfonic acids or salts thereof. Preferably, such bleaching components may be present in the compositions of the present invention in an amount of 0.01 to 50% by weight or 0.1 to 20% by weight. (2) Sources of hydrogen peroxide include inorganic perhydrate salts, such as alkali metal salts of perborates (usually monohydrate or tetrahydrate), percarbonates, persulfates, perphosphates, persilicates, and mixtures thereof, such as sodium salts. Preferably, such bleaching components may be present in the compositions of the present invention in an amount of 0.01 to 50% by weight or 0.1 to 20% by weight. (3) The term bleach activator, as used herein, refers to a compound that reacts with hydrogen peroxide to form a peracid via perhydrolysis. The peracid thus formed constitutes the activated bleach. Suitable bleach activators that may be used herein include those belonging to the classes of esters, amides, imides, or anhydrides. Suitable bleach activators include those having the formula R-(C=O)-L, where R is an optionally branched alkyl group having 6 to 14 carbon atoms or 8 to 12 carbon atoms if the bleach activator is hydrophobic, and less than 6 carbon atoms or less than 4 carbon atoms if the bleach activator is hydrophilic; and L is a leaving group. Examples of suitable leaving groups include benzoic acid and its derivatives, especially benzenesulfonate. Suitable bleach 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 bleach activators is disclosed in EP 624154, and a particularly preferred member of this family is acetyl triethyl citrate (ATC). Alternatively, the bleaching system may include a peroxyacid, for example, of the amide, imide, or sulfone type. The bleaching system may also include a peracid, such as 6-(phthalimido)peroxyhexanoic acid (PAP). Suitable bleach activators are also disclosed in WO 98 / 17767. While any suitable bleach activator may be used, in one aspect of the present invention, the subject cleaning composition may include NOBS, TAED, or a mixture thereof.When present, the peracid and / or bleach activator is generally present in the composition in an amount of 0.1 to 60%, 0.5 to 40%, or 0.6 to 10% by weight, based on the cleaning composition. (4) Diacyl Peroxide (DAP)—Preferred diacyl peroxide bleaching species include those having the general formula: 1 -C(O)-OO-(O)CR 2 wherein R 1 is C6~C 18 Alkyl, preferably containing a linear chain of at least 5 carbon atoms, and optionally containing one or more substituents (e.g., -N + C6-C alkyl groups containing one or more interrupting moieties (e.g., -CONH- or -CH=CH-) inserted between adjacent carbon atoms of the alkyl radical (e.g., -(CH3)3, -COOH, or -CN) and / or alkyl radicals 12 represents an alkyl group, and R 2 represents an aliphatic group compatible with the peroxide moiety, whereby R 1 and R 2 together contain a total of 8 to 30 carbon atoms. 1 and R 2 is a linear unsubstituted C6-C 12 In one embodiment, the DAP may be asymmetric, such that the hydrolysis of the R1 acyl group is rapid, producing a peracid, while the hydrolysis of the R2 acyl group is slow.

[0093] The tetraacyl peroxide bleaching species preferably has the general formula: R 3 -C(O)-OO-C(O)-(CH2)nC(O)-OO-C(O)-R 3 wherein R 3 represents a C1 to C9 alkyl or a C3 to C7 group, and n represents an integer of 2 to 12 or 4 to 10 (inclusive).

[0094] Preferably, the diacyl and / or tetraacyl peroxide bleaching species is present in an amount sufficient to achieve at least 0.5 ppm, at least 10 ppm, or at least 50 ppm by weight of the wash liquor. In preferred embodiments, the bleaching species is present in an amount sufficient to achieve 0.5 to 300 ppm, 30 to 150 ppm by weight of the wash liquor.

[0095] Preferably, the bleaching component comprises a bleach catalyst. When present, the peracid and / or bleach activator is generally present in the composition in an amount of 0.1 to 60%, 0.5 to 40%, or 0.6 to 10% by weight based on the composition. One or more hydrophobic peracids or precursors thereof may be used in combination with one or more hydrophilic peracids or precursors thereof.

[0096] Exemplary bleaching systems are also described, for example, in WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259, and WO 2007 / 087242.

[0097] Antifoaming agents The cleaning composition may include an antifoaming agent to reduce foam stability and foam generation. If the composition includes an antifoaming agent, the antifoaming agent may be provided in an amount of from about 0.01% to about 3% by weight.

[0098] Examples of antifoaming agents that can be used in the composition include ethylene oxide / propylene oxide block copolymers, such as those available under the name Pluronic® N3, silicone compounds, such as silica dispersed in polydimethylsiloxane, polydimethylsiloxane, and functionalized polydimethylsiloxanes, such as those available under the name Abil B9952, fatty amides, hydrocarbon waxes, fatty acids, fatty esters, fatty alcohols, fatty acid soaps, ethoxylates, mineral oils, polyethylene glycol esters, alkyl phosphate esters, such as monostearyl phosphate, and the like.

[0099] Lipase The compositions of the present invention also include a lipase in addition to the surfactant or surfactant system and solvent. The lipase can be any lipase. In one embodiment, the lipase is of microbial origin. In one embodiment, the lipase is of bacterial origin. In a preferred embodiment, the lipase is of fungal origin, for example, from a filamentous fungus or yeast.

[0100] Examples of lipases include lipases from the genus Thermomyces, for example from T. lanuginosus (formerly Humicola lanuginosa), described in EP 258068 and EP 305216; cutinases from the genus Humicola, for example from H. insolens (WO 96 / 13580); and Absidia reflexa, disclosed in U.S. Patent Application Publication No. 2009 / 0221033. Lipases from P. reflexa (SEQ ID NO: 3), strains of the genus Pseudomonas (some of which have now been renamed to the genus Burkholderia), such as P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 331376), Pseudomonas sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (P.Lipases derived from Streptomyces sp. (WO 96 / 12012), GDSL-type Streptomyces lipases (WO 10 / 065455), Magnaporthe grisea cutinase (WO 10 / 107560), Pseudomonas mendocina cutinase (U.S. Pat. No. 5,389,536), Thermobifida fusca lipase (WO 11 / 084412, WO 13 / 033318), Geobacillus stearothermophilus lipase (GDSL-type Streptomyces lipases) Examples of lipases that can be used include lipases from Bacillus stearothermophilus (WO 11 / 084417), lipases from Bacillus subtilis (WO 11 / 084599), and lipases from Streptomyces griseus (WO 11 / 150157) and S. pristinaespiralis (WO 12 / 137147).

[0101] Other examples include 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, WO 97 / 07202, WO 00 / 34450, WO 00 / 60063, WO 01 / 92502, WO 07 / 87508 and WO 09 / 109500.

[0102] Further examples include lipases, sometimes referred to as acyltransferases or perhydrolases, such as acyltransferases with homology 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 M. smegmatis perhydrolase, in particular the S54V variant used in the product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 10 / 100028).

[0103] Preferred commercially available lipase products include Lipolase™, Lipex™; Lipolex™, Lipoclean™, Lipex Evity 100L, Lipex Evity 105T, Lipex Evity 200L (Novozymes A / S), Lumafast (originally manufactured by Genencor), Preferenz L100 (Danisco US Inc.), and Lipomax (originally manufactured by Gist-Brocades).

[0104] When present in a cleaning composition, the lipase of the present invention may be present at a level of at least 0.0001 mg enzyme protein, at least 0.001 mg enzyme protein, at least 0.006 mg enzyme protein, at least 0.008 mg enzyme protein, at least 0.01 mg enzyme protein, at least 0.1 mg enzyme protein, at least 0.5 mg enzyme protein, at least 1 mg enzyme protein, at least 2 mg enzyme protein, at least 5 mg enzyme protein, at least 10 mg enzyme protein, or at least 20 mg enzyme protein per gram of composition.

[0105] Lipase of SEQ ID NO: 1 - Thermomyces lanuginosus lipase (TLL) In a preferred embodiment, the enzyme product of the invention or the cleaning composition of the invention comprises a lipase derived from a strain of the genus Thermomyces, in particular a strain of Thermomyces lanuginosus (synonym Humicola lanuginosa), or a variant thereof. In a specific embodiment, the lipase is that set forth in SEQ ID NO: 1 or a variant thereof.

[0106] In one embodiment, the lipase is: 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 1; ii) a variant of a parent lipase 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 to the lipase set forth in SEQ ID NO: 1; iii) A fragment of the lipase of (i) or (ii) having lipase activity. and The variant includes substitutions at positions corresponding to T231R+N233R and at least one or more (e.g., some) of D96E, D111A, D254S, G163K, P256T, G91T, and G38A of SEQ ID NO:1.

[0107] In a specific embodiment, the lipase used in the composition of the invention is a variant of a parent lipase, which variant has lipase activity and has at least 60%, in particular 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% and less than 100% sequence identity with SEQ ID NO: 1, and D96E+T231R+N233R; N33Q+D96E+T231R+N233R; N33Q+D111A+T231R+N233R; N33Q+T231R+N233R+P256T; N33Q+G38A+G91T+G163K+T231R+N233R+D254S; N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; D27R+N33Q+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T; D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+N33Q+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+D96E+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G38A+D96E+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D111A+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+D96E+D111A+G163K+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">D27R+D96E+D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+N33Q+G38A+D96E+D111A+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+G38A+D96E+D111A+G163K+E210Q+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D27R+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+G163K+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+G163K+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+D111A+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> D96E+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> G38A+D96E+D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> G91T+D96E+D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> G91T+D96E+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> G91T+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> N33Q+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr"> T231R+N233R+P256T<h2 style=";text-align:left;direction:ltr"> It contains a substitution selected from the group consisting of:

[0108] In another embodiment, the lipase is a variant of a parent lipase, said variant comprising: (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; (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%, and less than 100% sequence identity to SEQ ID NO:1; (c) has lipase activity;

[0109] In one embodiment, the lipase is a variant of a parent lipase, wherein the parent lipase is: 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 1; b) a fragment of the polypeptide of SEQ ID NO: 1 is selected from the group consisting of:

[0110] In one embodiment, the lipase has lipase activity and is a variant 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% and less than 100% sequence identity to SEQ ID NO:1.

[0111] In one embodiment, the lipase variant comprises a modification in at least one of the 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, where the numbering is according to SEQ ID NO: 1. More preferably, the lipase variant comprises at least one of the 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, the numbering being according to SEQ ID NO: 1.

[0112] In one embodiment, the lipase variant further comprises one of the substitutions selected from the group: S54T, S83T, G91A, A150G, I255A, and E239C.

[0113] In a preferred embodiment, the lipase variant comprises a substitution corresponding to E1C+N233C in SEQ ID NO: 1, and optionally one or more additional substitutions.

[0114] In specific 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% and 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 using SEQ ID NO: 1 for numbering:

[0115] [Table 2]

[0116] [Table 3]

[0117] [Table 4]

[0118] Lipase of SEQ ID NO: 2 In a preferred embodiment, the cleaning composition of the present invention comprises a lipase as set forth in SEQ ID NO: 2 or a variant thereof.

[0119] In one embodiment, the lipase is: 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:2; ii) A variant of a parent lipase having lipase activity that 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% sequence identity to the lipase set forth as SEQ ID NO:2, but less than 100% sequence identity; iii) A fragment of the lipase of (i) or (ii) having lipase activity and Such variants include those of the polypeptide shown as SEQ ID NO:2: (a) Substitutions corresponding to: D1E,Q;A4R;D5Q;L7Y;N8D,E,Q;K11E,Q;R24E,N,Q;N26Q;D27N,Q;A30N;N33Q;T35N;N39D,Q;A46Q;D48Q;F51I,V;L52N,E5 6N;N57Q;G59S;V60S,M,D62Q;D70Q;N71Q;N73S;I86F,P;N88D,Q;I90R;L93F;N94Q,R,S;D96H,I,Q,S;V98I;N101D,Q,R;S 105R;R108E,Q;D111Q;D122Q;D130Q;D158Q;N162D,E;Y164S;D165Q;D167Q;A173Q;N178D;A180E;N200Q;R209Q;Q210E;F 211A,N,S,T,Y;G212D,E,R;L227G,V228E,P;R231Q;R232E,Q;R233K,N,Q;T244E;N250D;I255A;A257S;L264A,V,I; (b) Substitutions corresponding to: A4E+F211V;A4E+L227G;A4E+T252A;D122N+L124S;D165N+D167S;D96N+V98S;E45N+A47S;E87K+F9 5Y;E87R+N94D;F211V+L227G;F211V+L264A;F211V+T252A;I238C+G246C;L227A+L264A;L227G+I2 69W;L264A+I269W;N250P+T252I;S105D+R108G;T123N+R125S;T252A+I269W;T252A+L264A;T252A+L264I;T252A+L264P;T252A+L264Q;T252A+L264S;T252A+L264T;T72N+K74S;V60M+L227G; and / or (c) Substitutions corresponding to: <h2 style=";text-align:left;direction:ltr">A40N+T252A+L264A;A46N+T252A+L264A;A46N+T252A+L264A;A46R+T252A+ L264A;D130H+N250P+T252I;D1A+T252A+L264A;D1C+T252A+L264A;D1F+T2 52A+L264A;D1G+T252A+L264A;D1H+T252A+L264A;D1L+T252A+L264A;D1M+ T252A+L264A;D1G+T252A+L264A;D1R+T252A+L264A;D1W+T252A+L264A;D1Y +T252A+L264A;D5R+T252A+L264A;D62R+T252A+L264A;F10L+T252A+L264A F10M+T252A+L264A;F211V+L264A+I269W;F211V+T252A+L264A;F51G+T252 A+L264A;F51K+T252A+L264A;G106E+N250P+T252I;G65A+T252A+L264A;G6 5W+T252A+L264A;H198I+T252A+L264A;H198N+P256T+A257I;K74G+T252A+L 264A;L12H+N250P+T252I;L227G+T252A+L264A;L75A+T252A+L264A;L75K+ T252A+L264A;L75Y+T252A+L264A;L7F+T252A+L264A;N250P+T252I+I255D ;N39S+T252A+L264A;N8K+T252A+L264A;N8R+T252A+L264A;N94D+T252A+L 264A;Q15M+T252A+L264A;R108Q+R179E+G212E;R232N+T252A+L264A;S37H+ N250P+T252I;S3R+T252A+L264A;T50H+T252A+L264A;T50L+T252A+L264A;T50M+T252A+L264A;T50W+T252A+L264A;T50Y+T252A+L264A;V228R+T252A+ L264A;V63C+T252A+L264A;V63E+T252A+L264A;V63G+T252A+L264A;V63I+ T252A+L264A;V63L+T252A+L264A;V63Q+T252A+L264A;V63S+T252A+L264A;A19T+T252A+L264A;A19S+T252A+L264A;K11L+T252A+L264A;A20V+T252A+L264A;A20T+T252A+L264A;S17C+T252A+L264A;I34S+T252A+L264A;T32P+T252A+L264A;N26A+T252A+L264A;N26W+T252A+L264A;N26K+T252A+L264A;S37V+T252A+L264A;S37Y+T252A+L264A;S37E+T252A+L264A;D27E+T252A+L264A;A38S+T252A+L264A;T72I+T252A+L264A;T72V+T252A+L264A;V60T+T252A+L264A;L43G+T252A+L264A;N33V+T252A+L264A;N33F+T252A+L264A;N33D+T252A+L264A;P42S+T252A+L264A;A47G+T252A+L264A;A47R+T252A+L264A;G31V+T252A+L264A;A46F+T252A+L264A;A46F+T252A+L264A;A46G+T252A+L264A;A40H+T252A+L264A;A46K+T252A+L264A;D62G+T252A+L264A;D62A+T252A+L264A;F66K+T252A+L264A;A49V+T252A+L264A;T50A+T252A+L264A;F51H+T252A+L264A;A49G+T252A+L264A;V63M+T252A+L264A;F51L+T252A+L264A;T50N+T252A+L264A;V63T+T252A+L264A;F51P+T252A+L264A;A49S+T252A+L264A;A49Q+T252A+L264A;V63A+T252A+L264A;S54R+T252A+L264A;F51Y+T252A+L264A;S54D+T252A+L264A;T64S+T252A+L264A;S54C+T252A+L264A;F66N+T252A+L264A;L52W+T252A+L264A;L52T+T252A+L264A;A68V+T252A+L264A;N57S+T252A+L264A;L67Y+T252A+L264A;V69Q+T252A+L264A;S58Y+T252A+L264A;N71C+T252A+L264A;D70R+T252A+L264A;V60M+T252A+L264A;N7 1G+T252A+L264A;V69E+T252A+L264A;V69K+T252A+L264A;N71D+T252A+L264A;N71T+T252A+L264A;V60A+ T252A+L264A;V60W+T252A+L264A;G61A+T252A+L264A;V60G+T252A+L264A;T72G+T252A+L264A;V60L+T25 2A+L264A;A4R+R233N+T252A;A4R+R233N+L264A;R233N+T252A+L264A;A4R+V60M+L227G;A4R+L227G+R233 N;A4R+V60M+R233N;V60M+L227G+R233N;V60M+L227G+L264V;V60M+L227G+L264I;V60M+L227G+T252A;A4R +L227A+L264A;G23A+N250P+T252I;V60K+N250P+T252I;L97V+N250P+T252I;A150G+N250P+T252I;V202L+ N250P+T252I;V228P+N250P+T252I;L227G+N250P+T252I;F211G+N250P+T252;V142I+N250P+T252I;V60M+L227G+V228Q;A4L+T252A+L264A;T114E+T252A+L264A;G156A+T252A+L264A;L168E+T252A+L264A;and / or; (d) Substitutions corresponding to: A4K+R231T+T252A+L264A;A4K+R232V+T252A+L264A;L227G+V228A+T252A+L264I;L7F+L227G+T252A+L264A;N250P+T252I+D254N+P256S ;Q249N+N250P+N251S+T252I;T244N+G246S+N250P+T252I;T91A+N92D+D96L+V98Q;T91A+V228L+T252A+L264S;V202C+N250P+T252I+P253 C;V60M+T91A+T252A+L264A;W221C+G246C+N250P+T252I;D1C+R233C+T252A+L264A;V60M+D99N+N101S+L227G;V60M+S119N+A121S+L227G;V60M+R125N+A127S+L227G;D1G+T252A+P256T+L264A;V60M+L227G+V228R+L264T;N39D+V60M+L227G+P256T;N73G+T252A+L264A;and / or (e) Substitutions corresponding to: T91A+H198N+D254S+P256T+A257I; T91A+T252A+I255L+P256K+L264A; V60M+L227G+V228L+T252A+L264Y; V60M+L227V+V228P+T252A+L264I; V60M+T91A+L227R+T252A+L264V; N33Q+V60M+G163N+D165S+L227G; R24E+A180E+N250D+T252A+L264A; and / or V60M+T91A+L227V+T252A+L264M; and / or (f) Substitutions corresponding to: L7F+T91A+A150G+L154V+T252A+L264A; and / or (g) Substitutions corresponding to: D1C+V202C+R233C+I238C+G245C+T252A+P253C+L264A; and / or A4R+I90V+N94E+D96L+N101P+R233N+T252A+L264A Includes.

[0120] In one embodiment, the lipase variant further comprises in SEQ ID NO:2: A4E;A20T;P29S;A46Q;S58N;T91A;N92D;L93F,I;S105D,E,N;R179G,Q;N200R ;Y220F;L227G;R231K;T244E;Q249E;T252A,S,V;N25S;A38T;R84S;N94D;V98Q ;N101K;D130H;D137G;R232K;T244A,N,K;A249G,R;N250P;T252I;D254S;P256 T;A257I;L264A;N94V;F95V;L97S;N101E;S105K;D129G;A134S;V187I;Q188H; R209Q; Q210D; G212S; D234R; G240D; N248D,E; Q249D,G; L264V; T267A; I269F; A28V; V60E,I,M; V63I; E87Q; N92D; V98Q; S105G; R179K; V228L; N248K; Q249D; I255G; L264P,Y; A4Q; L7F; A46K; Y53F; V60K; E87K; Y138F; A157V; Y194F; H198I; Y213F; L227V,V228A; and / or I255L, or containing one or more substitutions using SEQ ID NO: 2 for numbering.

[0121] In one embodiment, the lipase variant is in SEQ ID NO: 2: A20T+L93F;A4E+A46Q;F51I+T244E;L227G+R233N;L227G+T244E;L227G+T252A;L93I +V98I;N101D+S105D;Q210E+Q249E;R179Q+G212E;R231K+R233K;R233N+T252A;S105 D+G212E; S105E+R108Q; S105N+G212D; S105N+G212E; S58N+V60S; T244E+T252A; T252A+I255A; T252S+I255A; and / or T91A+V98I, or containing two substitutions using SEQ ID NO: 2 for numbering.

[0122] In one embodiment, the lipase is A4R+R233N; K223Q+R232Q; Q210E+N250D; R108Q+G212E; R24Q+N250D; and / or R24Q+Q210E; or including substitutions using SEQ ID NO: 2 for numbering.

[0123] In one embodiment, the lipase variant is in SEQ ID NO: 2: A38T+D96H+D137G;A4R+T252A+L264A;D1G+T252A+L264A;D62N+T252A+L264A;D165Q+N250P+T2 52I;H198S+Y220F+L264A;N101K+S105N+R108E;N94Q+N250P+T252I;Q210E+T244E+Q249G;Q210E +T252A+L264A; R231K+R232K+R233K; S83T+H198S+D254S; R233N+T252A+L264A; A46Q+T252A+L264A; N39D+T252A+L264A; a+L227G; or F51I+T252A+L264A, or containing substitutions using SEQ ID NO: 2 for numbering.

[0124] In one embodiment, the lipase variant is in SEQ ID NO: 2: A4R+R233N+T252A+L264A;A4R+V60M+L227G+R231T;A4R+V60M+L227G+R232V;A4R+V60M+L227G+R233N;E8 7Q+T91A+D96I+V98Q;G109R+Q210E+T244N+Q249E;L227G+R233N+T252A+L264A;L7F+Q210E+T252A+L264A ;Q188H+Q210E+T252A+L264A;Q210E+L227G+T252A+L264A;Q210N+G212S+N250P+T252I;V60S+L227G+T252A+L264A;R24E+N33Q+V60M+L227G;or R24E+V228P+T252A+L264A or containing substitutions using SEQ ID NO: 2 for numbering.

[0125] In one embodiment, the lipase variant is in SEQ ID NO:2: L227G+R233N+T244E+T252A+L264A; S105N+R108Q+D129G+D137G+G212D;; L7F+R24E+N39D+T252A+L264A; and / or R24E+V128A+V228E+T252A+L264A; or A20T+G163N+D165S+T252A+L264A, or including substitutions using SEQ ID NO: 2 for numbering.

[0126] In one embodiment, the lipase variant is in SEQ ID NO:2: L7F+N8K+Q210E+L227G+T252A+L264A; N8D+101K+S105G+R108Q+R179E+G212E; N8D+R209Q+Q210E+T244N+N248K+Q249E; V60E+S83T+T91A+H198S+T252A+L264P; or V60M+T91A+Q210E+V228L+T252A+L264Y, or containing substitutions using SEQ ID NO: 2 for numbering.

[0127] In one embodiment, the lipase variant is in SEQ ID NO:2: V60K+S83T+T91A+H198I+V228L+T252A+L264P; or V60M+A157V+Q210E+L227V+V228A+T252A+L264V, or containing substitutions using SEQ ID NO: 2 for numbering.

[0128] In one embodiment, the lipase variant is: Contains substitutions corresponding to D1E+A4Q+L7F+K11N+S37T+A46K+A133R+V142F+T170S+V202I+Q210E+L227G.

[0129] In certain preferred embodiments, the lipase has one of the following sets of substitutions corresponding to the following (using SEQ ID NO:2 for numbering):

[0130] [Table 5]

[0131] [Table 6]

[0132] [Table 7]

[0133] [Table 8]

[0134] [Table 9]

[0135] [Table 10]

[0136] Other lipases Other lipases contemplated according to the present invention are described 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 , those disclosed in WO 2019 / 201636, WO 2019 / 206994, WO 2019 / 215078, WO 2019 / 219903, WO 2019 / 243312, and Absidia sp. lipases and variants thereof disclosed in WO 2021 / 001400 (all incorporated herein by reference).

[0137] Suitable lipases can include lipases derived from Geotrichum candidum (also referred to as GCL I). Exemplary GCL I can be selected from SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, or SEQ ID NO:7.

[0138] In one embodiment, GCL I comprises the amino acid sequence of SEQ ID NO: 3 or an amino acid sequence having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, 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%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1. In one aspect, the polypeptide differs from the polypeptide comprising SEQ ID NO: 3 by up to 10, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 amino acids.

[0139] In another embodiment, GCL I of SEQ ID NO: 3 contains substitutions, deletions, and / or insertions at one or more (e.g., several) positions. The amino acid changes can be minor, i.e., conservative amino acid substitutions or insertions that do not significantly affect protein folding and / or activity; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions such as an amino-terminal methionine residue; small linker peptides of up to 20-25 residues; or small extensions that facilitate purification by altering net charge or another function, e.g., a polyhistidine tract, an antigenic epitope, or a binding domain.

[0140] Additional enzymes In addition to the lipase enzyme, the compositions of the present invention may contain one or more additional enzymes to provide cleaning performance. Examples of suitable enzymes include, but are not limited to, protease, cellulase, amylase, pectinase, mannanase, pectate lyase, phosphodiesterase (PDE), deoxyribonuclease (DNase), hexosaminidase, hemicellulose, or mixtures thereof. A typical combination is an enzyme cocktail, which may include, for example, protease and lipase together with alpha-amylase, phospholipase, cutinase, pectinase, mannanase, pectate lyase, phosphodiesterase (PDE), deoxyribonuclease (DNase), xanthanase, dispersin, or mixtures thereof.

[0141] When present in a cleaning composition, the aforementioned additional enzymes may be present at a level of at least 0.0001 mg enzyme protein, at least 0.001 mg enzyme protein, at least 0.006 mg enzyme protein, at least 0.008 mg enzyme protein, at least 0.01 mg enzyme protein, at least 0.1 mg enzyme protein, at least 0.5 mg enzyme protein, at least 1 mg enzyme protein, at least 2 mg enzyme protein, at least 5 mg enzyme protein, at least 10 mg enzyme protein, or at least 20 mg enzyme protein per gram of composition.

[0142] In general, the properties of the enzyme selected should be compatible with the detergent or cleaning composition selected (i.e., pH optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme should be present in an effective amount.

[0143] Proteases: In one aspect, suitable proteases may be of any origin, preferably bacterial or fungal, and optionally in the form of engineered or chemically modified variants. The protease may be an alkaline protease, such as a serine protease or a metalloprotease. The serine protease may be, for example, from the S1 family, such as trypsin, or the S8 family, such as subtilisin. The metalloprotease may be, for example, thermolysin, for example from the M4 family, or another metalloprotease, for example from the M5, M7, or M8 family.

[0144] The term "subtilase" refers to a subgroup of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 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 six subdivisions: the subtilisin family, thermitase family, proteinase K family, lantibiotic peptidase family, kexin family, and pyrrolysin family.

[0145] Although proteases suitable for detergent use can be obtained from a variety of organisms, including fungi such as Aspergillus, detergent proteases are generally obtained from bacteria, particularly Bacillus. Examples of Bacillus species from which subtilases are derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus, and Bacillus gibsonii. Specific subtilisins include subtilisin lentus, subtilisin novo, subtilisin Carlsberg, subtilisin BPN', subtilisin 309, subtilisin 147, and subtilisin 168, as well as, for example, protease PD138 (described in WO 93 / 18140). Other useful proteases include, for example, those described in WO 01 / 16285 and WO 02 / 16547.

[0146] Examples of trypsin-like proteases include the Fusarium proteases described in WO 94 / 25583 and WO 2005 / 040372, and the chymotrypsin proteases from Cellulomonas, described in WO 2005 / 052161 and WO 2005 / 052146.

[0147] Examples of metalloproteases include the neutral metalloproteases described in WO 2007 / 044993, such as those derived from Bacillus amyloliquefaciens, and the metalloproteases described in WO 2015 / 158723 and WO 2016 / 075078, for example.

[0148] Examples of useful proteases include those described in WO 89 / 06279, WO 92 / 19729, WO 96 / 34946, WO 98 / 20115, WO 98 / 20116, WO 99 / 11768, WO 01 / 44452, WO 03 / 006602, WO 04 / 006603, WO 05 / 006604, WO 06 / 006606, WO 07 / 006608, WO 08 / 006609, WO 09 / 006610, WO 10 / 006611, WO 11 / 006612, WO 12 / 006613, WO 13 / 006614, WO 14 / 006615, WO 15 / 006616, WO 16 / 006617, WO 17 / 006618, WO 18 / 006619, WO 19 ... and protease variants described in WO 2004 / 003186, WO 2004 / 041979, WO 2007 / 006305, WO 2011 / 036263, WO 2014 / 207227, WO 2016 / 087617, and WO 2016 / 174234. Preferred protease variants are, for example: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, A120S, S1 26L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V199I, Q200L, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, S253D, N255W, N255D, N255E, L256E, L256D The protease may comprise one or more mutations selected from the group consisting of T268A, T268B, and R269H, where the position numbers correspond to the positions in Bacillus lentus protease shown in SEQ ID NO: 1 of WO 2016 / 001449.Protease variants having one or more of these mutations are preferably variants of the Bacillus lentus protease (Savinase®, also known as subtilisin 309) set forth in SEQ ID NO: 1 of WO 2016 / 001449, or variants of the Bacillus amyloliquefaciens protease (BPN') set forth in SEQ ID NO: 2 of WO 2016 / 001449. Such protease variants preferably have at least 80% sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016 / 001449.

[0149] Another protease of interest is the alkaline protease from Bacillus lentus DSM 5483, described, for example, in WO 91 / 02792, and variants thereof, described, for example, in WO 92 / 21760, WO 95 / 23221, EP 1921147, EP 1921148, and WO 2016 / 096711.

[0150] Alternatively, the protease may be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004 / 067737, for example a variant comprising substitutions at one or more positions corresponding to positions 27, 109, 111, 171, 173, 174, 175, 180, 182, 184, 198, 199, and 297 of SEQ ID NO: 1 of WO 2004 / 067737, wherein the protease variant has at least 75% but less than 100% sequence identity to SEQ ID NO: 1 of WO 2004 / 067737. TY145 variants of interest are described, for example, in WO 2015 / 014790, WO 2015 / 014803, WO 2015 / 014804, WO 2016 / 097350, WO 2016 / 097352, WO 2016 / 097357, and WO 2016 / 097354.

[0151] Suitable commercially available protease enzymes include Alcalase®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase™, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In, and Progress® Excel (Novozymes). A / S), Maxatase™, Maxacal™, Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2™, FN3™, FN4 ex(trademark), Excellase®, Excellenz® P1000, Excellenz® P1250, Eraser®, Preferenz® P100, Preferenz® P300, Purafect Prime, Preferenz P110®, Effectenz P1000®, Purafect®, Effectenz P1050®, Purafect® Ox, Effectenz® P2000, Purafast®, Properase®, Opticlean®, and Optimase® (Danisco / DuPont), BLAP (sequence shown in Figure 29 of U.S. Pat. No. 5,352,604) and its variants (Henkel AG), and KAP (Bacillus alkalophilus) from Kao Corporation. Examples of suitable subtilisin include those sold under the trade name (B. alkalophilus subtilisin).

[0152] Amylases: In one embodiment, suitable amylases may be alpha-amylases or glucoamylases and may be of bacterial or fungal origin, including chemically modified or engineered variants. Amylases include, for example, alpha-amylases obtained from specialized strains of the Bacillus genus, such as Bacillus licheniformis, as described in more detail in GB 1,296,839.

[0153] Suitable amylases include amylases having SEQ ID NO: 2 in WO 95 / 10603 or variants thereof having 90% sequence identity to SEQ ID NO: 3. Preferred variants are set out 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.

[0154] A suitable different amylase is the amylase having SEQ ID NO: 6 in WO 02 / 010355, or a variant thereof having 90% sequence identity to SEQ ID NO: 6. A preferred variant of SEQ ID NO: 6 is one having deletions at positions 181 and 182 and a substitution at position 193.

[0155] Other suitable amylases include hybrid alpha-amylases comprising residues 1-33 of the alpha-amylase from B. amyloliquefaciens as set forth in SEQ ID NO:6 of WO 2006 / 066594 and residues 36-483 of the B. licheniformis alpha-amylase as set forth in SEQ ID NO:4 of WO 2006 / 066594, or variants thereof with 90% sequence identity. Preferred variants of this hybrid alpha-amylase include those with 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 variant of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of SEQ ID NO: 4 comprises the substitution: M197T; H156Y+A181T+N190F+A209V+Q264S; or G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S It has the following characteristics.

[0156] A further suitable amylase is the amylase having SEQ ID NO: 6 in WO 99 / 019467, or a variant thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 include those having substitutions, deletions, or insertions at one or more of the following positions: R181, G182, H183, G184, N195, I206, E212, E216, and K269. Particularly preferred amylases are those having deletions at positions R181 and G182, or H183 and G184.

[0157] Additional amylases that can be used include those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2, or SEQ ID NO: 7 of WO 96 / 023873, or variants thereof having 90% sequence identity to 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 include those having substitutions, deletions, or insertions at one or more of the following positions, using SEQ ID NO: 2 of WO 96 / 023873 for numbering: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304, and 476. More preferred variants include those having deletions at two positions selected from 181, 182, 183, and 184, for example, positions 181 and 182, positions 182 and 183, or positions 183 and 184. The most preferred amylase variants of SEQ ID NO:1, SEQ ID NO:2, or SEQ ID NO:7 have deletions at positions 183 and 184 and substitutions at one or more of positions 140, 195, 206, 243, 260, 304, and 476.

[0158] Other amylases that can be used include amylases having SEQ ID NO: 2 in WO 08 / 153815, SEQ ID NO: 10 in WO 01 / 66712, or variants thereof having 90% sequence identity to SEQ ID NO: 2 in WO 08 / 153815 or 90% sequence identity to SEQ ID NO: 10 in WO 01 / 66712. Preferred variants of SEQ ID NO: 10 in WO 01 / 66712 are those that have substitutions, deletions, or insertions at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264.

[0159] Further suitable amylases include amylases 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 include those having C-terminal truncations and / or substitutions, deletions or insertions 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 include substitutions 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 deletions at positions R180 and / or S181 or T182 and / or G183. The most preferred amylase variants of SEQ ID NO: 2 include substitutions: N128C+K178L+T182G+Y305R+G475K; N128C+K178L+T182G+F202Y+Y305R+D319T+G475K; S125A+N128C+K178L+T182G+Y305R+G475K; or S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K wherein the variant is C-terminally truncated and optionally further comprises a substitution at position 243 and / or a deletion at positions 180 and / or 181.

[0160] Further suitable amylases are those having SEQ ID NO: 1 of WO 13184577 or variants thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 include those having substitutions, deletions or insertions at one or more of the following positions: K176, R178, G179, T180, G181, E187, N192, M199, 1203, S241, R458, T459, D460, G476, and G477. More preferred variants of SEQ ID NO: 1 include substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K, and / or deletions at positions R178 and / or S179 or T180 and / or G181. The most preferred amylase variants of SEQ ID NO: 1 include substitutions: E187P+I203Y+G476K E187P+I203Y+R458N+T459S+D460T+G476K and The variant optionally further comprises a substitution at position 241 and / or a deletion at positions 178 and / or 179.

[0161] Further suitable amylases include those having SEQ ID NO: 1 of WO 10104675, or variants thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 include those having substitutions, deletions, or insertions at one or more of the following positions: N21, D97, V128 K177, R179, S180, I181, G182, M200, L204, E242, G477, and G478. More preferred variants of SEQ ID NO: 1 include those having substitutions at one or more of the following positions: N21D, D97N, V128I K177L, M200L, L204YF, E242QA, G477K, and G478K, and / or deletions at positions R179 and / or S180 or I181 and / or G182. The most preferred amylase variant of SEQ ID NO: 1 has the substitution: N21D+D97N+V128I and The variant optionally further comprises a substitution at position 200 and / or a deletion at positions 180 and / or 181.

[0162] Other suitable amylases include the alpha-amylase having SEQ ID NO: 12 in WO 01 / 66712, or a variant having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants include those having substitutions, deletions or insertions at one or more of the following positions of 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 substitutions R118K, N195F, R320K, and R458K, as well as variants additionally having substitutions at one or more positions selected from the group: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345, and A339, with variants additionally having substitutions at all of these positions being most preferred.

[0163] Other examples include amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078, and WO 2013 / 001087.

[0164] Commercially available amylases include Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natalase™, Liquozyme X, and BAN™ (manufactured by Novozymes A / S), and Rapidase™, Purastar™ / Effectenz™, Powerase, Preferenz S1000, Preferenz S100, and Preferenz S110 (manufactured by Genencor International Inc. / DuPont).

[0165] Cellulases: In one aspect, suitable cellulases include single component and mixtures of enzymes of bacterial or fungal origin. Chemically modified or engineered variants are also contemplated. Cellulases can be single component or mixtures of single component endo-1,4-beta-glucanases, also known as endoglucanases, for example.

[0166] Suitable cellulases include those derived from the genera Bacillus, Pseudomonas, Humicola, Myceliophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include fungal cellulases derived from Humicola insolens (U.S. Pat. No. 4,435,307) or Trichoderma, such as T. reesei or T. viride. Other suitable cellulases include those derived from Thielavia, such as Thielavia terrestris, as described in WO 96 / 29397, or fungal cellulases produced by Myceliophthora thermophila and Fusarium oxysporum, as disclosed in U.S. Patent Nos. 5,648,263, 5,691,178, 5,776,757, WO 89 / 09259, and WO 91 / 17244. Also of interest are cellulases derived from the genus Bacillus, as described in WO 02 / 099091 and JP 2000210081 A1. Suitable cellulases include alkaline or neutral cellulases with care benefits. Examples of cellulases are described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397 and WO 98 / 08940.Other examples include cellulase variants such as those described in WO 94 / 07998, EP 0 531 315, U.S. Pat. No. 5,457,046, U.S. Pat. No. 5,686,593, U.S. Pat. No. 5,763,254, WO 95 / 24471, and WO 98 / 12307.

[0167] Other cellulases include endo-beta-1,4-glucanase enzymes having a sequence that is at least 97% identical to the amino acid sequence of positions 1 to 773 of SEQ ID NO:2 in WO 2002 / 099091, or family 44 xyloglucanases, which have a sequence that is at least 60% identical to positions 40 to 559 of SEQ ID NO:2 in WO 2001 / 062903.

[0168] Commercially available cellulases include Carezyme®, Carezyme® Premium, Celluzyme®, Celluclean®, Celluclast®, Endolase®, Renozyme®; Whitezyme®, Celluclean® Classic, Cellusoft® (Novozymes A / S), Puradax®, Puradax HA, and Puradax EG (available from Genencor International Inc.), and KAC-500(B)™ (Kao Corporation).

[0169] Mannanases: In one embodiment, suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified variants are also included. The mannanase may be an alkaline mannanase of family 5 or 26. It may be a wild-type mannanase derived from the genus Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens. Suitable mannanases are described in WO 1999 / 064619. Commercially available mannanases include Mannaway (Novozymes A / S) and Purabrite® (Danisco / DuPont).

[0170] Pectate lyase, DNase, and / or PDE: Other preferred enzymes that may additionally be included in the compositions of the present invention include pectate lyase, such as those sold under the trade names Pectawash®, Pectaway®, or Xpect®. Finally, the compositions may also include a deoxyribonuclease (DNase) and / or a phosphodiesterase (PDE).

[0171] In one embodiment, in addition to a lipase of the present invention, the cleaning composition further comprises an amylase, such as BAN™ (Novozymes A / S).

[0172] In one embodiment, in addition to the lipase of the present invention, the cleaning composition further comprises a protease, dispersin, and / or DNase.

[0173] In one embodiment, in addition to the lipase of the present invention, the cleaning composition further comprises a protease and a cellulase.

[0174] In one embodiment, in addition to the lipase of the present invention, the cleaning composition further comprises a protease, an amylase, and a cellulase.

[0175] polymer The cleaning composition may contain 0.005 to 10 wt. % of the polymer, e.g., 0.5 to 5 wt. %, 2 to 5 wt. %, 0.5 to 2 wt. %, or 0.2 to 1 wt. %. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as described above, or may provide anti-redeposition, fabric protection, soil release, dye transfer inhibition, grease cleaning, and / or defoaming properties. Some polymers may have two or more of the above properties. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(ethylene glycol) or poly(ethylene oxide) (PEG or PEO), ethoxylated poly(ethyleneimine), (carboxymethyl)inulin (CMI), carboxylate polymers and copolymers, as well as lauryl methacrylate / acrylic acid copolymers, hydrophobically modified CMC (HM-CMC), silicones, copolycarboxylates such as polyacrylates, maleic acid / acrylic acid copolymers, acrylic acid copolymers, and the like. Examples include acrylate / styrene copolymers, poly(aspartic)acipolymers of terephthalic acid and oligomeric glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethene terephthalate) (PET-POET), poly(vinylpyrrolidone) (PVP), poly(vinylimidazole) (PVI), poly(vinylpyridine-N-oxide) (PVPO or PVPNO), and copoly(vinylimidazole / vinylpyrrolidone) (PVPVI). Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S-403E, and ChromaBond S-100 manufactured by Ashland Aqualon, and Sokalan® HP 165, Sokalan® HP 50 (dispersant), Sokalan® HP 53 (dispersant), Sokalan® HP 59 (dispersant), Sokalan® HP 56 (stain transfer inhibitor), and Sokalan® HP 66 K (stain transfer inhibitor) manufactured by BASF.Further exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternium ethoxysulfate. A particularly preferred polymer is the ethoxylated homopolymer Sokalan® HP 20 manufactured by BASF, which helps prevent soil redeposition in the wash liquor. Further exemplary polymers include sulfonated polycarboxylates, ethylene oxide-propylene oxide copolymers (PEO-PPO), copolymers of PEG with vinyl acetate, and diquaternium ethoxysulfate or quaternized sulfated ethoxylated hexamethylenediamine. Other exemplary polymers are disclosed, for example, in WO 2006 / 130575. Salts of the above-mentioned polymers are also contemplated.

[0176] Auxiliary substances Any detergent auxiliary ingredient known in the art may also be utilized. Exemplary auxiliary substances may include, alone or in combination, anticorrosion agents, anti-shrinkage agents, anti-soil redeposition agents, anti-wrinkle agents, bactericides, binders, corrosion inhibitors, disintegrants, dyes, enzyme stabilizers (including boric acid, borates, CMC, and / or polyols such as propylene glycol), foam boosters, foam (suds) regulators, perfumes, soil suspending agents, softeners, suds suppressors, discoloration inhibitors, and wicking agents. The selection of such ingredients is well within the skill of those skilled in the art. The cleaning composition of the present invention may also include a corrosion inhibitor (or "rust inhibitor") to prevent rust or corrosion on hard surfaces after washing or cleaning.

[0177] Soil Release Polymer The cleaning compositions of the present invention may also contain one or more soil-release polymers to aid in the removal of soil from the surface to be cleaned. Soil-release polymers may be, for example, nonionic or anionic terephthalate-based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, or polyester polyamides; see, for example, Chapter 7 of Powdered Detergents, Surfactant Science Series, Volume 71, Marcel Dekker, Inc. Another type of soil-release polymer is an amphiphilic alkoxylated grease-cleaning polymer comprising a core structure and multiple alkoxylate groups attached to the core structure. The core structure may comprise a polyalkyleneimine structure or a polyalkanolamine structure, as described in detail in WO 2009 / 087523 (incorporated herein by reference). Additionally, random graft copolymers are suitable soil-release polymers. Suitable graft copolymers are described in more detail in WO 2007 / 138054, WO 2006 / 108856, and WO 2006 / 113314 (incorporated herein by reference). Other soil-release polymers are substituted polysaccharide structures, particularly substituted cellulosic structures, such as modified cellulose derivatives such as those described in EP 1867808 or WO 2003 / 040279 (both incorporated herein by reference). Suitable cellulosic polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides, and mixtures thereof. Suitable cellulosic polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methyl cellulose, carboxymethyl cellulose, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, ester carboxymethyl cellulose, and mixtures thereof.

[0178] Probiotics The composition may include a probiotic (e.g., a probiotic spore), such as those described in WO 09 / 043709. Commercially available probiotics include Microvia® and Deep Clean Multi 5X (available from Novozymes A / S).

[0179] Cleaning composition product formulation The hard surface cleaning compositions of the present invention may be formulated in any convenient form, for example, a liquid, gel, paste, bar, powder, tablet, pouch having one or more compartments, single or multi-compartment unit dose form, or spray form.

[0180] The pouches can be configured as single or multiple compartments. They can be of any form, shape, and material suitable for holding the composition, e.g., preventing release of the composition from the pouch prior to contact with water. The pouch is made of a water-soluble film that encompasses the internal volume. The internal volume can be divided into compartments of the pouch. Preferred films are polymeric materials, preferably polymers that can be formed into films or sheets. Preferred polymers, copolymers, or derivatives thereof are selected polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers and hydroxypropylmethylcellulose (HPMC). Preferably, the level of polymer, e.g., PVA, in the film is at least about 60%. Preferred average molecular weights are typically from about 20,000 to about 150,000. The film can also be of a blended composition including a hydrolytically degradable, water-soluble polymer blend, such as polylactide and polyvinyl alcohol (known under the trade name M8630 sold by MonoSol LLC, Indiana, USA), and a plasticizer such as glycerol, ethylene glycerol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain solid cleaning compositions or components and / or liquid cleaning compositions or components separated by a water-soluble film.

[0181] The detergent or cleaning ingredients may be physically separated from one another by compartments within a water-soluble pouch or within different layers of a tablet, thereby avoiding undesirable storage interactions between the ingredients.

[0182] Non-unit-dosed liquid or gel detergents may be aqueous, typically containing at least 20% and up to 95% water by weight, e.g., up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, or up to about 35% water. Other types of liquids, such as, but not limited to, alkanols, amines, diols, ethers, and polyols, may be included in the aqueous liquid or gel. Aqueous liquid or gel detergents may contain 0-30% organic solvents. Liquid or gel detergents may also be non-aqueous.

[0183] The compositions of the present invention may be formulated as hand dish detergents, professional cleaning detergents, clean-in-place (CIP) detergents, or hard surface cleansers.

[0184] When formulated as a liquid or spray type, or paste form, the cleaning composition of the present invention preferably has a pH of less than 11, for example in the range of 6 to 9.5, in the range of 6.5 to 9, in the range of 6.8 to 8.5, in the range of 7 to 8, and more preferably a neutral pH of 6.5 to 7.5, for example pH 7.0, 7.1, or 7.3.

[0185] When formulated as a solid type, e.g., a tablet, the cleaning composition of the present invention is preferably dissolved in water to form a cleaning solution that is then applied to the hard surface to be cleaned. Such a cleaning solution preferably has a pH of less than 11, e.g., in the range of 6 to 9.5, 6.5 to 9, 6.8 to 8.5, or 7 to 8, more preferably in the range of 6.5 to 7.5, e.g., pH 7.0, 7.1, or 7.3.

[0186] Formulation of enzymes in co-granules The enzymes of the present invention can be formulated as granules, for example, co-granules that combine one or more enzymes, where each enzyme is present in more granules, ensuring a more uniform distribution of the enzymes within the detergent. This also reduces the physical segregation of the various enzymes due to their varying particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0187] Another example of formulating enzymes using co-granules is disclosed in WO 2013 / 188331, which relates to a cleaning composition comprising: (a) a multi-enzyme co-granule; (b) less than 10 weight percent zeolite (on an anhydrous basis); and (c) less than 10 weight percent phosphate (on an anhydrous basis), wherein the enzyme co-granule comprises 10 to 98 weight percent of a moisture sink component, and the composition additionally comprises 20 to 80 weight percent of a detergent moisture sink component. WO 2013 / 188331 also relates to a method of treating and / or cleaning a surface, the method comprising: (i) contacting the surface in an aqueous cleaning solution with the cleaning composition claimed and described herein; and (ii) rinsing and / or drying the surface.

[0188] The multi-enzyme co-granules may comprise an enzyme of the invention and one or more enzymes selected from the group consisting of (a) proteases, cellulases, amylases, pectinases, mannanases, pectate lyases, phosphodiesterases (PDEs), deoxyribonucleases (DNases), hexosaminidases, hemicellulases, and mixtures thereof.

[0189] In some embodiments, the hard surface cleaning composition may include the ingredients shown in Table 1 below.

[0190] [Table 11]

[0191] The invention is further summarized in the following paragraphs.

[0192] 1. (a) 0.1 to 60 wt. % of a surfactant system; (b) 0.1 to 40 wt. % of a solvent selected from the group consisting of lower alkanols, benzyl alcohol, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, e.g., linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10% by weight of lipase; 1. A hard surface cleaning composition comprising: 2. The composition of paragraph 1, wherein the surfactant system includes at least one surfactant selected from the group consisting of nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof.

[0193] 3. The composition of paragraph 1 or 2, wherein the surfactant system comprises one or more anionic surfactants and / or one or more nonionic surfactants.

[0194] 4. The composition of any one of paragraphs 1-3, wherein the surfactant system comprises one or more anionic surfactants, preferably linear alkylbenzene sulfonates (LAS), alcohol ether sulfates (AEOS), and / or alkyl sulfates (AS), particularly sodium lauryl sulfate (SLS).

[0195] 5. The surfactant system comprises one or more non-ionic surfactants, preferably alcohol ethoxylates (AEOs), especially linear alcohols (C 12~15 5. The composition of any one of paragraphs 1-4, comprising a hydroxypropyl ethoxylate (LAE).

[0196] 6. The composition of any one of paragraphs 1-5, wherein the anionic surfactant is present at a level of 0-20 wt%, 0.5-15 wt%, 2-15 wt%, 3-12 wt%, 4-10 wt%, or 1-5 wt%.

[0197] 7. The composition of any one of paragraphs 1 through 6, comprising an anionic surfactant linear alkylbenzene sulfonate (LAS) and a nonionic surfactant alcohol ethoxylate (AEO).

[0198] 8. The composition of any of the preceding paragraphs, wherein the nonionic surfactant is present at a level of 0.2 to 30 wt%, 0.5 to 25 wt%, 1 to 20 wt%, 2 to 15 wt%, 3 to 12 wt%, 4 to 10 wt%, or 6 to 8 wt%.

[0199] 9. Solvents include ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene-propylene glycol ethers, ethylene glycol phenyl ether, propylene glycol phenyl ether, propylene glycol methyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, tripropylene glycol butyl ether, tripropylene glycol methyl ether, ethylene glycol butyl ether, diethylene glycol methyl ether, diethylene glycol butyl ether, ethylene glycol dimethyl ether, ethylene glycol propyl ether, diethylene glycol ethyl ether, triethylene glycol methyl ether, triethylene glycol methyl ether, the composition of any of the preceding paragraphs, wherein the alkyl ether is selected from ethylene glycol ethyl ether, triethylene glycol butyl ether, ethylene glycol monobutyl ether, diethylene glycol monobutyl ether, triethylene glycol monobutyl ether, dipropylene glycol monobutyl ether, diethylene glycol monobutyl ether, hexyl ethoxylate (e.g., ethylene glycol monohexyl ether), 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, and combinations thereof, such as a combination of ethanol and diethylene glycol monobutyl ether, glycol ether, propylene glycol, or dipropylene glycol.

[0200] 10. The composition of any of the preceding paragraphs, wherein the solvent is present at a level of 0.2 to 35 wt%, 0.5 to 30 wt%, 1 to 25 wt%, 2 to 20 wt%, 3 to 15 wt%, 4 to 12 wt%, 5 to 10 wt%, or 6 to 8 wt%.

[0201] 11. The composition of any of the preceding paragraphs, further comprising one or more ingredients selected from the group of builders, chelating agents, dispersants, enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric dispersants, suds suppressors, dyes, fragrances, structural plasticizers, carriers, hydrotropes, processing aids, and / or pigments.

[0202] 12. The composition of any of the preceding paragraphs, further comprising an additional enzyme selected from the group consisting of protease, cellulase, amylase, pectinase, mannanase, pectate lyase, phosphodiesterase (PDE), deoxyribonuclease (DNase), hexosaminidase, hemicellulose, and combinations thereof.

[0203] 13. The composition of any one of paragraphs 1 to 12, wherein the lipase is of microbial origin, in particular of fungal or bacterial origin.

[0204] 14. The composition of any one of paragraphs 1-13, wherein the composition comprises a lipase, for example, a fungal lipase derived from a strain of Thermomyces lanuginosus lipase.

[0205] 15. Lipase is 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 1, 2, 3, 4, 5, 6, or 7; ii) variants with lipase activity having 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 to the lipase set forth as SEQ ID NO: 1, 2, 3, 4, 5, 6, or 7; iii) A fragment of the lipase of (i) or (ii) having lipase activity 15. The composition of any of paragraphs 1 through 14, wherein

[0206] 16. The composition of any one of paragraphs 1-15, wherein the lipase is a variant including T231R+N233R and optionally substitutions at positions corresponding to at least one or more of D96E, D111A, D254S, G163K, P256T, G91T, and G38A in SEQ ID NO:1.

[0207] 17. The lipase is a variant of a parent lipase, wherein 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% and less than 100% sequence identity to SEQ ID NO: 1, T231R+N233R, and: a.D96E+T231R+N233R b.N33Q+D96E+T231R+N233R; c.N33Q+D111A+T231R+N233R; d.N33Q+T231R+N233R+P256T; e.N33Q+G38A+G91T+G163K+T231R+N233R+D254S; f.N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; g.D27R+N33Q+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T; h.D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+P256T; i.D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S; j.D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; k.D96E+T231R+N233R+D254S; l.T231R+N233R+D254S+P256T; m.G163K+T231R+N233R+D254S; n.D27R+N33Q+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T; o.D27R+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; p.D96E+G163K+T231R+N233R+D254S; q.D27R+G163K+T231R+N233R+D254S; r.D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S; s.D27R+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T; t.D27R+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T; u.D27R+D96E+G163K+T231R+N233R+D254S; v.D27R+D96E+D111A+G163K+T231R+N233R+D254S+P256T; w.D27R+G38A+D96E+G163K+T231R+N233R+D254S+P256T; x.D111A+G163K+T231R+N233R+D254S+P256T; y.D111A+T231R+N233R; z.D111A+T231R+N233R+D254S+P256T; aa.D27R+D96E+D111A+G163K+T231R+N233R; bb.D27R+D96E+D111A+T231R+N233R; cc.D27R+N33Q+G38A+D96E+D111A+T231R+N233R+D254S+P256T; dd.D27R+G38A+D96E+D111A+G163K+E210Q+T231R+N233R+D254S+P256T; ee.D27R+T231R+N233R+D254S+P256T; ff.D96E+D111A+G163K+T231R+N233R; gg.D96E+D111A+G163K+T231R+N233R+D254S+P256T; hh.D96E+D111A+G163K+T231R+N233R+P256T; ii.D96E+D111A+T231R+N233R; jj.D96E+D111A+T231R+N233R+D254S; kk.D96E+D111A+T231R+N233R+D254S+P256T; ll.D96E+D111A+T231R+N233R+P256T; mm.D96E+G163K+T231R+N233R+D254S+P256T; nn.D96E+T231R+N233R+D254S+P256T; oo.D96E+T231R+N233R+P256T; pp.G38A+D96E+D111A+T231R+N233R; qq.G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; rr.G91T+D96E+D111A+T231R+N233R; ss.G91T+D96E+T231R+N233R; tt.G91T+T231R+N233R+D254S+P256T; uu.N33Q+D96E+D111A+G163K+T231R+N233R+D254S+P256T; vv.T231R+N233R+D254S+P256T; ww.T231R+N233R+P256T 17. The composition of any one of paragraphs 1-16, comprising a substitution at a position corresponding to at least one or more of D96E, D111A, D254S, G163K, P256T, G91T, and G38A of SEQ ID NO:1 selected from the group consisting of:

[0208] 18. The lipase is a variant of a parent lipase, said variant comprising: (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; (b) has at least 60% but less than 100% sequence identity to SEQ ID NO:1; (c) having lipase activity The composition of any one of paragraphs 1 to 17.

[0209] 19. The composition of any one of paragraphs 1 to 18, 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, wherein the numbering is according to SEQ ID NO: 1.

[0210] 20. The composition of paragraph 18 or 19, 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, wherein the numbering is according to SEQ ID NO: 1.

[0211] 21. The composition of any one of paragraphs 18 to 20, wherein the lipase variant further comprises one of the substitutions selected from the group of: S54T, S83T, G91A, A150G, I255A, and E239C, and the numbering is according to SEQ ID NO: 1.

[0212] 22. The composition of any one of paragraphs 18 to 21, wherein the lipase variant comprises the substitutions E1C+N233C and one or more additional substitutions, and the numbering is according to SEQ ID NO: 1.

[0213] 23. 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%, and less than 100% sequence identity to SEQ ID NO: 1, and the following set of substitutions using SEQ ID NO: 1 for numbering: E1C+H198L+N233C E1C+H198G+N233C E1C+L69V+N233C E1C+L69T+N233C E1C+L69S+N233C E1C+L69H+N233C E1C+L69F+N233C E1C+L69C+N233C E1C+H198Y+N233C E1C+H198T+N233C E1C+H198G+N233C E1C+L227F+N233C E1C+L227R+N233C E1C+E210T+N233C E1C+E210N+N233C E1C+V176M+N233C E1C+K98T+N233C E1C+K98E+N233C E1C+E56S+N233C E1C+E56Q+N233C E1C+E56R+N233C E1C+F51M+N233C E1C+D27R+F51Y+N233C E1C+V2I+N233C E1C+V2N+N233C E1C+V2K+N233C E1C+V2A+N233C E1C+D96L+N233C E1C+L69R+N233C E1C+V2Y+N233C E1C+N233C+P256T E1C+N233C+D254S E1C+T231R+N233C E1C+H198S+N233C E1C+D111A+N233C E1C+D96E+N233C E1C+G38A+N233C E1C+N33Q+N233C E1C+N33K+N233C E1C+E210A+N233C E1C+E210Q+N233C E1C+E210R+N233C E1C+H198D+N233C E1C+K98R+N233C E1C+K98V+N233C E1C+F51L+N233C E1C+F51I+N233C E1C+K237C E1C+L227G+N233C E1C+E210K+N233C E1C+V176L+N233C E1C+K98Q+N233C E1C+E56K+N233C E1C+L147S+N233C+D254S E1C+Y220F+N233C E1C+K98I+N233C E1C+N233C E1C+D27R+F51I+E56R+K98E+T231R+N233C E1C+D27R+F51I+E56R+K98E+T231R+N233C+D254S E1C+D27R+G38A+F51L+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T E1C+D27R+G38A+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+G38R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+F51L+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+D27R+F51L+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T E1C+D27R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+D27R+G38A+F51I+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ P256T E1C+D27R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+D27R+F51V+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+D254S+ P256T E1C+D27R+F51V+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+ P256T E1C+D27R+F51V+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+D27R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+ P256T E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+F51V+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T E1C+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+F51V+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+F51V+K98I+D111A+G163K+H19S+Y220F+T231R+N233C+D254S+P256T E1C+F51I+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+D27R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+N33K+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+ T231R+N233C E1C+G38R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+G38R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+ N233C+D254S+P256T 23. The composition of any one of paragraphs 18 to 22, comprising or consisting of a substitution corresponding to one of:

[0214] 24. Lipase is 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:2; ii) Variants with lipase activity having 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 to the lipase set forth as SEQ ID NO:2: iii) A fragment of the lipase of (i) or (ii) having lipase activity The composition of paragraphs 1 to 23.

[0215] 25. The composition of paragraph 24, comprising or consisting of the amino acid sequence of SEQ ID NO:2.

[0216] 26. The lipase is a variant of SEQ ID NO: 2; Variants include the following of the polypeptide shown as SEQ ID NO:2: (a) Substitutions corresponding to: D1E,Q; A4R; D5Q; L7Y; N8D,E,Q; K11E,Q; R24E,N,Q; N26Q; D27N,Q; A30N; N33Q; T35N; N39D,Q; A46Q; D48Q; F51I,V; L52N,E56N; N57Q; G59S; V60S,M,D62Q; D70Q; N71Q; N73S; I86F,P; N88D,Q; I90R; L93F; N94Q,R,S; D96H,I,Q,S; V98I; N101D ,Q,R;S105R;R108E,Q;D111Q;D122Q;D130Q;D158Q;N162D,E;Y164S;D165Q;D167Q;A173Q;N178D;A180E;N200Q;R209Q;Q210E;F211A,N,S,T,Y;G212D,E,R;L227G,V228E,P;R231Q;R232E,Q;R233K,N,Q;T244E;N250D;I255A;A257S;L264A,V,I; and / or (b) Substitutions corresponding to: A4E+F211V; A4E+L227G; A4E+T252A; D122N+L124S; D165N+D167S; D96N+V98S; E45N+A47S; E87K+F95Y; E87R+N94D; F211V+L227G; F211V+L264A; F211V+T252A; I238C+G246C; L227A+L264A; L2 27G+I269W;L264A+I269W;N250P+T252I;S105D+R108G;T123N+R125S;T252A+I269W;T252A+L264A;T252A+L264I;T252A+L264P;T252A+L264Q;T252A+L264S;T252A+L264T;T72N+K74S;V60M+L227G; and / or (c) Substitutions corresponding to: <h2 style=";text-align:left;direction:ltr">A40N+T252A+L264A;A46N+T252A+L264A;A46N+T252A+L264A;A46R+T252A+ L264A;D130H+N250P+T252I;D1A+T252A+L264A;D1C+T252A+L264A;D1F+T2 52A+L264A;D1G+T252A+L264A;D1H+T252A+L264A;D1L+T252A+L264A;D1M+ T252A+L264A;D1G+T252A+L264A;D1R+T252A+L264A;D1W+T252A+L264A;D1Y +T252A+L264A;D5R+T252A+L264A;D62R+T252A+L264A;F10L+T252A+L264A F10M+T252A+L264A;F211V+L264A+I269W;F211V+T252A+L264A;F51G+T252 A+L264A;F51K+T252A+L264A;G106E+N250P+T252I;G65A+T252A+L264A;G6 5W+T252A+L264A;H198I+T252A+L264A;H198N+P256T+A257I;K74G+T252A+L 264A;L12H+N250P+T252I;L227G+T252A+L264A;L75A+T252A+L264A;L75K+ T252A+L264A;L75Y+T252A+L264A;L7F+T252A+L264A;N250P+T252I+I255D ;N39S+T252A+L264A;N8K+T252A+L264A;N8R+T252A+L264A;N94D+T252A+L 264A;Q15M+T252A+L264A;R108Q+R179E+G212E;R232N+T252A+L264A;S37H+ N250P+T252I;S3R+T252A+L264A;T50H+T252A+L264A;T50L+T252A+L264A;T50M+T252A+L264A;T50W+T252A+L264A;T50Y+T252A+L264A;V228R+T252A+ L264A;V63C+T252A+L264A;V63E+T252A+L264A;V63G+T252A+L264A;V63I+ T252A+L264A;V63L+T252A+L264A;V63Q+T252A+L264A;V63S+T252A+L264A;A19T+T252A+L264A;A19S+T252A+L264A;K11L+T252A+L264A;A20V+T252A+L264A;A20T+T252A+L264A;S17C+T252A+L264A;I34S+T252A+L264A;T32P+T252A+L264A;N26A+T252A+L264A;N26W+T252A+L264A;N26K+T252A+L264A;S37V+T252A+L264A;S37Y+T252A+L264A;S37E+T252A+L264A;D27E+T252A+L264A;A38S+T252A+L264A;T72I+T252A+L264A;T72V+T252A+L264A;V60T+T252A+L264A;L43G+T252A+L264A;N33V+T252A+L264A;N33F+T252A+L264A;N33D+T252A+L264A;P42S+T252A+L264A;A47G+T252A+L264A;A47R+T252A+L264A;G31V+T252A+L264A;A46F+T252A+L264A;A46F+T252A+L264A;A46G+T252A+L264A;A40H+T252A+L264A;A46K+T252A+L264A;D62G+T252A+L264A;D62A+T252A+L264A;F66K+T252A+L264A;A49V+T252A+L264A;T50A+T252A+L264A;F51H+T252A+L264A;A49G+T252A+L264A;V63M+T252A+L264A;F51L+T252A+L264A;T50N+T252A+L264A;V63T+T252A+L264A;F51P+T252A+L264A;A49S+T252A+L264A;A49Q+T252A+L264A;V63A+T252A+L264A;S54R+T252A+L264A;F51Y+T252A+L264A;S54D+T252A+L264A;T64S+T252A+L264A;S54C+T252A+L264A;F66N+T252A+L264A;L52W+T252A+L264A;L52T+T252A+L264A;A68V+T252A+L264A;N57S+T252A+L264A;L67Y+T252A+L264A;V69Q+T252A+L264A;S58Y+T252A+L264A;N71C+T252A+L264A;D70R+T252A+L264A;V60M+T252A+L264A;N71G+ T252A+L264A;V69E+T252A+L264A;V69K+T252A+L264A;N71D+T252A+L264A;N71T+T252A+L264A;V60A+T252A +L264A;V60W+T252A+L264A;G61A+T252A+L264A;V60G+T252A+L264A;T72G+T252A+L264A;V60L+T252A+L264 A;A4R+R233N+T252A;A4R+R233N+L264A;R233N+T252A+L264A;A4R+V60M+L227G;A4R+L227G+R233N;A4R+V60M +R233N;V60M+L227G+R233N;V60M+L227G+L264V;V60M+L227G+L264I;V60M+L227G+T252A;A4R+L227A+L264A ;G23A+N250P+T252I;V60K+N250P+T252I;L97V+N250P+T252I;A150G+N250P+T252I;V202L+N250P+T252I;V22 8P+N250P+T252I;L227G+N250P+T252I;F211G+N250P+T252I;V142I+N250P+T252I;V60M+L227G+V228Q;A4L+T252A+L264A;T114E+T252A+L264A;G156A+T252A+L264A;L168E+T252A+L264A;N73G+T252A+L264A;and / or; (d) Substitutions corresponding to: A4K+R231T+T252A+L264A;A4K+R232V+T252A+L264A;L227G+V228A+T252A+L264I;L7F+L227G+T252A+L264A;N250P+T252I+D2 54N+P256S;Q249N+N250P+N251S+T252I;T244N+G246S+N250P+T252I;T91A+N92D+D96L+V98Q;T91A+V228L+T252A+L264S;V20 2C+N250P+T252I+P253C;V60M+T91A+T252A+L264A;W221C+G246C+N250P+T252I;D1C+R233C+T252A+L264A;V60M+D99N+N101S+L227G;V60M+S119N+A121S+L227G;V60M+R125N+A127S+L227G;D1G+T252A+P256T+L264A;V60M+L227G+V228R+L264T; and / or (e) Substitutions corresponding to: T91A+H198N+D254S+P256T+A257I; T91A+T252A+I255L+P256K+L264A; V60M+L227G+V228L+T252A+L264Y; V60M+L227V+V228P+T252A+L264I; V60M+T91A+L227R+T252A+L264V; N33Q+V60M+G163N+D165S+L227G; R24E+A180E+N250D+T252A+L264A; and / or V60M+T91A+L227V+T252A+L264M; and / or (f) Substitutions corresponding to: L7F+T91A+A150G+L154V+T252A+L264A; and / or (g) Substitutions corresponding to: D1C + V202C + R233C + I238C + G245C + T252A + P253C + L264A; and / or A4R + I90V + N94E + D96L + N101P + R233N + T252A + L264A 26. The composition of paragraph 24 or 25, which is a variant of SEQ ID NO: 2, comprising:

[0217] 27. 15. The composition of paragraph 26, further comprising one or more detergent ingredients: A4E;A20T;P29S;A46Q;S58N;T91A;N92D;L93F,I;S105D,E,N;R179G,Q;N200R; Y220F;L227G;R231K;T244E;Q249E;T252A,S,V;N25S;A38T;R84S;N94D;V98Q;N 101K;D130H;D137G;R232K;T244A,N,K;A249G,R;N250P;T252I;D254S;P256T;A 257I;L264A;N94V;F95V;L97S;N101E;S105K;D129G;A134S;V187I;Q188H;R209 The composition of paragraph 26, further comprising one or more substitutions corresponding to Q; Q210D; G212S; D234R; G240D; N248D,E; Q249D,G; L264V; T267A; I269F; A28V; V60E,I,M; V63I; E87Q; N92D; V98Q; S105G; R179K; V228L; N248K; Q249D; I255G; L264P,Y; A4Q; L7F; A46K; Y53F; V60K; E87K; Y138F; A157V; Y194F; H198I; Y213F; L227V,V228A; and / or I255L (using sequence number 2 for numbering).

[0218] 28. A20T+L93F;A4E+A46Q;F51I+T244E;L227G+R233N;L227G+T244E;L227G+T252A;L93I+V 98I;N101D+S105D;Q210E+Q249E;R179Q+G212E;R231K+R233K;R233N+T252A;S105D+G21 28. The composition of any of paragraphs 26 or 27, comprising substitutions corresponding to (using SEQ ID NO: 2 for numbering) T244E+T252A; T252A+I255A; T252S+I255A; and / or T91A+V98I.

[0219] 29. The composition of any of paragraphs 26-28, comprising substitutions corresponding to A4R+R233N; K223Q+R232Q; Q210E+N250D; R108Q+G212E; R24Q+N250D and / or R24Q+Q210E (using SEQ ID NO: 2 for numbering).

[0220] 30. A38T+D96H+D137G;A4R+T252A+L264A;D1G+T252A+L264A;D62N+T252A+L264A;D165Q+N250P+T252I;H1 98S+Y220F+L264A;N101K+S105N+R108E;N94Q+N250P+T252I;Q210E+T244E+Q249G;Q210E+T252A+L264A 30. The composition of any of paragraphs 26 to 29, comprising substitutions corresponding to (using SEQ ID NO: 2 for numbering): R231K+R232K+R233K; S83T+H198S+D254S; R233N+T252A+L264A; A46Q+T252A+L264A; N39D+T252A+L264A; R24E+V60M+L227G; and / or F51I+T252A+L264A.

[0221] 31. A4R+R233N+T252A+L264A;A4R+V60M+L227G+R231T;A4R+V60M+L227G+R232V;A4R+V60M+L227G+R233N;E87Q+T 91A+D96I+V98Q;G109R+Q210E+T244N+Q249E;L227G+R233N+T252A+L264A;L7F+Q210E+T252A+L264A;Q188H+Q 31. The composition of any of paragraphs 26-30, comprising substitutions corresponding to (using SEQ ID NO: 2 for numbering): 210E+T252A+L264A; Q210E+L227G+T252A+L264A; Q210N+G212S+N250P+T252I; V60S+L227G+T252A+L264A; R24E+N33Q+V60M+L227G; and / or R24E+V228P+T252A+L264A.

[0222] 32. The composition of any of paragraphs 26-31, comprising substitutions corresponding to (using SEQ ID NO: 2 for numbering): L227G + R233N + T244E + T252A + L264A; S105N + R108Q + D129G + D137G + G212D; L7F + R24E + N39D + T252A + L264A; R24E + V128A + V228E + T252A + L264A; or A20T + G163N + D165S + T252A + L264A.

[0223] 33. L7F+N8K+Q210E+L227G+T252A+L264A;8D+101K+S105G+R108Q+R179E+G212E;N8 D+R209Q+Q210E+T244N+N248K+Q249E;V60E+S83T+T91A+H198S+T252A+L264P;or 33. The composition of any of paragraphs 26-32, comprising substitutions corresponding to V60M+T91A+Q210E+V228L+T252A+L264Y (using SEQ ID NO: 2 for numbering purposes).

[0224] 34. V60K+S83T+T91A+H198I+V228L+T252A+L264P; or The composition of any of paragraphs 26-33, including substitutions corresponding to V60M+A157V+Q210E+L227V+V228A+T252A+L264V (using SEQ ID NO: 2 for numbering purposes).

[0225] 35. The composition of any of paragraphs 26-34, including substitutions corresponding to D1E+A4Q+L7F+K11N+S37T+A46K+A133R+V142F+T170S+V202I+Q210E+L227G (using SEQ ID NO: 2 for numbering purposes).

[0226] 36. The composition of any of the preceding paragraphs, wherein the additional enzyme is a protease, hexosaminidase, DNase, amylase, cellulase, or a combination thereof, e.g., a combination of protease and DNase, and / or a combination of hexosaminidase, or a combination of protease and amylase.

[0227] 37. The composition of any of the preceding paragraphs, wherein the composition comprises probiotic spores, preferably the probiotic spores are of Bacillus genus origin.

[0228] 38. The composition of any of the preceding paragraphs formulated as a liquid, gel, paste, bar, powder, tablet, pouch with one or more compartments, single or multi-compartment unit dose form, or spray form.

[0229] 39. The composition of any of the preceding composition paragraphs which is a hand dish detergent, a professional cleaning detergent, a medical cleaning detergent, or a hard surface cleanser.

[0230] 40. (a) 1 to 60 wt. %, e.g., 3 to 40 wt. %, 5 to 25 wt. % of a surfactant system; (b) 1 to 40 wt. %, e.g., 3 to 20 wt. %, 5 to 10 wt. % of a solvent selected from the group consisting of lower alkanols, benzyl alcohols, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, e.g., linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10% by weight of lipase; wherein preferably said lipase is as defined in any of the preceding composition paragraphs 14 to 35.

[0231] 41. Surfactant systems include linear alkylbenzene sulfonates (LAS), alcohol ether sulfates (AEOS), alkyl sulfates (AS), especially sodium lauryl sulfate (SLS) and sodium laureth sulfate (SLES), and alcohol ethoxylates (AEO), especially linear alcohol (C 12~1541. The cleaning composition of paragraph 40, comprising one or more surfactants selected from:

[0232] 42. The cleaning composition of paragraphs 40-41, wherein the solvent is present at a level of 2 to 12 wt.%, e.g., 2.1 to 10 wt.%, 2.2 to 10 wt.%, 2.4 to 8 wt.%, 2.6 to 8 wt.%, 2.8 to 5 wt.%, 3 to 6 wt.%, 4 to 6 wt.%, based on the total weight of the composition, and the solvent includes: at least a lower alkyl glycol ether, such as ethylene glycol monohexyl ether, or a mixture of ethylene glycol monohexyl ether and dipropylene glycol monobutyl ether; or at least an alcohol ethoxylate, such as a linear alcohol ethoxylate, a branched alcohol, and / or an oxoalcohol ethoxylate.

[0233] 43. The composition of any of the preceding composition paragraphs, which is a spray-type detergent and has a pH of less than 11, e.g., in the range of 6 to 9.5, in the range of 6.5 to 9, in the range of 6.8 to 8.5, or in the range of 7 to 8, and more preferably has a neutral pH of 6.5 to 7.5, e.g., pH 7.0, 7.1, or 7.

[0234] 44. The composition of any of the preceding composition paragraphs, formulated in liquid form and having a pH of less than 11, e.g., in the range of 6-9.5, 6.5-9, 6.8-8.5, or 7-8, more preferably a neutral pH of 6.5-7.5, e.g., pH 7.0, 7.1, or 7.

[0235] 45. A method of cleaning an article, comprising contacting the surface with the cleaning composition of any one of the preceding paragraphs, preferably wherein the article is a surface, such as a hard surface, or a fabric.

[0236] 46. The method of paragraph 45, wherein the contacting is carried out by spraying, wiping, pouring, dipping, and / or wiping the surface with the hard surface cleaning composition.

[0237] 47. The method of paragraph 45 or 46, wherein the hard surface is selected from steel, rubber, plastic, glass, ceramic, melamine, wood, a coated surface, a cement countertop, a kitchen countertop surface, and a medical device surface.

[0238] 48. The method of any of paragraphs 45-47, wherein the lipase is formulated at a concentration of at least 0.0001 mg of enzyme protein per gram of the hard surface cleaning composition, e.g., at least 0.001 mg of enzyme protein, at least 0.006 mg of enzyme protein, at least 0.008 mg of enzyme protein, at least 0.01 mg of enzyme protein, at least 0.1 mg of enzyme protein, at least 0.5 mg of enzyme protein, at least 1 mg of enzyme protein, at least 2 mg of enzyme protein, at least 5 mg of enzyme protein, at least 10 mg of enzyme protein, or at least 20 mg of enzyme protein.

[0239] 49. A ready-to-use article for cleaning surfaces, such as hard surfaces, comprising any of the above cleaning compositions.

[0240] 50. An article of paragraph 49 that is a wipe or sponge.

[0241] 51. The article of paragraph 49 or 50, saturated with any of the preceding hard surface cleaning compositions.

[0242] The present invention is further illustrated in the following non-limiting examples. [Example]

[0243] Assay I: Lipase activity determined by p-nitrophenyl (pNP) assay The hydrolysis activity of lipase can be determined by a kinetic assay using p-nitrophenyl acyl esters as substrates. Substrates p-nitrophenyl butyrate (C4), p-nitrophenyl caproate (C6), p-nitrophenyl caprate (C10), p-nitrophenyl laurate (C12), and p-nitrophenyl palmitate (C16) (all from Sigma-Aldrich Denmark A / S, Kirkebjerg Alle 84, 2605 Brondby; catalog numbers: C3: N-9876, C6: N-0502, C10: N-0252, C12: N-2002, C16: N-2752) are diluted from 100 mM stock solutions in DMSO to final concentrations of 1 mM and 25 mM in assay buffer (50 mM Tris, pH 7.7, 0.4% Triton® X-100). Lipase in 50 mM Hepes; pH 8.0; 10 ppm Triton® X-100; + / - 20 mM CaCl was added to the following final protein concentrations: 0.01 mg / ml; 5 x 10 -3 mg / ml; 2.5 x 10 -4 mg / ml; and 1.25 × 10 -4 The substrate solution is added at 100 mg / ml to a 96-well NUNC plate (catalog no. 260836, Kamstrupvej 90, DK-4000, Roskilde). The release of p-nitrophenol by hydrolysis of p-nitrophenyl acyl can be monitored at 405 nm for 5 min at 10 s intervals using a Spectra max 190 (Molecular Devices GmbH, Bismarckring 39, 88400 Biberach an der Riss, Germany).

[0244] Materials and Methods Lipase A: Thermomyces lanuginosus lipase (TLL) as shown in SEQ ID NO: 1, with the following substitutions: E1C + D27R + G38A + F51V + D96E + K98I + D111A + G163K + H198S + Y220F + T231R + N233C + D254S + P256T Solvent A: Diethylene glycol monobutyl ether (BuCb) (available from Dow chemical) Solvent B: Glycol ether (EPH) (available from Usolf) Model detergent M1: 2 wt% fatty alcohol polyoxyethylene ether-9 (AEO-9). The pH of the model detergent was adjusted to about 11 or 8.5 by using monoethanolamine. A commercial detergent was used: DAWN Powerwash spray detergent (available from P&G), which contains approximately 3% by weight of dipropylene glycol butyl ether (DPGBE) solvent. Model detergent V1: 4% by weight sodium laureth sulfate, 1% by weight alkyldimethylamine oxide (OA-2), 2.84% by weight ethylene glycol monohexyl ether (C6EO1), 2.78% by weight DPGBE, 3.2% by weight PPG 400. Adjusted to 100% with water. Model detergent V2: 4% by weight sodium laureth sulfate, 1% by weight alkyldimethylamine oxide (OA-2), 2.84% by weight ethylene glycol monohexyl ether (C6EO1), 2.78% by weight DPGBE, 3.2% by weight fatty alcohol polyoxyethylene ether-9 (AEO-9). Water to 100%.

[0245] Example 1 Soil removal testing of model detergents for hard surface applications Six different oils were mixed together in the amounts shown in Table 2 below to prepare an oil mixture. A stainless steel card was weighed to obtain the initial weight (labeled as MO). Approximately 0.3 g of the oil mixture was spread evenly on the stainless steel card. The oil mixture-soiled card was then aged in a 120°C oven for 1 hour and kept dry until use.

[0246] [Table 12]

[0247] The soiled cards were weighed to obtain the pre-wash weight (labeled as M1) and then immersed in beakers containing various detergent formulations (see Table 3 below) at 35°C for 15 minutes or 7.5 minutes. The cards were then removed from the beakers and allowed to dry at room temperature. The dried cards were weighed to obtain the post-wash weight (labeled as M2).

[0248] The cleaning performance (or soil removal rate) of the various formulations was calculated as follows: (M1-M2) / (M1-M0) x 100%

[0249] Three replicates were performed for each formulation and the average stain removal rates are summarized in Table 3 below.

[0250] The improvement in soil removal rate (ISR) due to the addition of lipase and / or solvent was calculated as follows: Soil removal rate of model detergent with lipase and / or solvent - Soil removal rate of model detergent alone

[0251] [Table 13]

[0252] As can be seen from Table 2 above, the soil removal rate decreased when the pH of the detergent was lowered from pH 11 to pH 8.5 (Formulation 2 vs. Formulation 1). Adding lipase or solvent to the hard surface model detergent under reduced pH offset some of the loss in cleaning performance (Formulations 3 or 4 vs. Formulation 2; Formulations 6 or 7 vs. Formulation 2). Surprisingly, when both lipase and solvent were added together to the model detergent, the soil removal rate was greatly improved, even exceeding that of the original high pH model detergent.

[0253] Additionally, by comparing formulations 9 or 10 with formulation 2, it is clear that the inclusion of both lipase and solvent together in a hard surface detergent can achieve similar cleaning performance in a much shorter time (50% less), or in other words, can improve the cleaning efficiency of the detergent.

[0254] The enhanced cleaning effect due to the synergistic effect of lipase and solvent allows hard surface cleaning detergents to be formulated as low or mild pH detergents (e.g., pH 9 or even below) without compromising cleaning performance compared to traditional high pH formulations.

[0255] Example 2 Establishing enhanced cleaning effects in commercial detergents DAWN Powerwash spray detergent (available from P&G) contains solvents such as dipropylene glycol butyl ether and hexyl ethoxylate. 50 ppm of Lipase A was added to the detergent.

[0256] Example 2a: Testing on greasy homemade stains Preparation of greasy homemade stain: 1) Beef tallow was melted in a 70°C water bath. 2) Using a pipette, remove 40-100 μL of the molten beef tallow and apply it to a 6 cm diameter circle on the tile. 3) Use a figure to spread the stain evenly over the surface of the tile. 4) Wait approximately 2-4 hours before performing the cleaning test.

[0257] Cleaning test: 1) Prepare a spray detergent containing 50 ppm lipase. 2) Spray the detergent with or without lipase onto the stain once (one full trigger spray). 3) Leave at room temperature for 15 minutes or 1 minute (see Table 4 below), then rinse gently under running water for approximately 20 seconds. 4) Prepare a 0.3% Oil Red O (available from Sigma) solution in 75% ethanol. 5) The cleaned tiles are immersed in a 0.3% Oil Red O solution to visualize residual greasy stains. The more residual stain there is, the redder the tile will appear. 6) Allow the tiles to dry at room temperature. 7) Measure the R460nm of the dried tile by DigiEye (Model Number: DigiEye Colour Measurement and Imaging System, Serial Number DE0114501). The higher the R460nm value, the less reddish the tile is, and therefore the higher the level of stain removal. 8) Nine replicates were performed and the average R460nm values are listed in Table 4 below.

[0258] [Table 14]

[0259] The results, confirmed in Table 4, showed the enhanced cleaning effects (increased levels of soil removal and improved wash efficiency) described above, and additionally suggested that by using both lipase and solvent, the amount of detergent could be reduced (e.g., 20% reduction) while still achieving better soil removal performance (condition 3 vs. 1).

[0260] Example 2b: Test with stubborn technical stain DM-90 Cleaning test: 1) Prepare a spray detergent containing 50 ppm lipase. 2) Spray the detergent with and without lipase three times onto a DM-90 stain tile (available from CFT (Center For Test materials)). 3) Leave at room temperature for 15 minutes or 2 minutes (see Table 5 below), then rinse gently under running water for approximately 20 seconds. 4) Allow the tiles to dry at room temperature. 5) The R460nm of the dried tile is measured by DigiEye (Model Number: DigiEye Colour Measurement and Imaging System, Serial Number DE0114501). A higher R460nm value indicates a higher level of soil removal or soil removal performance. 6) Ten replicates were performed and the average R460nm values are tabulated in Table 5 below. A picture of the ten replicates is shown in Figure 1. From Figure 1, it is clear that under conditions 1 or 2, the entire plate is very reddish, indicating that most of the stain still remained. Conversely, under condition 3, where the detergent contains both solvent and lipase, the reddish areas are replaced by whitish / grayish circles (which are the areas where the detergent has come into contact), indicating that the stain has been removed.

[0261] [Table 15]

[0262] The results, confirmed in Table 5, showed the enhanced cleaning efficacy described above and additionally suggested that by using both lipase and solvent, the amount of detergent could be reduced (e.g., 20% reduction) while still achieving better soil removal performance against stubborn technical stains (condition 3 vs. 1).

[0263] Example 3 Testing the removal of greasy stains with model dishwashing detergents a) Preparation of bovine tallow 1) Melt the beef tallow in a 70°C water bath. 2) Using a pipette, remove 40 μL of the molten beef tallow and apply it to a 6 cm diameter circle on the melamine tile. 3) Use a figure to spread the stain evenly over the surface of the tile. 4) Wait approximately 2-4 hours before performing the cleaning test. b) Preparation of a mixed stain containing fat 5) A mixed stain containing fat (beef tallow: hot pot base seasoning containing salad oil, approximately 3:2) is melted in a water bath at 70°C. 6) Using a pipette, remove 40 μL of the oily melt mix stain and apply it to a 6 cm diameter circle on the melamine tile. 7) Use a figure to spread the stain evenly over the surface of the tile. 8) Wait approximately 2-4 hours before performing the cleaning test.

[0264] Washing performance test 1) Model detergents V1 and V2 were prepared with or without 77 ppm Lipase A. The pH of the detergents was adjusted to pH 9, 10, or 10.5 by using sodium hydroxide. 2) Spray the detergent with or without Lipase A onto each stain three times. 3) Leave at room temperature for 15 minutes, then rinse gently under running water for approximately 10 seconds. 4) Allow the tiles with the mixed oil stain to dry at room temperature. For the tallow stained tiles, perform the following steps 5) and 6) to visualize the residual stain before measurement. 5) Prepare a 0.3% Oil Red O (available from Sigma) solution in 75% ethanol. 6) Visualize residual greasy stain by immersing the cleaned cow tallow tiles in a 0.3% Oil Red O solution and allowing the tiles to dry at room temperature. The more residual stain there is, the redder the tile will appear. 7) Measure the R460nm of the dried tile by DigiEye (Model Number: DigiEye Colour Measurement and Imaging System, Serial Number DE0114501). A higher R460nm value indicates a higher level of soil removal or a cleaner tile. 8) Three replicates were performed and the average R460nm values are listed in Tables 6-8 below.

[0265] [Table 16]

[0266] [Table 17]

[0267] [Table 18]

[0268] From Tables 6, 7, 8, and Figure 2, it is clear that model detergents V1 and V2 can demonstrate significant and consistent lipase performance against greasy stains. Also, the significant cleaning effect of lipase is perceptible to the naked eye. See Figure 2.

[0269] Example 4 Greasy stain removal test on fabric Preparation of oil-containing mixed stain 1) A mixed stain containing fat (beef tallow: hot pot base seasoning containing salad oil, approximately 3:2) is melted in a water bath at 70°C. 2) Using a pipette, remove 30 μL of the oily melt-mix stain and apply it to the PCN01 fabric, and use your finger to spread the stain evenly over the surface of the fabric; the final circle of stain was approximately 2.8 cm. 3) Wait overnight before performing the cleaning test.

[0270] Washing performance test 1) Prepare model detergent V2 with or without 77 ppm Lipase A. 2) Spray the detergent with or without Lipase A onto each stain three times. 3) Leave at room temperature for 15 minutes, then rinse under running water for approximately 10 seconds. 4) Allow the fabric to dry thoroughly at room temperature. 5) The R460nm of the dried fabric is measured by Datacolor 800V (serial number 8814595). A higher R460nm value indicates a higher level of soil removal or cleaner fabric. 6) Three replicates were performed and the average R460nm values of the three replicates are listed in Table 9 below.

[0271] [Table 19]

[0272] From Table 9, it can be seen that detergents containing the solvents of the present invention can boost lipase performance against greasy stains present on fabrics.

Claims

1. (a) 0.1 to 60 wt. % of a surfactant system; (b) 0.1 to 40 wt. % of a solvent selected from the group consisting of lower alkanols, benzyl alcohol, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, e.g., linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10% by weight of a lipase; 1. A hard surface cleaning composition comprising:

2. 10. The composition of claim 1, wherein the surfactant system comprises at least one surfactant selected from the group consisting of nonionic surfactants, anionic surfactants, cationic surfactants, amphoteric surfactants, zwitterionic surfactants, semi-polar nonionic surfactants, and mixtures thereof.

3. The solvent may be ethanol, propanol, isopropanol, butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene-propylene glycol ethers, ethylene glycol phenyl ether, propylene glycol phenyl ether, propylene glycol methyl ether, propylene glycol propyl ether, dipropylene glycol methyl ether, tripropylene glycol butyl ether, tripropylene glycol methyl ether, ethylene glycol butyl ether, diethylene glycol methyl ether, diethylene glycol butyl ether, ethylene glycol dimethyl ether, ethylene glycol propyl ether, diethylene glycol ethyl ether, triethylene glycol methyl ether, triethylene glycol methyl ether, 3. The composition of claim 1 or 2, wherein the alkyl ether is selected from ethylene glycol ethyl ether, triethylene glycol butyl ether, ethylene glycol monobutyl ether, diethylene glycol monobutyl ether, triethylene glycol monobutyl ether, dipropylene glycol monobutyl ether, diethylene glycol monobutyl ether, hexyl ethoxylates (e.g., ethylene glycol monohexyl ether), 2-ethoxyethyl alcohol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, and combinations thereof, such as a combination of ethanol and diethylene glycol monobutyl ether, glycol ether, propylene glycol, or dipropylene glycol.

4. The lipase is 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO: 1, 2, 3, 4, 5, 6, or 7; ii) variants having lipase activity that have 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 to the lipase set forth as SEQ ID NO: 1, 2, 3, 4, 5, 6, or 7; iii) A fragment of the lipase of (i) or (ii) having lipase activity. The composition according to any one of claims 1 to 3, wherein

5. 5. The composition of any one of claims 1 to 4, wherein the lipase is a variant comprising T231R+N233R and optionally substitutions at positions corresponding to at least one or more of D96E, D111A, D254S, G163K, P256T, G91T, and G38A in SEQ ID NO:

1.

6. The lipase is a variant of a parent lipase, wherein 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% and less than 100% sequence identity to SEQ ID NO: 1, T231R+N233R, and: a. D96E+T231R+N233R b. N33Q+D96E+T231R+N233R; c. N33Q+D111A+T231R+N233R; d. N33Q+T231R+N233R+P256T; e. N33Q+G38A+G91T+G163K+T231R+N233R+D254S; f. N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; g. D27R+N33Q+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T; h. D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+P256T; i. D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S; j. D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; k.D96E+T231R+N233R+D254S; l.T231R+N233R+D254S+P256T; m.G163K+T231R+N233R+D254S; n.D27R+N33Q+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T; o.D27R+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; p.D96E+G163K+T231R+N233R+D254S; q.D27R+G163K+T231R+N233R+D254S; r.D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S; s.D27R+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T; t.D27R+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T; u.D27R+D96E+G163K+T231R+N233R+D254S; v.D27R+D96E+D111A+G163K+T231R+N233R+D254S+P256T; w.D27R+G38A+D96E+G163K+T231R+N233R+D254S+P256T; x.D111A+G163K+T231R+N233R+D254S+P256T; y.D111A+T231R+N233R; z.D111A+T231R+N233R+D254S+P256T; aa.D27R+D96E+D111A+G163K+T231R+N233R; bb.D27R+D96E+D111A+T231R+N233R; cc.D27R+N33Q+G38A+D96E+D111A+T231R+N233R+D254S+P256T; dd.D27R+G38A+D96E+D111A+G163K+E210Q+T231R+N233R+D254S+P256T; ee.D27R+T231R+N233R+D254S+P256T; ff.D96E+D111A+G163K+T231R+N233R; gg.D96E+D111A+G163K+T231R+N233R+D254S+P256T; hh.D96E+D111A+G163K+T231R+N233R+P256T; ii.D96E+D111A+T231R+N233R; jj. D96E+D111A+T231R+N233R+D254S; kk. D96E+D111A+T231R+N233R+D254S+P256T; ll. D96E+D111A+T231R+N233R+P256T; mm. D96E+G163K+T231R+N233R+D254S+P256T; nn. D96E+T231R+N233R+D254S+P256T; oo. D96E+T231R+N233R+P256T; pp. G38A+D96E+D111A+T231R+N233R; qq. G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T; rr. G91T+D96E+D111A+T231R+N233R; ss. G91T+D96E+T231R+N233R; tt. G91T+T231R+N233R+D254S+P256T; uu. N33Q+D96E+D111A+G163K+T231R+N233R+D254S+P256T; vv. T231R+N233R+D254S+P256T; lol. T231R+N233R+P256T 6. The composition of any one of claims 1 to 5, comprising a substitution at a position corresponding to at least one or more of D96E, D111A, D254S, G163K, P256T, G91T, and G38A of SEQ ID NO: 1 selected from the group consisting of:

7. 7. The composition of any one of claims 1 to 6, wherein the lipase variant comprises the substitutions E1C+N233C and one or more additional substitutions, the numbering being according to SEQ ID NO:

1.

8. 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% and less than 100% sequence identity with SEQ ID NO: 1 and the following set of substitutions using SEQ ID NO: 1 for numbering: E1C+H198L+N233C E1C+H198G+N233C E1C+L69V+N233C E1C+L69T+N233C E1C+L69S+N233C E1C+L69H+N233C E1C+L69F+N233C E1C+L69C+N233C E1C+H198Y+N233C E1C+H198T+N233C E1C+H198G+N233C E1C+L227F+N233C E1C+L227R+N233C E1C+E210T+N233C E1C+E210N+N233C E1C+V176M+N233C E1C+K98T+N233C E1C+K98E+N233C E1C+E56S+N233C E1C+E56Q+N233C E1C+E56R+N233C E1C+F51M+N233C E1C+D27R+F51Y+N233C E1C+V2I+N233C E1C+V2N+N233C E1C+V2K+N233C E1C+V2A+N233C E1C+D96L+N233C E1C+L69R+N233C E1C+V2Y+N233C E1C+N233C+P256T E1C+N233C+D254S E1C+T231R+N233C E1C+H198S+N233C E1C+D111A+N233C E1C+D96E+N233C E1C+G38A+N233C E1C+N33Q+N233C E1C+N33K+N233C E1C+E210A+N233C E1C+E210Q+N233C E1C+E210R+N233C E1C+H198D+N233C E1C+K98R+N233C E1C+K98V+N233C E1C+F51L+N233C E1C+F51I+N233C E1C+K237C E1C+L227G+N233C E1C+E210K+N233C E1C+V176L+N233C E1C+K98Q+N233C E1C+E56K+N233C E1C+L147S+N233C+D254S E1C+Y220F+N233C E1C+K98I+N233C E1C+N233C E1C+D27R+F51I+E56R+K98E+T231R+N233C E1C+D27R+F51I+E56R+K98E+T231R+N233C+D254S E1C+D27R+G38A+F51L+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T E1C+D27R+G38A+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+G38R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+F51L+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+D27R+F51L+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T E1C+D27R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+D27R+G38A+F51I+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ P256T E1C+D27R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+D27R+F51V+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+D254S+ P256T E1C+D27R+F51V+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+ P256T E1C+D27R+F51V+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+D27R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+ P256T E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+F51V+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T E1C+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T E1C+F51V+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+F51V+K98I+D111A+G163K+H19S+Y220F+T231R+N233C+D254S+P256T E1C+F51I+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+D27R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+N33K+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+ T231R+N233C E1C+G38R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T E1C+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+ D254S+P256T E1C+D27R+G38R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+ N233C+D254S+P256T 8. A composition according to any one of claims 1 to 7, comprising or consisting of a substitution corresponding to one of:

9. The lipase is 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% identity, at least 96%, at least 97%, at least 98%, or at least 99%, or 100% sequence identity to SEQ ID NO:2; ii) Variants with lipase activity having 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 to the lipase set forth as SEQ ID NO:2: iii) A fragment of the lipase of (i) or (ii) having lipase activity. The composition according to any one of claims 1 to 8, wherein

10. The composition of any one of claims 1 to 9, comprising or consisting of the amino acids of SEQ ID NO:

2.

11. 11. The composition of any one of claims 1 to 10, wherein the additional enzyme is a protease, a hexosaminidase, a DNase, an amylase, a cellulase, or a combination thereof, such as a combination of a protease and a DNase, and / or a hexosaminidase, or a combination of a protease and an amylase.

12. The composition according to any one of claims 1 to 11, wherein the composition comprises probiotic spores, preferably the probiotic spores are of Bacillus origin.

13. The composition according to any one of claims 1 to 12, which is a spray-type detergent and has a pH of less than 11, for example, in the range of 6 to 9.5, in the range of 6.5 to 9, in the range of 6.8 to 8.5, or in the range of 7 to 8, more preferably a neutral pH of 6.5 to 7.5, for example, pH 7.0, 7.1, or 7.

14. A method of cleaning a hard surface, comprising contacting said surface with a hard surface cleaning composition according to any one of claims 1 to 13.

15. (a) 1 to 60 wt. %, e.g., 3 to 40 wt. %, 5 to 25 wt. % of a surfactant system; (b) 1 to 40 wt. %, e.g., 3 to 20 wt. %, 5 to 10 wt. % of a solvent selected from the group consisting of lower alkanols, benzyl alcohol, lower alkyl ethers, glycols, aryl glycol ethers, lower alkyl glycol ethers, glycerol ketals, esters, hydrocarbon / ester mixtures, dibasic esters, alcohol ethoxylates, e.g., linear alcohol ethoxylates, branched alcohol ethoxylates, or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10% by weight of a lipase; wherein preferably said lipase is as defined in any one of claims 4 to 10.

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