Hard surface cleaning composition and cleaning method

Abstract

Disclosed is a hard surface cleaning composition comprising: (a) from 0.1 to 60 wt% of a surfactant system; (b) 0.1 to 40 wt% of a solvent, wherein the solvent is selected from the group consisting of lower alkanols, benzyl alcohols, lower alkyl ethers, ethylene glycol, aryl glycol ethers, lower alkyl glycol ethers, glyceroketal, esters, hydrocarbon / ester blends, dibasic esters, linear alcohol ethoxylates, branched alcohols, oxo-synthetic alcohol ethoxylates, and combinations thereof; and (c) optionally from 0.001 to 10 wt% of a lipase.

Description

[0001] References to sequence listings

[0002] This application contains a Sequence Listing in computer readable form, which is incorporated herein by reference. Technical Field

[0003] The present invention relates to a cleaning composition for removing stains, in particular lipid or greasy soils, from hard surfaces, such as tableware or kitchen worktop surfaces. The present invention also relates to a method for cleaning hard surfaces and a ready-to-use article comprising said composition. Background Art

[0004] Hard surface cleaning compositions can be used on a variety of surfaces, such as industrial surfaces and household surfaces (e.g., kitchen surfaces). During use between cleanings, these surfaces can rapidly accumulate various dirts, such as greasy dirt, dust, and even biofilms, and soon these dirts become difficult to remove. For ease of cleaning, conventional hard surface cleaning agents have a high pH (generally higher than pH 10). However, high pH cleaning agents can harm the skin of the hands and also damage the environment. High pH may also damage surface materials (e.g., coatings) and cause surface roughness, which makes it more difficult to remove dirt. In addition, in some cases, the washing performance of high pH conventional detergents may not be enough to remove stubborn stains such as kitchen grease.

[0005] Therefore, there is a need to develop hard surface cleaning compositions having a milder pH and improved cleaning performance compared to high pH conventional cleaning compositions.

[0006] On the other hand, in some current detergent formulations, lipases do not show satisfactory enhanced washing performance, which limits the application of lipases in, for example, hard surface cleaning detergents. Therefore, there is a need to develop a detergent formulation that enables lipases to work significantly and continuously, thereby promoting the removal of greasy soils (e.g., kitchen grease). Summary of the invention

[0007] The present invention relates to a hard surface cleaning composition, comprising:

[0008] (a) 0.1 to 60 wt % of a surfactant system;

[0009] (b) 0.1 to 40 wt % of a solvent, wherein the solvent is 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and combinations thereof; and optionally

[0010] (c) 0.001 to 10 wt% of lipase.

[0011] The cleaning composition of the present invention may further comprise one or more components selected from the following group: a builder, a chelating agent, a dispersant, an enzyme stabilizer, a catalytic material, a bleach activator, hydrogen peroxide, a source of hydrogen peroxide, a preformed peracid, a polymeric dispersing agent, a suds suppressor, a dye, a perfume, a structural elastic agent, a carrier, a hydrotrope, a processing aid, a pigment and / or an additional enzyme.

[0012] In a preferred embodiment, the cleaning composition of the present invention comprises one or more lipases shown in any one of SEQ ID NO: 1, 2, 3, 4, 5, 6 or 7 or variants thereof.

[0013] In an embodiment, the cleaning composition of the present invention comprises a commercial lipase product selected from the group consisting of: Lipolase TM 、Lipex TM ;Lipolex TM , Lipoclean TM , Lipex Evity 100L, Lipex Evity 105T, LipexEvity 200L (from Novozymes), Lumafast (originally from Genencor), Preferenz L100 (Danisco US Inc.), and Lipomax (originally from Gist-Brocades).

[0014] In an embodiment, the cleaning composition of the present invention comprises a solvent selected from the group consisting of ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene glycol-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 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-ethoxyethanol, 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, ethylene glycol ethers, propylene glycol or dipropylene glycol.

[0015] The present invention also relates to methods for cleaning hard surfaces which methods comprise contacting the surface with a hard surface cleaning composition of the present invention.

[0016] The present invention further relates to a ready-to-use article (eg a wipe or sponge) for cleaning hard surfaces, wherein the article comprises a hard surface cleaning composition according to the invention.

[0017] Sequence Overview

[0018] SEQ ID NO: 1 is the wild-type Thermomyces lanuginosus lipase (synonym: Humicola lanuginosa DSM 4109 lipase), often abbreviated to "TLL".

[0019] SEQ ID NO: 2 is a variant of the Thermomyces lanuginosus lipase as disclosed in SEQ ID NO: 2 in WO 2019 / 154952.

[0020] SEQ ID NO: 3 is a lipase from Geotrichum candidum.

[0021] SEQ ID NO: 4 is a lipase from Geotrichum candidum.

[0022] SEQ ID NO: 5 is a lipase from Geotrichum candidum.

[0023] SEQ ID NO: 6 is a lipase from Geotrichum candidum.

[0024] SEQ ID NO: 7 is a lipase from Geotrichum candidum. BRIEF DESCRIPTION OF THE DRAWINGS

[0025] The present invention will now be described in more detail with reference to the accompanying drawings showing exemplary embodiments of the invention, in which:

[0026] Figure 1 Shown are DM-90 stained tiles washed under different wash conditions.

[0027] Figure 2 Shown is the washing performance of standard detergent V2 (pH 8) with or without lipase on mixed greasy stains with a soak time of 15 min.

[0028] definition

[0029] 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.

[0030] If not otherwise indicated, all percentage references relating to the disclosed compositions relate to wt % relative to the total weight of the respective composition.

[0031] Lipase: The terms "lipase / lipase enzyme", "lipolytic enzyme", "lipid esterase", "lipolytic polypeptide" and "lipolytic protein" refer to enzymes in the EC3.1.1 class as defined in the enzyme nomenclature. It may have lipase activity (triacylglycerol lipase, EC3.1.1.3), cutinase activity (EC3.1.1.74), sterol esterase activity (EC3.1.1.13) and / or wax ester hydrolase activity (EC3.1.1.50). For the purposes of the present invention, lipase activity (i.e., the hydrolytic activity of lipase) may be determined using a pNP assay with substrates of varying chain lengths, as described in Assay 1 in the Examples section.

[0032] Snippet: The term "fragment" means a polypeptide that lacks one or more (e.g., several) amino acids at the amino and / or carboxyl terminus of a polypeptide; wherein the fragment has lipase activity. In one aspect, the fragment contains at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90% or at least 95% but less than 100% of the number of amino acids 1 to 269 of SEQ ID NO: 1 or 2.

[0033] Parent or parent lipase: The term "parent" or "parent lipase" means a lipase that is altered to produce an enzyme variant. The 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 a parent lipase shown in SEQ ID NO: 1, 2, 3, 4, 5, 6 or 7.

[0034] Wild-type lipase: The term "wild-type" lipase means a lipase expressed by a naturally occurring microorganism found in nature, such as a bacterium, yeast or filamentous fungus. In an embodiment, the wild-type lipase may be a lipase as shown in SEQ ID NO: 1 (derived from Thermomyces lanuginosus DSM 4109 (synonym: Humicola lanuginosus DSM 4109)) or an Absidia sp. lipase as shown in SEQ ID NO: 3 of WO 2021 / 001400.

[0035] Cleaning ingredients:The term "cleaning components" is defined herein to mean the types of chemicals that can be used in cleaning compositions. Examples of cleaning components are alkalis, surfactants, solvents, hydrotropes, builders, co-builders, chelators or chelating agents, bleach systems or bleach components, polymers, foam boosters, suds suppressors, dispersants, dye transfer inhibitors, perfumes, bactericides, fungicides, corrosion inhibitors, soil suspending agents, soil release polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, preservatives, solvents and solubilizing agents.

[0036] Cleaning composition The term "cleaning composition" (also referred to as "detergent composition") refers to a composition for removing unwanted compounds from items to be cleaned, such as hard surfaces. Cleaning compositions can be used, for example, for household cleaning and industrial cleaning. These terms encompass any substance / compound and product form (e.g., liquid, gel, powder, granular, paste or spray composition) selected for the particular type of cleaning composition desired. In addition to containing the lipase of the present invention, the cleaning composition of the present invention may also 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 components as described above.

[0037] alkyl: The term "alkyl" refers to a straight or branched monovalent hydrocarbon radical having a specified number of carbon atoms. The alkyl group may be unsubstituted or substituted with a substituent that does not interfere with the specific function of the composition, and may be substituted once or twice with the same or different groups. The substituent may include, for example, an alkoxy, hydroxyl, sulfhydryl, amino, alkyl-substituted amino, nitro, carboxyl, carbonyl, carbonyloxy, cyano, methylsulfonylamino, or halogen. Examples of "alkyl" include, but are not limited to, methyl, ethyl, n-propyl, isopropyl, n-butyl, sec-butyl, tert-butyl, n-pentyl, n-hexyl, 3-methylpentyl, etc.

[0038] Sequence identity:The degree of association between two amino acid sequences or between two nucleotide sequences is described by parameter " sequence identity ".For purposes of the present invention, use as in EMBOSS software package (EMBOSS: European Molecular Biology Open Software Suite (The European Molecular Biology Open Software Suite), Rice et al., 2000, Trends Genet. [Genetics Trend] 16: 276-277) (preferred 6.6.0 version or updated version) Ni Deman (Needle) program implemented in Ni Deer (Needle) algorithm (Needleman and Wunsch, 1970, J.Mol.Biol. [Molecular Biology Magazine] 48: 443-453) determine the output of sequence identity between two amino acid sequences as " longest identity ".The parameter used is gap opening penalty 10, gap extension penalty 0.5 and 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 output of the "longest identity" flagged by Needle is calculated as follows:

[0039] (number of identical residues x 100) / (length of alignment - total number of gaps in the alignment)

[0040] Variants: The term "variant" means a polypeptide / enzyme having similar activity to a parent enzyme that comprises a change (i.e., substitution, insertion and / or deletion) at one or more (e.g., several) positions. Substitution means replacing an amino acid occupying a position with a different amino acid; deletion means removing an amino acid occupying a position; and insertion means adding an amino acid adjacent to and immediately following an amino acid occupying a position. In the context of the present invention, the variant of the identified lipase has the enzymatic activity of the parent. In one embodiment, the lipase activity of the variant is increased compared to a parent lipase (e.g., an enzyme comprising or consisting of the amino acid sequence of SEQ ID NO: 1, or an enzyme comprising or consisting of the amino acid sequence shown in SEQ ID NO: 2).

[0041] Hard Surfaces:The term "hard surface" includes household surfaces (e.g., showers, sinks, toilets, bathtubs, countertops, windows, mirrors, floors, etc.) and industrial surfaces (e.g., transportation vehicles, storage tanks, bioreactors, fermenters, mixing vessels, pipes, bottling line equipment, and other equipment used in biotechnology manufacturing (e.g., pharmaceutical manufacturing, food and beverage manufacturing). The term can also include surfaces of medical or dental instruments that come into contact with a patient, where the patient can be a human or an animal. Exemplary hard surfaces can be steel surfaces, rubber surfaces, plastic surfaces, glass surfaces, ceramic surfaces, melamine surfaces, wood surfaces, coated surfaces, cement countertops, kitchen countertops, endoscope surfaces, arthroscopic scalpel surfaces, hemostats, Kocher's clamp surfaces, and tracheostomy knife surfaces, etc.

[0042] Variant naming conventions

[0043] For the purposes of the present invention, the lipase disclosed as SEQ ID NO: 1 is used to determine the corresponding amino acid residue in another lipase. The amino acid sequence of another lipase is aligned with SEQ ID NO: 1, and based on the alignment, the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) implemented in the Needle program of the EMBOSS software package (EMBOSS: European Molecular Biology Open Software Package, Rice et al., 2000, Trends Genet. [Genetics Trends] 16: 276-277) (preferably version 5.0.0 or later) is used to determine the amino acid position number corresponding to any amino acid residue in the polypeptide disclosed in SEQ ID NO: 1. The parameters used are a gap opening penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.

[0044] The identity of the corresponding amino acid residue in another lipase can be determined by aligning multiple polypeptide sequences using several computer programs using their respective default parameters, including but not limited to MUSCLE (Multiple Sequence Comparison by Logarithmic Expectation; Version 3.5 or later; Edgar, 2004, Nucleic Acids Research 32:1792-1797), MAFFT (Version 6.857 or later; Katoh and Kuma, 2002, Nucleic Acids Research 30:3059-3066; Katoh et al., 2005, Nucleic Acids Research 33:511-518; Katoh and Toh, 2007, Bioinformatics 23:372-374; Katoh et al., 2009, Methods in Molecular Biology 23:372-374. Biology [Molecular Biology Methods] 537:39-64; Katoh and Toh, 2010, Bioinformatics [Bioinformatics] 26:1899-1900) and EMBOSS EMMA (version 1.83 or later; Thompson et al., 1994, Nucleic Acids Research [Nucleic Acids Research] 22:4673-4680) using ClustalW.

[0045] When other enzymes diverge from the lipase of SEQ ID NO: 1, so that traditional sequence-based comparison methods cannot detect their relationship (Lindahl and Elofsson, 2000, J. Mol. Biol. [Journal of Molecular Biology] 295: 613-615), other pairwise sequence comparison algorithms can be used. Higher sensitivity in sequence-based searches can be obtained using search programs that use probabilistic representations (profiles) of families of polypeptides to search databases. For example, the PSI-BLAST program generates multiple profiles through an iterative database search process and is capable of detecting distant homologs (Atschul et al., 1997, Nucleic Acids Res. [Nucleic Acids Research] 25: 3389-3402). Even higher sensitivity can be achieved if a family or superfamily of polypeptides has one or more representatives 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) use information from a variety of sources (PSI-BLAST, secondary structure predictions, structural alignment spectra, and solvation potential) as input to a neural network that predicts the structural fold of a query sequence. Similarly, the method of Gough et al., 2000, J. Mol. Biol. 313:903-919 can be used to align sequences of unknown structure with superfamily models present in the SCOP database. These alignments, in turn, can be used to generate homology models for polypeptides, and the accuracy of such models can be assessed using a variety of tools developed for this purpose.

[0046] For proteins of known structure, there are several tools and resources that can be used to retrieve and generate structural alignments. For example, the SCOP superfamily of proteins has been structurally aligned, and those alignments are accessible and downloadable. Multiple algorithms such as distance alignment matrices (Holm and Sander, 1998, Proteins 33:88-96) or combinatorial extensions (Shindyalov and Bourne, 1998, Protein Engineering 11:739-747) can be used to align two or more protein structures, and the implementation of these algorithms can be used in addition to query structural databases with target structures to find possible structural homologues (e.g., Holm and Park, 2000, Bioinformatics 16:566-567).

[0047] In the context of the present invention, when describing variants, the nomenclature described below is used for ease of reference. Accepted IUPAC single-letter or three-letter amino acid abbreviations are used.

[0048] replace :For amino acid substitution, the following nomenclature is used: original amino acid, position, substituted amino acid. Accordingly, the threonine at position 226 is replaced by alanine as "Thr226Ala" or "T226A". Multiple mutations are separated by a plus sign ("+"), for example, "Gly205Arg+Ser411Phe" or "G205R+S411F" represents that the glycine (G) and serine (S) at position 205 and position 411 are replaced by arginine (R) and phenylalanine (F), respectively.

[0049] Missing : For amino acid deletions, the following nomenclature is used: original amino acid, position, * Accordingly, the deletion of the glycine at position 195 is indicated as "Gly195*" or "G195*". Multiple deletions are separated by a plus sign ("+"), for example, "Gly195*+Ser411*" or "G195*+S411*".

[0050] insert : For amino acid insertions, the following nomenclature is used: original amino acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of lysine after glycine at position 195 is represented as "Gly195GlyLys" or "G195GK". Insertions of multiple amino acids are represented as [original amino acid, position, original amino acid, inserted amino acid #1, inserted amino acid #2; etc.]. For example, the insertion of lysine and alanine after glycine at position 195 is represented as "Gly195GlyLysAla" or "G195GKA".

[0051] In such a case, the inserted amino acid residues are numbered by adding lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue. In the above example, the sequence would therefore be:

[0052] Parents: Variants: 195 195195a195b G GKA

[0053] Multiple changes Variants containing multiple alterations are separated by plus signs ("+"), for example, "Arg170Tyr+Gly195Glu" or "R170Y+G195E" represent substitutions of arginine at position 170 and glycine at position 195 by tyrosine and glutamic acid, respectively.

[0054] Different changesWhen different changes can be introduced at one position, these different changes are separated by a comma, for example "Arg170Tyr,Glu" or "R170Y,E" represents that the arginine at position 170 is replaced by tyrosine or glutamic acid. Thus, "Tyr167Gly,Ala+Arg170Gly,Ala" represents the following variants:

[0055] “Tyr167Gly+Arg170Gly”, “Tyr167Gly+Arg170Ala”, “Tyr167Ala+Arg170Gly” and “Tyr167Ala+Arg170Ala”. DETAILED DESCRIPTION

[0056] The present inventors unexpectedly found that adding lipase to a hard surface cleaning composition together with a solvent provides enhanced cleaning effect and improved washing efficiency (especially for oil stain removal or greasy stain removal). Therefore, compared to high pH conventional hard surface cleaning detergents, the cleaning composition of the present invention can not only provide better cleaning effect, but also save time and labor costs. In addition, the pH of the cleaning composition can be reduced from, for example, pH 11 to a milder pH (e.g., below pH 9 or neutral pH) without affecting the cleaning effect / washing performance.

[0057] Cleaning composition of the present invention

[0058] A first aspect of the present invention relates to a hard surface cleaning composition comprising:

[0059] (a) 0.1 to 60 wt % of a surfactant system;

[0060] (b) 0.1 to 40 wt % of a solvent, wherein the solvent is 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and combinations thereof; and optionally

[0061] (c) 0.001 to 10 wt% of lipase.

[0062] The compositions of the present invention can be formulated as ready-to-use detergents or concentrated (e.g., 2X, 5X or 10X concentrated) detergents that can be diluted on-site before application. Enzymes (e.g., lipases) can be added when formulating concentrates or added on-site to diluted versions.

[0063] Composition components

[0064] The non-limiting list of composition components set forth below is applicable to the compositions and methods of the present invention, and may be desirably incorporated into certain embodiments of the present invention, for example, to assist or enhance cleaning performance, to treat hard surfaces to be cleaned, or to modify the aesthetics of these compositions in the context of spices, colorants, dyes, etc. The precise nature of these components, and their level of incorporation will depend on the physical form of the composition and the nature of the cleaning operation in which the composition will be used. Although the components mentioned below are classified under general headings according to specific functionality, this is not to be construed as limiting, since, as will be appreciated by the skilled artisan, the components may contain additional functionality.

[0065] Suitable component materials include, but are not limited to, surfactants, builders, chelating agents, dispersants, enzymes, and enzyme stabilizers, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric dispersants, clay removers, suds suppressors, dyes, perfumes, perfume delivery systems, carriers, hydrotropes, processing aids, and solvents. In addition to the following disclosure, suitable examples of such other components and usage levels are found in US 5576282, US 6306812, and US 6326348, which are hereby incorporated by reference.

[0066] Surfactant or surfactant system

[0067] The detergent or cleaning composition of the present invention comprises a surfactant or a surfactant system, a lipase and a solvent compound. In an embodiment, 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.

[0068] 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%-60%.

[0069] Suitable anionic surfactants include sulfate and sulfonate detersive surfactants.

[0070] Suitable sulfonate surfactants include alkylbenzene sulfonates, in one aspect C 10-13Alkylbenzene sulfonate. Suitable alkylbenzene sulfonate (LAS) can be obtained by sulfonating commercially available linear alkylbenzene (LAB); suitable LABs include low 2-phenyl LABs, such as or Other suitable LABs include high 2-phenyl LABs such as Suitable anionic detersive surfactants are alkylbenzene sulfonates obtained by the DETAL catalyzed process, but other synthetic routes (such as HF) may also be suitable. In one aspect, the magnesium salt of LAS is used.

[0071] Suitable sulfate surfactants include alkyl sulfates, in one aspect C 8-18 Alkyl sulfates, or mainly C 12 Alkyl sulfate.

[0072] Another suitable sulfate surfactant is an alkyl alkoxylated sulfate, in one aspect an alkyl ethoxylated sulfate, in one aspect C 8-18 Alkyl alkoxylated sulfate, in another aspect C 8-18 Alkyl ethoxylated sulfates, typically the alkyl alkoxylated sulfates have an average degree of alkoxylation of 0.5 to 20 or 0.5 to 10, typically the alkyl alkoxylated sulfates are C 20 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 Alkyl ethoxylated sulfate.

[0073] The alkyl sulfates, alkyl alkoxylated sulfates and alkyl benzene sulfonates may be linear or branched, substituted or unsubstituted.

[0074] The surfactant can be a mid-chain branched detersive surfactant, in one aspect a mid-chain branched anionic detersive surfactant, in one aspect a mid-chain branched alkyl sulfate and / or a mid-chain branched alkylbenzene sulfonate, such as a mid-chain branched alkyl sulfate. In one aspect, the mid-chain branch is C 1-4 Alkyl groups are typically methyl and / or ethyl groups.

[0075] Non-limiting examples of anionic surfactants include sulfates and sulfonates, in particular linear alkylbenzene sulfonates (LAS), isomers of LAS, branched alkylbenzene sulfonates (BABS), phenylalkanesulfonates, alpha-olefin sulfonates (AOS), olefin sulfonates, alkene sulfonates, alkane-2,3-diylbis(sulfates), hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS) or sodium lauryl sulfate (SLS), fatty alcohol sulfates (FAS), primary alcohol sulfates (PAS), Alcohol ether sulfates (AES or AEOS or FES, also known as alcohol ethoxy sulfates or fatty alcohol ether sulfates), sodium laureth sulfate (SLES), secondary alkane sulfonates (SAS), paraffin sulfonates (PS), ester sulfonates, sulfonated fatty acid glycerides, α-sulfonic fatty acid methyl esters (α-SFMe or SES) (including methyl sulfonate (MES)), alkyl succinic acid or alkenyl succinic acid, dodecenyl / tetradecenyl succinic acid (DTSA), fatty acid derivatives of amino acids, diesters and monoesters of sulfosuccinic acid or soap, and combinations thereof.

[0076] The anionic surfactant may be 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%, 5 to 15 wt% or 6 to 8 wt%.

[0077] Suitable nonionic surfactants are selected from the group consisting of: C8-C 18 Alkyl ethoxylates, such as C6-C 12 Alkylphenol alkoxylates, wherein the alkoxylate units may be ethyleneoxy units, propyleneoxy units or mixtures thereof; C 12 -C 18 Alcohol and C6-C 12 Condensation products of alkylphenols with ethylene oxide / propylene oxide block polymers, such as C 14 -C 22 Medium chain branched alcohol; C 14 -C 22 Mid-chain branched alkyl alkoxylates, typically having an average degree of alkoxylation of 1 to 30; alkyl polysaccharides, in one aspect alkyl polyglycosides; polyhydroxy fatty acid amides; ether-terminated poly(alkoxylated) alcohol surfactants; and mixtures thereof.

[0078] Suitable nonionic detersive surfactants include alkyl glucosides and / or alkyl alkoxylated alcohols.

[0079] In one aspect, the nonionic detersive surfactant comprises an alkyl alkoxylated alcohol, in one aspect C 8-18Alkyl alkoxylated alcohols, such as C 8-18 The alkyl ethoxylated alcohol may have an average degree of alkoxylation of 1 to 50, 1 to 30, 1 to 20, or 1 to 10. In one aspect, the alkyl alkoxylated alcohol may be C 8-18 Alkyl ethoxylated alcohols having an average degree of ethoxylation of from 1 to 10, 1 to 7, more preferably 1 to 5 or 3 to 7. The alkyl alkoxylated alcohols may be linear or branched, and substituted or unsubstituted. Suitable nonionic surfactants include

[0080] 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 (PFA), alkoxylated fatty acid alkyl esters such as ethoxylated and / or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE), nonylphenol ethoxylates (NPE), alkyl polyglycosides (APG), alkoxylated amines, fatty acid monoethanolamide (FAM), fatty acid diethanolamide (FADA), ethoxylated fatty acid monoethanolamide (EFAM), propoxylated fatty acid monoethanolamide (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamide (GA), or fatty acid glucamide (FAGA)), and products available under the SPAN and TWEEN trade names, and combinations thereof.

[0081] Suitable cationic detersive surfactants include alkyl pyridinium compounds, alkyl quaternary ammonium compounds, alkyl quaternary phosphonium compounds, alkyl trisulfonium compounds and mixtures thereof.

[0082] Suitable cationic detersive surfactants are quaternary ammonium compounds having the general formula: (R)(R1)(R2)(R3)N + X - , wherein R is a linear or branched, substituted or unsubstituted C 6-18 An alkyl or alkenyl moiety, R1 and R2 are independently selected from a methyl or ethyl moiety, R3 is a hydroxyl, hydroxymethyl or hydroxyethyl moiety, and X is an anion providing charge neutrality, suitable anions include: halogen ions, such as chloride ions; sulfate ions; and sulfonate ions. Suitable cationic detersive surfactants are mono-C 6-18 Alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride. Highly suitable cationic detersive surfactants are mono-C 8-10 Alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride, mono-C 10-12 Alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride and mono-C 10 Alkyl mono-hydroxyethyl dimethyl quaternary ammonium chloride.

[0083] Non-limiting examples of cationic surfactants include alkyl dimethylethanol quaternary ammonium (ADMEAQ), cetyl trimethyl ammonium bromide (CTAB), dimethyl distearylammonium chloride (DSDMAC), and alkyl benzyl dimethyl ammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quaternary ammonium, and combinations thereof.

[0084] Suitable amphoteric surfactants / zwitterionic surfactants include amine oxides and betaines (e.g., alkyl dimethyl betaines, sulfobetaines) or combinations thereof. Amine-neutralized anionic surfactants-anionic surfactants and auxiliary anionic co-surfactants can exist in acid form, and the acid form can be neutralized to form surfactant salts that are desired for use in the detergent composition of the present invention. Typical agents for neutralization include metal counterion bases, such as hydroxides, such as NaOH or KOH. Other preferred agents for neutralizing the anionic surfactants of the present invention and auxiliary anionic surfactants or co-surfactants in their acid form include ammonia, amines, or alkanolamines. Alkanolamines are preferred. Suitable non-limiting examples include monoethanolamine, diethanolamine, triethanolamine, and other linear or branched alkanolamines known in the art; for example, highly preferred alkanolamines include 2-amino-1-propanol, 1-aminopropanol, monoisopropanolamine, or 1-amino-3-propanol. Amine neutralization can be performed to a complete or partial extent, for example, part of the anionic surfactant mixture can be neutralized with sodium or potassium, and part of the anionic surfactant mixture can be neutralized with an amine or alkanolamine.

[0085] Non-limiting examples of semi-polar surfactants include amine oxides (AO), such as alkyl dimethyl amine oxides

[0086] 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. The preferred weight ratio of anionic to nonionic surfactants is at least 2:1, or at least 1:1 to 1:10.

[0087] In embodiments, the compositions of the present invention comprise one or more anionic surfactants and / or one or more nonionic surfactants.

[0088] In a preferred embodiment, the composition of the present invention comprises one or more anionic surfactants, preferably from the group of linear alkylbenzene sulfonic acid (LAS), alcohol ether sulfates (AEOS) and / or alkyl sulfates (AS), in particular sodium lauryl sulfate (SLS) and sodium laureth sulfate (SLES).

[0089] In an embodiment, the composition of the present invention comprises one or more nonionic surfactants, preferably alcohol ethoxylates (AEO), especially linear alcohols (C 12-15 ) ethoxylate (LAE).

[0090] In one embodiment, the composition of the present invention comprises an anionic surfactant linear alkylbenzene sulfonic acid (LAS) and a nonionic surfactant alcohol ethoxylate (AEO).

[0091] In one embodiment, the composition of the present invention comprises an anionic surfactant sodium laureth sulfate (SLES) and a nonionic surfactant alcohol ethoxylate (AEO).

[0092] The nonionic surfactant may be 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%.

[0093] In embodiments, the ratio between the anionic surfactant and the nonionic surfactant ranges from 1:10 to 10:1, such as 1:5 to 5:1 or 1:3 to 2:1.

[0094] In certain embodiments, the composition comprises a surfactant system as described in Table 1 below.

[0095] Solvents

[0096] The cleaning compositions of the present invention may include solvents, for example, to improve soil removal performance or to adjust the viscosity of the final composition. Suitable solvents that can be used 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and the like.

[0097] 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 glycol-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 ethyl ethers, 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-ethoxyethanol, 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, ethylene glycol ethers, propylene glycol, or dipropylene glycol.

[0098] Suitable alcohol ethoxylates may be linear (preferably C 4-10 ) alcohol ethoxylate, branched alcohol, oxo alcohol ethoxylate. The ethoxylation number may preferably be 1, 2, 3, 4, 5, 6, 7 or 8. In one embodiment, suitable solvents of the present invention comprise at least one alcohol ethoxylate, such as hexyl ethoxylate (e.g. 2-(hexyloxy)ethanol), 2-ethoxyethanol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, phenoxyethanol, and the like.

[0099] The solvent may be present at a level of 0.1 to 40 wt%, 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%.

[0100] In an embodiment, two or three or more solvents are combined, for example, ethanol and diethylene glycol monobutyl ether, ethanol and diethylene glycol monobutyl ether and propylene glycol, ethanol and propylene glycol, or isopropyl alcohol and dipropylene glycol are combined.

[0101] In one embodiment, the cleaning composition comprises one or more alcohol ethoxylates. For example, the cleaning composition comprises 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-ethoxyethanol, 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.

[0102] 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 (C6EO1), and further comprises one or more ester solvents selected from the group consisting of 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-ethoxyethanol, 2-(2-ethoxyethoxy)ethanol, triethylene glycol monoethyl ether, 2-(hexyloxy)ethanol, 2-(2-hexyloxyethoxy)ethanol, and phenoxyethanol.

[0103] In one embodiment, the cleaning composition comprises two solvents: ethylene glycol monohexyl ether (C6EO1) and dipropylene glycol monobutyl ether (DPGBE). Preferably, the weight ratio of the two solvents ranges from 1:10 to 10:1, for example, ranges from 1:5 to 5:1, 1:2 to 3:1, for example, about 1:1.

[0104] Stabilizer

[0105] Stabilizers that can be used in the cleaning composition include, but are not limited to, aliphatic primary amines, betaines, borates, calcium ions, sodium citrate, citric acid, sodium formate, glycerol, malonic acid, organic diacids, polyols, propylene glycol, and mixtures thereof. Exemplary ranges of stabilizers may include 0-20 wt%, for example, between about 0.5 wt% and about 15 wt% and between about 2 wt% and about 10 wt%. In one embodiment, the stabilizer is sodium citrate or sodium carbonate.

[0106] In embodiments of the cleaning composition, the amount of stabilizer is preferably between about 0.01 wt % and about 5 wt %; more preferably between about 0.05 wt % and about 2.5 wt %; most preferably between about 0.1 wt % and about 1 wt %.

[0107] soap

[0108] The composition of the present invention may also contain soap. Without being limited by theory, it may be desirable to include soap because it acts partly as a surfactant, partly as a builder, and may be used to suppress foam. Any soap known in the art for use in laundry detergents may be utilized. In one embodiment, the composition contains from 0wt% to 20wt%, 0.5wt% to 20wt%, 4wt% to 10wt%, or 4wt% to 7wt% soap.

[0109] Examples of soaps useful herein include oleic acid soaps, palmitic acid soaps, palm kernel fatty acid soaps, and mixtures thereof. Typical soaps are in the form of mixtures of fatty acid soaps having varying chain lengths and degrees of substitution. One such mixture is topped palm kernel fatty acid.

[0110] In a preferred embodiment, the composition comprises cocoa fatty acid.Other suitable fatty acids are saturated and / or unsaturated and can be obtained from natural sources such as plant or animal esters (e.g., palm kernel oil, palm oil, coconut oil, babassu oil, safflower oil, tall oil, castor oil, tallow and fish oils, greases, and mixtures thereof), or synthetically prepared (e.g., via oxidation of petroleum or via hydrogenation of carbon monoxide by the Fischer Tropsch process).

[0111] Water-soluble additives

[0112] The composition of the present invention may also include one or more hydrotropes. Hydrotropes are compounds that dissolve hydrophobic compounds in aqueous solutions (or, conversely, polar substances in non-polar environments). Typically, hydrotropes have both hydrophilic and hydrophobic characteristics (so-called amphiphilic properties, as known from surfactants); however, the molecular structure of hydrotropes is generally not conducive to spontaneous self-aggregation, see, for example, a review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not show a critical concentration, above which self-aggregation as found for surfactants and lipid formation of micelles, lamellae or other well-defined mesophases will occur. On the contrary, many hydrotropes show a continuous type of aggregation process, in which the size of the aggregates grows with increasing concentration. However, many hydrotropes change the phase behavior, stability, and colloidal properties of systems containing substances with polar and non-polar characteristics (including mixtures of water, oil, surfactants, and polymers). The use of hydrotropes in detergent or cleaning compositions allows, for example, more concentrated surfactant formulations to be produced (eg in the process of compacting liquid detergents by removing water) without causing undesirable phenomena such as phase separation or high viscosity.

[0113] The detergent composition of the present invention can contain from 0 to 10 wt%, for example from 0 to 5 wt%, 0.5 to 5 wt%, or from 3 to 5 wt% of a hydrotrope. Any hydrotrope known in the art for use in detergents can be utilized. Non-limiting examples of hydrotropes include sodium benzene sulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyethylene glycol ethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfonate, and combinations thereof.

[0114] Builders and co-builders

[0115] The compositions of the present invention may also include one or more builders, co-builders, builder systems or mixtures thereof. When a builder is used, the cleaning composition will typically include from 0 to 60 wt%, at least 1 wt%, 2 to 60 wt% or 5 to 10 wt% of the builder. In dishwashing cleaning compositions, the level of builder is typically, for example, 5 to 45 wt% or 10 to 35 wt%. The composition may be substantially free of builders; substantially free means "no intentionally added" zeolite and / or phosphate. Typical zeolite builders include zeolite A, zeolite P and zeolite MAP. A typical phosphate builder is sodium tripolyphosphate.

[0116] Builder and / or co-builder can be particularly 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 can be used. The limiting examples of builders include zeolite, 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 from Hoechst), ethanolamines (e.g., 2-aminoethane-1-ol (MEA), iminodiethanol (DEA) and 2,2',2"-nitrilotriethanol (TEA)), and carboxymethyl inulin (CMI), and combinations thereof.

[0117] The composition may include a co-builder alone or in combination with a builder (e.g., a zeolite builder). Non-limiting examples of co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly(acrylic acid) (PAA) or co-(acrylic acid / maleic acid) (PAA / PMA). Further non-limiting examples include citrates, chelating agents (e.g., aminocarboxylates, aminopolycarboxylates, and phosphonates), and alkyl succinic or alkenyl succinic acids. Further specific examples include 2,2',2"-nitrilotriacetic acid (NTA), ethylenediaminetetraacetic acid (EDTA), diethylenetriaminepentaacetic acid (DTPA), iminodisuccinic 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), ethylenediaminetetra(methylene)tetra(phosphonic acid) (EDTMPA), diethylenetriaminepenta(methylene)penta(phosphonic acid) (DTPMPA), N-(2-hydroxyethyl)iminodiacetic acid (EDG), aspartic acid-N-monoacetic acid (ASMA), aspartic acid-N,N-diacetic acid (ASDA), aspartic acid-N-monopropionic acid (ASMP), iminodisuccinic acid (IDA), N-(2-sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SE N-(2-sulfomethyl)glutamic acid (SMGL), N-(2-sulfoethyl)glutamic acid (SEGL), N-methyliminodiacetic acid (MIDA), α-alanine-N,N-diacetic acid (α-ALDA), serine-N,N-diacetic acid (SEDA), isoserine-N,N-diacetic acid (ISDA), phenylalanine-N,N-diacetic acid (PHDA), anthranilic acid-N,N-diacetic acid (ANDA), para-aminobenzenesulfonic acid-N,N-diacetic acid (SLDA), taurine-N,N-diacetic acid (TUDA) and sulfomethyl-N,N-diacetic acid (SMDA), N-(hydroxyethyl)-ethylenediaminetriacetic acid (HEDTA), diethanolglycine (DEG), diethylenetriaminepenta(methylenephosphonic acid) (DTPMP), aminotri(methylenephosphonic acid) (ATMP), and combinations and salts thereof. Additional exemplary builders and / or co-builders are described, for example, in WO 09 / 102854, US 5977053.

[0118] Chelating agents and crystal growth inhibitors

[0119] The compositions of the present invention may also contain chelating agents and / or crystal growth inhibitors. Suitable molecules include copper, iron and / or manganese chelating agents 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, ethylenediamine disuccinic 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 ( Typically, the composition may contain 0.005 to 15 wt % or 3.0 to 10 wt % of a chelating agent or crystal growth inhibitor.

[0120] Bleaching components

[0121] The composition of the present invention may also include a bleaching component. Suitable bleaching components for incorporation into the composition of the present invention or for use in the method of the present invention include one bleaching component or a mixture of more than one bleaching component. Suitable bleaching components include bleaching catalysts, photobleaches, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids and mixtures thereof. Typically, when a bleaching component is used, the composition of the present invention may include 0 to 30 wt%, 0.00001 to 90 wt%, 0.0001 to 50 wt%, 0.001 to 25 wt% or 1 to 20 wt%. Examples of suitable bleaching components include:

[0122] (1) Preformed peracids: Suitable preformed peracids include, but are not limited to, compounds selected from the group consisting of: preformed peroxyacids or salts thereof, typically peroxycarboxylic acids or salts thereof, or peroxysulfuric acid or salts thereof. Preferably, such bleaching components may be present in the composition of the present invention in an amount of 0.01 to 50 wt % or 0.1 to 20 wt %.

[0123] (2) Hydrogen peroxide sources include, for example, inorganic perhydrate salts, including alkali metal salts, such as sodium perborate (usually monohydrate or tetrahydrate), sodium percarbonate, sodium persulfate, sodium perphosphate, sodium persilicate and mixtures thereof. Preferably, such bleaching components may be present in the composition of the present invention in an amount of 0.01 to 50 wt % or 0.1 to 20 wt %.

[0124] (3) The term bleach activator means herein a compound which reacts with hydrogen peroxide to form a peracid via a perhydrolysis reaction. The peracid thus formed constitutes the activated bleach. Suitable bleach activators to be used herein include those belonging to the class of esters, amides, imides or anhydrides. Suitable bleach activators are those having R-(C=O)-L, wherein R is an alkyl group (optionally branched) having from 6 to 14 carbon atoms, or from 8 to 12 carbon atoms when the bleach activator is hydrophobic, and having less than 6 carbon atoms or less than 4 carbon atoms when the bleach activator is hydrophilic; and L is a leaving group. Examples of suitable leaving groups are benzoic acid and its derivatives - especially benzene sulfonates. 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 particularly preferred in that family is acetyl triethyl citrate (ATC). Alternatively, the bleaching system may comprise peroxy acids of the amide, imide or sulfone type, for example. The bleaching system may also comprise a peracid, such as 6-(phthalimido)perhexanoic acid (PAP). Suitable bleach activators are also disclosed in WO 98 / 17767. Although any suitable bleach activator may be employed, in one aspect of the invention, the subject cleaning composition may comprise NOBS, TAED or a mixture thereof. When present, the peracid and / or bleach activator is typically present in the composition in an amount of 0.1 to 60 wt%, 0.5 to 40 wt% or 0.6 to 10 wt% (based on the cleaning composition).

[0125] (4) Diacyl Peroxides (DAP) - Preferred diacyl peroxide bleaching species include those selected from diacyl peroxides having the following general formula: 1 -C(O)-OO-(O)CR 2 , where R 1 Indicates C6-C 18 An alkyl group is preferably a straight chain group having at least 5 carbon atoms and optionally containing one or more substituents (e.g., -N + (CH3)3, -COOH or -CN) and / or one or more interrupting moieties (e.g., -CONH- or -CH=CH-) inserted between adjacent carbon atoms of the alkyl group.12 alkyl group, and R 2 represents an aliphatic group that is compatible with the peroxide portion so that R 1 and R 2 Together, they contain a total of 8 to 30 carbon atoms. In a preferred aspect, R 1 and R 2 It is a straight chain unsubstituted C6-C 12 In one embodiment, the DAP may be asymmetric such that the R1 acyl group preferentially hydrolyzes rapidly to produce the peracid, but the R2 acyl group hydrolyzes slowly.

[0126] The tetraacyl peroxide bleaching species is preferably selected from tetraacyl peroxides having the following general formula: R 3 -C(O)-OO-C(O)-(CH2)nC(O)-OO-C(O)-R 3 , where R 3 represents a C1-C9 alkyl group or a C3-C7 group, and n represents an integer from 2 to 12 or 4 to 10 both inclusive.

[0127] Preferably, the diacyl and / or tetraacyl peroxide bleaching species is present in an amount sufficient to provide at least 0.5 ppm, at least 10 ppm, or at least 50 ppm of washing liquor by weight. In a preferred embodiment, the bleaching species is present in an amount sufficient to provide from 0.5 to 300 ppm, 30 to 150 ppm of washing liquor by weight.

[0128] Preferably, the bleaching component comprises a bleach catalyst. When present, the peracid and / or bleach activator is typically present in the composition in an amount of from 0.1 to 60 wt%, 0.5 to 40 wt% or from 0.6 to 10 wt% (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.

[0129] Exemplary bleaching systems are also described in, for example, WO 2007 / 087258, WO 2007 / 087244, WO 2007 / 087259 and WO 2007 / 087242.

[0130] Defoaming agent

[0131] The cleaning composition may include a defoaming agent to reduce the stability of the foam and reduce foaming. When the composition includes a defoaming agent, the defoaming agent may be provided in an amount between about 0.01 wt % and about 3 wt %.

[0132] Examples of defoaming 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), polydimethylsiloxanes and functionalized polydimethylsiloxanes (such as those available under the name Abil B9952), fatty amides, hydrocarbon waxes, fatty acids, fatty acid esters, fatty alcohols, fatty acid soaps, ethoxylates, mineral oils, polyethylene glycol esters, alkyl phosphates (such as monostearyl phosphate), and the like.

[0133] Lipase

[0134] In addition to surfactant or surfactant system and solvent, the composition of the present invention also comprises lipase. The lipase can be any lipase. In an embodiment, the lipase is of microbial origin. In an embodiment, the lipase is of bacterial origin. In a preferred embodiment, the lipase is of fungal origin, such as derived from filamentous fungi or yeast.

[0135] Examples of lipases include lipases from thermophilic fungi, e.g., from Thermomyces lanuginosus (formerly named Humicola lanuginosus) as described in EP 258068 and EP 305216; cutinases from Humicola, e.g., H. insolens (WO 96 / 13580); a lipase from Absidia reflexa disclosed in US 2009 / 0221033 A1 (SEQ ID NO: 3); lipases from strains of Pseudomonas (some of these are now renamed Burkholderia), e.g., P. alcaligenes or P. pseudoalcaligenes (EP 218272), P. cepacia (EP 218273), P. cepacia (EP 218274), P. cepacia (EP 218275), P. cepacia (EP 218276), P. cepacia (EP 218277), P. cepacia (EP 218278), P. cepacia (EP 218279), P. cepacia (EP 218271), P. cepacia (EP 218273). 331376), Pseudomonas species (P.sp.) strain SD705 (WO 95 / 06720 and WO 96 / 27002), P. wisconsinensis (WO 96 / 12012); GDSL-type Streptomyces lipase (WO 10 / 065455); cutinase from Magnaporthe grisea (WO 10 / 107560); cutinase from Pseudomonas mendocina (US 5,389,536); lipase from Thermobifida fusca (WO 11 / 084412, WO 13 / 033318); Geobacillus stearothermophilus ( stearothermophilus lipase (WO 11 / 084417); a lipase from Bacillus subtilis (WO 11 / 084599); and a lipase from Streptomyces griseus (WO 11 / 150157) and from S. pristinaespiralis (WO 12 / 137147).

[0136] Other examples are lipase variants, such as those described in EP 407225, WO 92 / 05249, WO 94 / 01541, WO 94 / 25578, WO 95 / 14783, WO 95 / 30744, WO 95 / 35381, WO 95 / 22615, WO 96 / 00292, WO 97 / 04079, WO 97 / 07202, WO 00 / 34450, WO 00 / 60063, WO 01 / 92502, WO 07 / 87508 and WO 09 / 109500.

[0137] Still other examples are 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 the Mycobacterium smegmatis perhydrolase, in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO 10 / 100028).

[0138] Preferred commercial lipase products include Lipolase TM 、Lipex TM ;Lipolex TM , Lipoclean TM , LipexEvity 100L, Lipex Evity 105T, Lipex Evity 200L (Novozymes A / S), Lumafast (from Genencor), Preferenz L100 (Danisco USA), and Lipomax (from Gist-Brocades).

[0139] When present in a cleaning composition, the lipase of the present invention may be present at a level of at least 0.0001 mg of enzyme protein, 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 per gram of composition.

[0140] SEQ ID NO:1 lipase - Thermomyces lanuginosus lipase (TLL)

[0141] In a preferred embodiment, the enzyme product of the present invention or the cleaning composition of the present invention comprises a lipase or a variant thereof derived from a strain of Thermomyces spp., in particular Thermomyces lanuginosus (synonym: Humicola lanuginosus). In a specific embodiment, the lipase is a lipase shown in SEQ ID NO: 1 or a variant thereof.

[0142] In an embodiment, the lipase is:

[0143] 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;

[0144] ii) a variant of a parent lipase having lipase activity and 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 with the lipase shown in SEQ ID NO: 1;

[0145] iii) a fragment of the lipase in (i) or (ii) having lipase activity,

[0146] Wherein, the variant comprises substitutions at positions corresponding to T231R+N233R, and at least one or more (e.g., several) of D96E, D111A, D254S, G163K, P256T, G91T, and G38A of SEQ ID NO: 1.

[0147] In a specific embodiment, the lipase used in the composition of the present invention is a variant of a parent lipase, wherein the variant has lipase activity, 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% but less than 100% sequence identity to SEQ ID NO: 1, and comprises a substitution selected from the group consisting of:

[0148] D96E+T231R+N233R;

[0149] N33Q+D96E+T231R+N233R;

[0150] <h2 style=";text-align:left;direction:ltr">N33Q+D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0151] <h2 style=";text-align:left;direction:ltr"> N33Q+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0152] <h2 style=";text-align:left;direction:ltr"> N33Q+G38A+G91T+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0153] <h2 style=";text-align:left;direction:ltr"> N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0154] <h2 style=";text-align:left;direction:ltr"> D27R+N33Q+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0155] <h2 style=";text-align:left;direction:ltr"> D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0156] <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">

[0157] <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">

[0158] <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">

[0159] <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">

[0160] <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">

[0161] <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">

[0162] <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">

[0163] <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">

[0164] <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">

[0165] <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">

[0166] <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">

[0167] <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">

[0168] <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">

[0169] <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">

[0170] <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">

[0171] <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">

[0172] <h2 style=";text-align:left;direction:ltr"> D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0173] <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">

[0174] <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">

[0175] <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">

[0176] <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">

[0177] <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">

[0178] <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">

[0179] <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">

[0180] D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0181] D96E+D111A+G163K+T231R+N233R+P256T;

[0182] D96E+D111A+T231R+N233R;

[0183] D96E+D111A+T231R+N233R+D254S;

[0184] D96E+D111A+T231R+N233R+D254S+P256T

[0185] D96E+D111A+T231R+N233R+P256T;

[0186] D96E+G163K+T231R+N233R+D254S+P256T;

[0187] D96E+T231R+N233R+D254S+P256T;

[0188] D96E+T231R+N233R+P256T;

[0189] G38A+D96E+D111A+T231R+N233R;

[0190] G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0191] G91T+D96E+D111A+T231R+N233R;

[0192] G91T+D96E+T231R+N233R;

[0193] G91T+T231R+N233R+D254S+P256T;

[0194] N33Q+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0195] T231R+N233R+D254S+P256T;

[0196] T231R+N233R+P256T.

[0197] In another embodiment, the lipase is a variant of a parent lipase, wherein the variant

[0198] (a) comprises 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 comprises 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;

[0199] (b) having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity to SEQ ID NO: 1;

[0200] (c) having lipase activity.

[0201] In an embodiment, the lipase is a variant of a parent lipase, wherein the parent lipase is selected from the group consisting of:

[0202] 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;

[0203] b) A fragment of the polypeptide of SEQ ID NO:1.

[0204] In an embodiment, the lipase is a variant having lipase activity and having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95% identity, at least 96%, at least 97%, at least 98%, or at least 99% but less than 100% sequence identity to SEQ ID NO: 1.

[0205] In an embodiment, the lipase variant comprises a modification in at least one of the following positions corresponding to: E1, V2, D27, N33, G38, F51, E56, L69, D96, K98, D111, G163, V176, H198, E210, Y220, L227, T231, N233, K237, D254 and P256, wherein the numbering is according to SEQ ID NO:1. More preferably, the lipase variant comprises at least one of the following modifications corresponding to E1C, V2Y, D27R, N33K, N33Q, G38A, F51V, E56K, L69R, D96E, D96L, K98I, K98Q, D111A, G163K, V176L, H198S, E210K, Y220F, L227G, T231R, N233R, N233C, K237C, D254S and P256T, wherein the numbering is according to SEQ ID NO: 1.

[0206] In an embodiment, the lipase variant further comprises one substitution selected from the group consisting of S54T, S83T, G91A, A150G, I255A and E239C.

[0207] In a preferred embodiment, the lipase variant comprises substitutions corresponding to E1C+N233C in SEQ ID NO: 1 and optionally one or more further substitutions.

[0208] In specific embodiments, the variant has lipase activity, has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99% but less than 100% sequence identity to SEQ ID NO: 1, and comprises or consists of a substitution corresponding to one of the following substitution groups numbered using SEQ ID NO: 1:

[0209]

[0210]

[0211]

[0212]

[0213] SEQ ID NO:2 lipase

[0214] In a preferred embodiment, the cleaning composition of the present invention comprises the lipase represented by SEQ ID NO: 2 or a variant thereof.

[0215] In an embodiment, the lipase is:

[0216] 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;

[0217] ii) a variant of a parent lipase having lipase activity and 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 with the lipase shown in SEQ ID NO: 2;

[0218] iii) a fragment of the lipase in (i) or (ii) having lipase activity,

[0219] This variant includes:

[0220] (a) corresponds to the following substitution:

[0221] 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,E 56N; N57Q; G59S; V60S,M, D62Q; D70Q; N71Q; N73S; I86F,P; N88D,Q; I90R; L93F; N94Q,R,S; D96H,I,Q,S; V98I; 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

[0222] (b) corresponds to the following substitution:

[0223] A4E+F211V; A4E+L227G; A4E+T252A; D122N+L124S; D165N+D167S; D96N+V98S; E45N+A47S; E87K+F 95Y; E87R+N94D; F211V+L227G; F211V+L264A; F211V+T252A; I238C+G246C; L227A+L264A; L227G+I 269W; 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

[0224] (c) corresponds to the following substitution:

[0225] <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+L264A; 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; 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;

[0226] (d) corresponding to the following substitutions:

[0227] 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+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; N39D+V60M+L227G+P256T; N73G+T252A+L264A; and / or

[0228] (e) corresponding to the following substitutions:

[0229] 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

[0230] (f) corresponding to the following substitutions:

[0231] L7F+T91A+A150G+L154V+T252A+L264A; and / or

[0232] (g) corresponding to the following substitutions:

[0233] D1C+V202C+R233C+I238C+G245C+T252A+P253C+L264A; and / or

[0234] A4R+I90V+N94E+D96L+N101P+R233N+T252A+L264A

[0235] These counterparts are those of the polypeptide shown as SEQ ID NO:2.

[0236] In an embodiment, the lipase variant further comprises one or more substitutions corresponding to:

[0237] A4E; A20T; P29S; A46Q; S58N; T91A; N92D; L93F,I; S105D,E,N; R179G,Q; N2 00R; Y220F; L227G; R231K; T244E; Q249E; T252A,S,V; N25S; A38T; R84S; N9 4D; V98Q; N101K; D130H; D137G; R232K; T244A,N,K; A249G,R; N250P; T252I ;D254S; P256T; A257I; L264A; N94V; F95V; L97S; N101E; S105K; D129G; A13 4S; 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, the corresponding items are SEQ ID NO: 2 or using SEQ ID NO: 2 for numbering.

[0238] In an embodiment, the lipase variant comprises two substitutions corresponding to:

[0239] A20T+L93F; A4E+A46Q; F51I+T244E; L227G+R233N; L227G+T244E; L227G+T25 2A; L93I+V98I; N101D+S105D; Q210E+Q249E; R179Q+G212E; R231K+R233K; R2 33N+T252A; S105D+G212E; S105E+R108Q; S105N+G212D; S105N+G212E; S58N+V60S; T244E+T252A; T252A+I255A; T252S+I255A; and / or T91A+V98I, which correspond to those in SEQ ID NO:2 or are numbered using SEQ ID NO:2.

[0240] In an embodiment, the lipase comprises a substitution corresponding to:

[0241] A4R+R233N; K223Q+R232Q; Q210E+N250D; R108Q+G212E; R24Q+N250D; and / or R24Q+Q210E; these correspondences are in SEQ ID NO:2 or are numbered using SEQ ID NO:2.

[0242] In an embodiment, the lipase variant comprises a substitution corresponding to:

[0243] A38T+D96H+D137G; A4R+T252A+L264A; D1G+T252A+L264A; D62N+T252A+L264A; D165Q+N2 50P+T252I; 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, which correspond to those in SEQ ID NO:2 or are numbered using SEQ ID NO:2.

[0244] In an embodiment, the lipase variant comprises a substitution corresponding to:

[0245] A4R+R233N+T252A+L264A; A4R+V60M+L227G+R231T; A4R+V60M+L227G+R232V; A4R+V60M+L227G+R2 33N; E87Q+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, these corresponding items are in SEQ ID NO:2 or are numbered using SEQ ID NO:2.

[0246] In an embodiment, the lipase variant comprises a substitution corresponding to:

[0247] 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, and these corresponding items are in SEQ ID NO:2 or are numbered using SEQ ID NO:2.

[0248] In an embodiment, the lipase variant comprises a substitution corresponding to:

[0249] 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, these corresponding items are in SEQ ID NO:2 or are numbered using SEQ ID NO:2.

[0250] In an embodiment, the lipase variant comprises a substitution corresponding to:

[0251] V60K+S83T+T91A+H198I+V228L+T252A+L264P; or V60M+A157V+Q210E+L227V+V228A+T252A+L264V, which correspond to SEQ ID NO: 2 or are numbered using SEQ ID NO: 2.

[0252] In an embodiment, the lipase variant comprises a substitution corresponding to:

[0253] D1E+A4Q+L7F+K11N+S37T+A46K+A133R+V142F+T170S+V202I+Q210E+L227G.

[0254] In certain preferred embodiments, the lipase has one of the following substitution groups corresponding to the following (using SEQ ID NO: 2 for numbering):

[0255]

[0256]

[0257]

[0258]

[0259]

[0260]

[0261] Other lipases

[0262] Other lipases contemplated according to the present invention are those disclosed in WO 2019 / 038164, WO 2019 / 121585, WO 2019 / 138121, WO 2019 / 155789, WO 2019 / 155790, WO 2019 / 185519, WO 2019 / 185610, WO 2019 / 185612, WO 2019 / 201636, WO 2019 / 206994, WO 2019 / 215078, WO 2019 / 219903, WO 2019 / 243312, and the Absidia sp. lipase and variants thereof disclosed in WO 2021 / 001400 (all of which are hereby incorporated by reference).

[0263] Suitable lipases may include lipases derived from Geotrichum candidum (also known as GCL I). Exemplary GCL I may be those selected from SEQ ID NO:3, SEQ ID NO:4, SEQ ID NO:5, SEQ ID NO:6, or SEQ ID NO:7.

[0264] In embodiments, GCL I comprises the amino acid sequence of SEQ ID NO: 3, or comprises an amino acid sequence having at least 60%, such as 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, these polypeptides differ 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.

[0265] In an embodiment, the GCL I of SEQ ID NO: 3 comprises substitutions, deletions and / or insertions at one or more (e.g., several) positions. The amino acid changes may be of a minor nature, i.e., conservative amino acid substitutions or insertions that do not significantly affect the folding and / or activity of the protein; typically small deletions of 1-30 amino acids; small amino-terminal 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 changing the net charge or another function (e.g., a polyhistidine stretch, an antigenic epitope, or a binding domain).

[0266] Other enzymes

[0267] In addition to lipase, the composition of the present invention may also include one or more additional enzymes that provide cleaning performance. Examples of suitable enzymes include, but are not limited to, proteases, cellulases, amylases, pectinases, mannanases, pectin lyases, phosphodiesterases (PDE), deoxyribonucleases (DNases), hexosaminidase, hemicelluloses, or mixtures thereof. A typical combination is an enzyme mixture that may include, for example, proteases and lipases together with alpha-amylases, phospholipases, cutinases, pectinases, mannanases, pectin lyases, phosphodiesterases (PDE), deoxyribonucleases (DNases), xanthanases, dispersoids, or mixtures thereof.

[0268] When present in the cleaning composition, the above additional enzymes may be present at a level of at least 0.0001 mg of enzyme protein, 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 per gram of composition.

[0269] Generally, the properties of the selected enzyme (ie, pH optimum, compatibility with other enzyme ingredients or non-enzyme ingredients, etc.) should be compatible with the selected detergent or cleaning composition, and the enzyme should be present in an effective amount.

[0270] Protease: In one aspect, suitable proteases can be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants. Proteases can be alkaline proteases, such as serine proteases or metalloproteases. Serine proteases can be, for example, S1 family (such as trypsin) or S8 family (such as subtilisin). Metalloproteases can be, for example, thermolysin, such as thermolysin from M4 family, or another metalloprotease, such as those from M5, M7 or M8 family.

[0271] The term "subtilase" refers to a subgroup of serine proteases according to Siezen et al., Protein Eng. [Protein Engineering] 4 (1991) 719-737 and Siezen et al., Protein Sci. [Protein Science] 6 (1997) 501-523. Serine proteases are a subgroup of proteases characterized by having a serine in the active site that forms a covalent adduct with the substrate. Subtilases can be divided into six subclasses: the subtilisin family, the thermophilic protease family, the proteinase K family, the lanthionine antibiotic peptidase family, the Kexin family, and the Pyrolysin family.

[0272] Although proteases suitable for detergent use can be obtained from a variety of organisms, including fungi such as Aspergillus, detergent proteases have generally been obtained from bacteria, particularly from 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. Particular subtilisins include subtilisinlentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN', subtilisin 309, subtilisin 147, and subtilisin 168, and, for example, protease PD138 (described in WO93 / 18140). Other useful proteases are those described, for example, in WO 01 / 16285 and WO 02 / 16547.

[0273] Examples of trypsin-like proteases include the Fusarium protease (described in WO 94 / 25583 and WO 2005 / 040372), and the chymotrypsin derived from Cellumonas (described in WO 2005 / 052161 and WO 2005 / 052146).

[0274] Examples of metalloproteases include neutral metalloproteases described in WO 2007 / 044993 (such as those derived from Bacillus amyloliquefaciens), and metalloproteases described, for example, in WO 2015 / 158723 and WO 2016 / 075078.

[0275] Examples of useful proteases are the protease variants 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 2004 / 003186, WO 2004 / 041979, WO 2007 / 006305, WO 2011 / 036263, WO 2014 / 207227, WO 2016 / 087617 and WO 2016 / 174234. Preferred protease variants may, for example, comprise one or more mutations selected from the group consisting of 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, H118 N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y1 61A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V193M, N198D, V 199I, Q200L, Y203W, S206G, L211Q, L211D, N212D, N212S, M216S, A226V, K229L, Q230H, Q239R, N246K, S253D, N255W, N255D, N255E, L256E, L256D T268A and R269H, wherein the position numbers correspond to the positions of the Bacillus lentus protease shown in SEQ ID NO: 1 of WO 2016 / 001449. The protease variant having one or more of these mutations is preferably the Bacillus lentus protease shown in SEQ ID NO: 1 of WO 2016 / 001449 ( Also referred to as a variant of subtilisin 309) or a variant of Bacillus amyloliquefaciens protease (BPN') shown in SEQ ID NO: 2 of WO 2016 / 001449. Such a protease variant preferably has at least 80% sequence identity with SEQ ID NO: 1 or SEQ ID NO: 2 of WO 2016 / 001449.

[0276] Another protease of interest is the alkaline protease from Bacillus lentus DSM 5483 (as described, for example, in WO 91 / 02792) and variants thereof (these variants are described, for example, in WO 92 / 21760, WO 95 / 23221, EP 1921147, EP1921148 and WO 2016 / 096711).

[0277] 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 a substitution 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 with SEQ ID NO: 1 of WO 2004 / 067737. TY145 variants of interest are described in, for example, WO 2015 / 014790, WO 2015 / 014803, WO 2015 / 014804, WO 2016 / 097350, WO 2016 / 097352, WO 2016 / 097357 and WO 2016 / 097354.

[0278] Suitable commercially available proteases may include those sold under the following trade names: Duralase TM 、Durazym TM , Ultra, Ultra、Primase TM , Ultra, Ultra, Pro, Blaze 100T, Blaze 125T、Blaze 150T, Blaze 200T, Uno, In and Excel (Novozymes), those sold under the following trade names: Maxatase TM Maxacal TM , Ox, OxP, FN2 TM、FN3 TM 、FN4 exTM , Excellenz TM P1000、Excellenz TM P1250、Eraser TM , P100, P300, Purafect Prime, Preferenz P110 TM 、Effectenz P1000 TM , Effectenz P1050 TM , Ox, Effectenz TM P2000, Purafast TM , Opticlean TM and (Densnick / DuPont), BLAP (sequence shown in Figure 29 of US 5352604) and its variants (Henkel AG), and KAP (alkalophilic Bacillus subtilisin) from Kao Corporation (Kao).

[0279] Amylase: In one aspect, suitable amylases may be alpha-amylases or glucoamylases and may be of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, such as a particular strain of Bacillus licheniformis (described in more detail in GB 1,296,839).

[0280] Suitable amylases include those having SEQ ID NO: 2 in WO 95 / 10603 or variants thereof having 90% sequence identity to SEQ ID NO: 3. Preferred variants are described in WO 94 / 02597, WO 94 / 18314, WO 97 / 43424 and in SEQ ID NO: 4 of WO 99 / 019467, such as variants having substitutions in 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.

[0281] Various suitable amylases include those having SEQ ID NO: 6 in WO 02 / 010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having deletions at positions 181 and 182 and a substitution at position 193.

[0282] Other suitable amylases are hybrid alpha-amylases comprising residues 1-33 of an alpha-amylase derived from Bacillus amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of a Bacillus licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006 / 066594, or variants thereof having 90% sequence identity. Preferred variants of this hybrid alpha-amylase are those having a substitution, deletion or insertion at one or more of the following positions: G48, T49, G107, H156, A181, N190, M197, 1201, A209, and Q264. The most preferred variant of the hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from Bacillus amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006 / 066594 and residues 36-483 of SEQ ID NO: 4 is a variant having the following substitutions:

[0283] M197T;

[0284] H156Y+A181T+N190F+A209V+Q264S; or

[0285] G48A+T49I+G107A+H156Y+A181T+N190F+I201F+A209V+Q264S.

[0286] Another suitable amylase is an amylase having SEQ ID NO: 6 in WO 99 / 019467 or a variant thereof having 90% sequence identity with SEQ ID NO: 6. Preferred variants of SEQ ID NO: 6 are those having 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 in positions R181 and G182, or positions H183 and G184.

[0287] Additional amylases that can be used are those having SEQ ID NO: 1, SEQ ID NO: 3, SEQ ID NO: 2 or SEQ ID NO: 7 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 are those having substitutions, deletions or insertions at one or more of the following positions: 140, 181, 182, 183, 184, 195, 206, 212, 243, 260, 269, 304, and 476, using SEQ ID 2 of WO 96 / 023873 for numbering. More preferred variants are those with deletions in two positions selected from 181, 182, 183, and 184, such as 181 and 182, 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 are those with deletions in positions 183 and 184 and substitutions at one or more of positions 140, 195, 206, 243, 260, 304, and 476.

[0288] Other amylases that can be used are those having SEQ ID NO: 2 of WO 08 / 153815, SEQ ID NO: 10 in WO 01 / 66712, or a variant thereof having 90% sequence identity to SEQ ID NO: 2 of WO 08 / 153815, or a variant thereof having 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 having substitutions, deletions or insertions at one or more of the following positions: 176, 177, 178, 179, 190, 201, 207, 211, and 264.

[0289] Additional suitable amylases are those having SEQ ID NO: 2 of WO 09 / 061380, or variants thereof having 90% sequence identity to SEQ ID NO: 2. Preferred variants of SEQ ID NO: 2 are those having 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 are those with 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 those with deletions in positions R180 and / or S181 or T182 and / or G183. The most preferred amylase variants of SEQ ID NO: 2 are those with the following substitutions:

[0290] N128C+K178L+T182G+Y305R+G475K;

[0291] N128C+K178L+T182G+F202Y+Y305R+D319T+G475K;

[0292] S125A+N128C+K178L+T182G+Y305R+G475K; or

[0293] S125A+N128C+T131I+T165I+K178L+T182G+Y305R+G475K, wherein these variants are C-terminally truncated and optionally further comprise a substitution at position 243 and / or a deletion at position 180 and / or position 181.

[0294] Another suitable amylase is an amylase having SEQ ID NO: 1 of WO13184577, or a variant thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 are those having a substitution, deletion or insertion 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 are those with substitutions at one or more of the following positions: K176L, E187P, N192FYH, M199L, I203YF, S241QADN, R458N, T459S, D460T, G476K, and G477K, and / or those with deletions in positions R178 and / or S179 or T180 and / or G181. The most preferred amylase variants of SEQ ID NO: 1 are those with the following substitutions:

[0295] E187P+I203Y+G476K

[0296] E187P+I203Y+R458N+T459S+D460T+G476K

[0297] Wherein these variants optionally further comprise a substitution at position 241 and / or a deletion at position 178 and / or position 179.

[0298] Another suitable amylase is an amylase having SEQ ID NO: 1 of WO 10104675 or a variant thereof having 90% sequence identity to SEQ ID NO: 1. Preferred variants of SEQ ID NO: 1 are 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 are those having substitutions at one or more of the following positions: N21D, D97N, V128I, K177L, M200L, L204YF, E242QA, G477K, and G478K, and / or those having deletions in positions R179 and / or S180 or I181 and / or G182. The most preferred amylase variants of SEQ ID NO: 1 are those having the following substitutions:

[0299] N21D+D97N+V128I

[0300] Wherein the variants optionally further comprise a substitution at position 200 and / or a deletion at position 180 and / or position 181.

[0301] Other suitable amylases are alpha-amylases having SEQ ID NO: 12 in WO01 / 66712 or variants having at least 90% sequence identity to SEQ ID NO: 12. Preferred amylase variants are those having substitutions, deletions or insertions at one or more of the following positions of SEQ ID NO: 12 in WO01 / 66712: R28, R118, N174; R181, G182, D183, G184, G186, W189, N195, M202, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, N484. Particularly preferred amylases include variants having deletions of D183 and G184 and having substitutions R118K, N195F, R320K, and R458K, and variants additionally having substitutions at one or more positions selected from the group consisting of: M9, G149, G182, G186, M202, T257, Y295, N299, M323, E345, and A339, most preferably variants additionally having substitutions at all of these positions.

[0302] Other examples are amylase variants such as those described in WO 2011 / 098531, WO 2013 / 001078 and WO 2013 / 001087.

[0303] Commercially available amylase is Duramyl TM Termamyl TM 、Fungamyl TM 、Stainzyme TM 、StainzymePlus TM 、Natalase TM , Liquozyme X and BAN TM (from Novozymes), and Rapidase TM 、Purastar TM / Effect TM , Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International / DuPont).

[0304] Cellulase:In one aspect, suitable cellulases include single components and mixtures of enzymes of bacterial or fungal origin. Chemically modified mutants or protein engineered mutants are also contemplated. The cellulases can be, for example, single component endo-1,4-β-glucanase (also known as endoglucanase) or a mixture of single component endo-1,4-β-glucanase.

[0305] Suitable cellulases include those from Bacillus, Pseudomonas, Humicola, Myceliophthora, Fusarium, Thielavia, Trichoderma, and Acremonium. Exemplary cellulases include fungal cellulases from Humicola insolens (US 4,435,307) or from Trichoderma, such as T. reesei or T. viride. Other suitable cellulases are from Thielavia, e.g., Thielavia terrestris described in WO 96 / 29397 or fungal cellulases produced by Myceliophthora thermophila and Fusarium oxysporum as disclosed in US 5,648,263, US 5,691,178, US 5,776,757, WO 89 / 09259, and WO 91 / 17244. Cellulases from Bacillus are also relevant as described in WO 02 / 099091 and JP 2000210081. Suitable cellulases are alkaline or neutral cellulases having care benefits. Examples of cellulases are described in EP 0 495 257, EP 0 531 372, WO 96 / 11262, WO 96 / 29397, WO 98 / 08940. Other examples are cellulase variants as described in WO 94 / 07998, EP 0 531 315, US 5,457,046, US 5,686,593, US 5,763,254, WO 95 / 24471, WO 98 / 12307.

[0306] Other cellulases are endo-β-1,4-glucanases having a sequence that is at least 97% identical to the amino acid sequence from position 1 to position 773 of SEQ ID NO: 2 of WO 2002 / 099091; or Family 44 xyloglucanases having a sequence that is at least 60% identical to positions 40-559 of SEQ ID NO: 2 of WO 2001 / 062903.

[0307] Commercially available cellulases include Premium, Classic, (Novozymes), Puradax HA, and Puradax EG (available from Genencor International), and KAC-500 (B) TM (Kao Corporation).

[0308] Mannanase: In one aspect, suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included. The mannanase may be an alkaline mannanase of family 5 or 26. It may be a wild type from Bacillus or Humicola, in particular from B. agaradhaerens, B. licheniformis, B. alkaliphilic, B. clausii or Humicola insolens. Suitable mannanases are described in WO 1999 / 064619. Commercially available mannanases are Mannaway (Novozymes) and (Danisco / DuPont).

[0309] Pectate lyase, DNase and / or PDE The compositions of the present invention may additionally contain other preferred enzymes, including pectin lyases, e.g. or Pectin lyase is sold under the trade name Pectinase. Finally, the composition may also comprise a deoxyribonuclease (DNase) and / or a phosphodiesterase (PDE).

[0310] In one embodiment, in addition to the lipase of the present invention, the cleaning composition further comprises an amylase, such as BAN TM (From Novozymes).

[0311] In one embodiment, the cleaning composition further comprises a protease, a dispersant and / or a DNase in addition to the lipase of the present invention.

[0312] In one embodiment, the cleaning composition further comprises a protease and a cellulase in addition to the lipase of the present invention.

[0313] In one embodiment, the cleaning composition further comprises, in addition to the lipase of the present invention, a protease, an amylase and a cellulase.

[0314] polymer

[0315] The cleaning composition may contain 0.005%-10%, such as 0.5%-5%, 2%-5%, 0.5%-2% or 0.2%-1% polymer by weight. Any polymer known in the art for use in detergents may be utilized. The polymer may function as a co-builder as mentioned above, or may provide anti-redeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning, and / or defoaming properties. Some polymers may have more than one of the above-mentioned properties. Exemplary polymers include (carboxymethyl)cellulose (CMC), poly(vinyl alcohol) (PVA), poly(ethylene glycol dimethacrylate) or poly(ethylene oxide) (PEG or PEO), ethoxylated poly(ethyleneimine), (carboxymethyl)inulin (CMI), carboxylate polymers and d, and lauryl methacrylate / acrylic acid copolymers, hydrophobically modified CMC (HM-CMC), silicones, co-carboxylates such as polyacrylates, maleic acid / acrylic acid copolymers, acrylate / styrene copolymers, poly(aspartic) acid polymers of terephthalic acid and oligoethylene glycols, copolymers of poly(ethylene terephthalate) and poly(oxyethylene 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 from Ashland Aqualon, and ChromaBond S-200 from BASF. HP 165, HP 50 (dispersant), HP 53 (dispersant), HP 59 (dispersant), HP 56 (dye transfer inhibitor), HP 66K (dye transfer inhibitor). Additional exemplary polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO), and diquaternary ammonium ethoxysulfates. A particularly preferred polymer is the ethoxylated homopolymer of BASF HP 20, which helps prevent soil redeposition in the wash liquor. Additional exemplary polymers include sulfonated polycarboxylates, ethylene oxide-propylene oxide copolymers (PEO-PPO), copolymers of PEG and vinyl acetate, and diquaternary ammonium ethoxysulfate or quaternary ammonium sulfate ethoxylated hexamethylenediamine. Other exemplary polymers are disclosed, for example, in WO 2006 / 130575. Salts of the above-mentioned polymers are also contemplated.

[0316] Supplementary Materials

[0317] Any detergent auxiliary component known in the art can also be used. Exemplary auxiliary materials may include anticorrosives, shrink-proofing agents, antifouling redeposition agents, wrinkle-resistant agents, bactericides, adhesives, corrosion inhibitors, disintegrants (disintegrant / disintegration agents), dyes, enzyme stabilizers (including boric acid, borates, CMC, and / or polyols such as propylene glycol), foam enhancers, foam (foam) regulators, spices, dirt suspending agents, softeners, foam suppressants, dark inhibitors and wicking agents used alone or in combination. The selection of such ingredients is fully within the technical scope of the technician. Cleaning compositions of the present invention may also include corrosion inhibitors (or "rust inhibitors") to prevent hard surfaces from rusting or corroding after washing or cleaning.

[0318] Soil Release Polymers

[0319] The cleaning composition of the present invention may also include one or more soil release polymers that help remove soil from the surface to be cleaned. Soil release polymers may be, for example, polymers based on nonionic or anionic terephthalic acid, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides, see, for example, Powdered Detergents, Surfactant science series, Vol. 71, Chapter 7 of Marcel Dekker, Inc. Another type of soil release polymer is an amphiphilic alkoxylated grease cleaning polymer comprising a core structure and a plurality of alkoxylated groups attached to the core structure. The core structure may include a polyalkylimine structure or a polyalkanolamine structure, as described in detail in WO 2009 / 087523 (incorporated hereby by reference). In addition, 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, especially substituted cellulose structures, such as modified cellulose derivatives, such as those described in EP 1867808 or WO 2003 / 040279 (both of which are hereby incorporated 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, zwitterionic modified cellulose, and mixtures thereof. Suitable cellulosic polymers include methylcellulose, carboxymethylcellulose, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, ester carboxymethylcellulose, and mixtures thereof.

[0320] Probiotics

[0321] These compositions may include prebiotics (e.g. probiotic spores) such as those described in WO 09 / 043709. Commercially available probiotics include and Deep Clean Multi 5X (available from Novozymes).

[0322] Formulation of cleaning composition products

[0323] 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 multiple compartment unit dosage form, or spray form.

[0324] The bag can be configured as a single chamber or multiple chambers. They can have any form, shape and material suitable for holding the composition, such as not allowing the composition to be released from the bag before contact with water. The bag is made of a water-soluble film, which includes an internal volume. The internal volume can be divided into the chambers of the bag. The preferred film is a polymer material, preferably a polymer forming a film or sheet. Preferred polymers, copolymers or derivatives thereof are selected polyacrylates and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylate, most preferably polyvinyl alcohol copolymers and hydroxypropylmethylcellulose (HPMC). Preferably, the level of polymer in the film, such as PVA, is at least about 60%. The preferred average molecular weight will typically be about 20,000 to about 150,000. The film may also be a blended composition comprising a hydrolytically degradable and water soluble polymer blend such as polylactic acid and polyvinyl alcohol (known under trade reference M8630, as sold by MonoSol LLC, Indiana, USA) plus a plasticizer like glycerol, ethylene glycol, propylene glycol, sorbitol and mixtures thereof. The pouch may contain a solid cleaning composition or partial components and / or a liquid cleaning composition or partial components separated by a water soluble film.

[0325] The detergent ingredients or cleaning components may be physically separated from each other by compartments in water-soluble bags or in different layers of a tablet. Thus, undesirable storage interactions between the components may be avoided.

[0326] Non-unit dose liquid or gel detergents can be aqueous, typically containing at least 20% and up to 95% water by weight, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water. Other types of liquids including but not limited to alkanols, amines, glycols, ethers, and polyols can be included in the aqueous liquid or gel. The aqueous liquid or gel detergent can contain 0%-30% organic solvents. The liquid or gel detergent can be non-aqueous.

[0327] The composition of the present invention may be formulated as a hand dishwashing detergent, a professional cleaning detergent, a clean-in-place (CIP) detergent or a hard surface cleaner.

[0328] When formulated as a liquid or spray type or paste form, the cleaning composition of the present invention preferably has a pH below 11, for example in the range of 6-9.5, in the range of 6.5-9, in the range of 6.8-8.5, in the range of 7-8, more preferably has a neutral pH of 6.5-7.5, such as pH 7.0, 7.1 or 7.3.

[0329] When formulated as a solid type, such as a tablet, the cleaning composition of the present invention is preferably dissolved in water to form a washing liquid, which is then applied to the hard surface to be cleaned. Such a washing liquid preferably has a pH below 11, such as in the range of 6-9.5, in the range of 6.5-9, in the range of 6.8-8.5, in the range of 7-8, and more preferably in the range of pH 6.5-7.5, such as pH 7.0, 7.1 or 7.3.

[0330] Formulation of enzymes in co-granules

[0331] Enzyme of the present invention can be formulated as granules, for example, as co-granules combining one or more enzymes. Then, each enzyme will be present in a variety of granules, which ensure that the enzyme is more evenly distributed in the detergent. This also reduces the physical isolation of different enzymes caused by different particle sizes. The method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com disclosure IPCOM000200739D.

[0332] Another example of a formulation of enzymes by 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 wt% of zeolite (on anhydrous basis); and (c) less than 10 wt% of phosphate (on anhydrous basis), wherein the enzyme co-granule comprises from 10 to 98 wt% of a water sink component, and the composition further comprises from 20 to 80 wt% of a detergent water sink component. WO 2013 / 188331 also relates to a method for treating and / or cleaning a surface, the method comprising the steps of: (i) contacting the surface in an aqueous washing liquor with a cleaning composition as claimed and described herein, (ii) rinsing and / or drying the surface.

[0333] The multi-enzyme co-granule may comprise an enzyme of the invention and (a) one or more enzymes selected from the group consisting of proteases, cellulases, amylases, pectinases, mannanases, pectin lyases, phosphodiesterases (PDEs), deoxyribonucleases (DNases), hexosaminidase, hemicelluloses, and mixtures thereof.

[0334] In some embodiments, the hard surface cleaning composition may include the components shown in Table 1 below.

[0335] Table 1. Components of exemplary cleaning compositions of the present invention

[0336]

[0337] The invention is further summarized in the following paragraphs:

[0338] 1. A hard surface cleaning composition, comprising:

[0339] (a) 0.1 to 60 wt % of a surfactant system;

[0340] (b) 0.1 to 40 wt % of a solvent, wherein the solvent is 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and combinations thereof; and optionally

[0341] (c) 0.001 to 10 wt% of lipase.

[0342] 2. The composition of paragraph 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.

[0343] 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.

[0344] 4. A composition as described in any of paragraphs 1-3, wherein the surfactant system comprises one or more anionic surfactants, preferably linear alkylbenzene sulfonic acid (LAS), alcohol ether sulfate (AEOS) and / or alkyl sulfate (AS), especially sodium lauryl sulfate (SLS).

[0345] 5. A composition as described in any of paragraphs 1 to 4, wherein the surfactant system comprises one or more nonionic surfactants, preferably alcohol ethoxylates (AEO), especially linear alcohols (C 12-15 ) ethoxylate.

[0346] 6. The composition of any of paragraphs 1-5, wherein the anionic surfactant is present at a level of 0 to 20 wt%, 0.5 to 15 wt%, 2 to 15 wt%, 3 to 12 wt%, 4 to 10 wt%, or 1 to 5 wt%.

[0347] 7. The composition of any of paragraphs 1-6, wherein the composition comprises an anionic surfactant linear alkylbenzene sulfonic acid (LAS) and a nonionic surfactant alcohol ethoxylate (AEO).

[0348] 8. A composition as described in any of the preceding paragraphs, wherein the nonionic surfactant is present at a level of 0.2 to 30wt%, 0.5 to 25wt%, 1 to 20wt%, 2 to 15wt%, 3 to 12wt%, 4 to 10wt%, or 6 to 8wt%.

[0349] 9. A composition as described in any of the preceding paragraphs, wherein the solvent is selected from ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene glycol-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 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-ethoxyethanol, 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, ethylene glycol ethers, propylene glycol or dipropylene glycol.

[0350] 10. A composition as described in 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%.

[0351] 11. A composition as described in any of the preceding paragraphs, wherein the composition further comprises one or more components selected from the following group: a builder, a chelating agent, a dispersant, an enzyme stabilizer, a catalytic material, a bleach activator, hydrogen peroxide, a source of hydrogen peroxide, a preformed peracid, a polymer dispersant, a suds suppressor, a dye, a perfume, a structural elastic agent, a carrier, a hydrotrope, a processing aid and / or a pigment.

[0352] 12. A composition as described in any of the preceding paragraphs, wherein the composition further comprises an additional enzyme selected from the group consisting of: proteases, cellulases, amylases, pectinases, mannanases, pectin lyases, phosphodiesterases (PDEs), deoxyribonucleases (DNases), hexosaminidase, hemicelluloses, and combinations thereof.

[0353] 13. The composition of any of paragraphs 1-12, wherein the lipase is of microbial origin, particularly fungal or bacterial origin.

[0354] 14. The composition of any of paragraphs 1-13, wherein the composition comprises a lipase, such as a fungal lipase derived from a strain of Thermomyces lanuginosus.

[0355] 15. A composition as described in any of paragraphs 1-14, wherein the lipase is

[0356] 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;

[0357] ii) a variant having lipase activity and 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 with a lipase as shown in SEQ ID NO: 1, 2, 3, 4, 5, 6 or 7;

[0358] iii) a fragment of the lipase according to (i) or (ii) having lipase activity.

[0359] 16. The composition of any of paragraphs 1-15, wherein the lipase is a variant comprising substitutions at positions corresponding to T231R+N233R of SEQ ID NO: 1, and optionally at least one or more of D96E, D111A, D254S, G163K, P256T, G91T and G38A.

[0360] 17. A composition as described in any of paragraphs 1-16, wherein 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% but less than 100% sequence identity to SEQ ID NO: 1, and comprises a substitution at a position corresponding to T231R+N233R, and at least one or more of D96E, D111A, D254S, G163K, P256T, G91T and G38A of SEQ ID NO: 1, which is selected from the group consisting of:

[0361] a.D96E+T231R+N233R;

[0362] b.N33Q+D96E+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0363] <h2 style=";text-align:left;direction:ltr"> c.N33Q+D111A+T231R+N233R;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0364] <h2 style=";text-align:left;direction:ltr"> d.N33Q+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0365] <h2 style=";text-align:left;direction:ltr"> e.N33Q+G38A+G91T+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0366] <h2 style=";text-align:left;direction:ltr"> f.N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0367] <h2 style=";text-align:left;direction:ltr"> g.D27R+N33Q+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0368] <h2 style=";text-align:left;direction:ltr"> h.D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0369] <h2 style=";text-align:left;direction:ltr"> i.D27R+N33Q+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0370] <h2 style=";text-align:left;direction:ltr"> j.D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0371] <h2 style=";text-align:left;direction:ltr"> k.D96E+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0372] <h2 style=";text-align:left;direction:ltr"> l.T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0373] <h2 style=";text-align:left;direction:ltr"> m.G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0374] <h2 style=";text-align:left;direction:ltr"> n.D27R+N33Q+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0375] <h2 style=";text-align:left;direction:ltr"> o.D27R+G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0376] <h2 style=";text-align:left;direction:ltr"> p.D96E+G163K+T231R+N233R+D254S;<h2 style=";text-align:left;direction:ltr"> <h2 style=";text-align:left;direction:ltr">

[0377] q.D27R+G163K+T231R+N233R+D254S;

[0378] r.D27R+G38A+G91T+D96E+D111A+G163K+T231R+N233R+D254S;

[0379] s.D27R+G38A+G91T+D96E+G163K+T231R+N233R+D254S+P256T;

[0380] t.D27R+G38A+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0381] u.D27R+D96E+G163K+T231R+N233R+D254S;

[0382] v.D27R+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0383] w.D27R+G38A+D96E+G163K+T231R+N233R+D254S+P256T

[0384] x.D111A+G163K+T231R+N233R+D254S+P256T;

[0385] y.D111A+T231R+N233R;

[0386] z.D111A+T231R+N233R+D254S+P256T;

[0387] aa.D27R+D96E+D111A+G163K+T231R+N233R;

[0388] bb.D27R+D96E+D111A+T231R+N233R;

[0389] cc.D27R+N33Q+G38A+D96E+D111A+T231R+N233R+D254S+P256T;

[0390] dd.D27R+G38A+D96E+D111A+G163K+E210Q+T231R+N233R+D254S+P256T;

[0391] ee.D27R+T231R+N233R+D254S+P256T;

[0392] ff.D96E+D111A+G163K+T231R+N233R;

[0393] gg.D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0394] hh.D96E+D111A+G163K+T231R+N233R+P256T;

[0395] ii.D96E+D111A+T231R+N233R;

[0396] jj.D96E+D111A+T231R+N233R+D254S;

[0397] kk.D96E+D111A+T231R+N233R+D254S+P256T

[0398] ll.D96E+D111A+T231R+N233R+P256T;

[0399] mm.D96E+G163K+T231R+N233R+D254S+P256T;

[0400] nn.D96E+T231R+N233R+D254S+P256T;

[0401] oo.D96E+T231R+N233R+P256T;

[0402] pp.G38A+D96E+D111A+T231R+N233R;

[0403] qq.G91T+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0404] rr.G91T+D96E+D111A+T231R+N233R;

[0405] ss.G91T+D96E+T231R+N233R;

[0406] tt.G91T+T231R+N233R+D254S+P256T;

[0407] uu.N33Q+D96E+D111A+G163K+T231R+N233R+D254S+P256T;

[0408] vv.T231R+N233R+D254S+P256T;

[0409] ww.T231R+N233R+P256T.

[0410] 18. A composition as described in any of paragraphs 1-17, wherein the lipase is a variant of a parent lipase, wherein the variant

[0411] (a) comprises 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 comprises 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;

[0412] (b) having at least 60% but less than 100% sequence identity to SEQ ID NO: 1;

[0413] (c) having lipase activity.

[0414] 19. The composition of any of paragraphs 1-18, 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.

[0415] 20. The composition of any of paragraphs 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.

[0416] 21. The composition of any of paragraphs 18-20, wherein the lipase variant further comprises one of the substitutions selected from the group consisting of S54T, S83T, G91A, A150G, I255A, and E239C, wherein the numbering is according to SEQ ID NO: 1.

[0417] 22. The composition of any of paragraphs 18-21, wherein the lipase variant comprises substitutions E1C+N233C and one or more additional substitutions, wherein numbering is according to SEQ ID NO: 1.

[0418] 23. The composition of any of paragraphs 18-22, 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% but less than 100% sequence identity to SEQ ID NO: 1, and comprises or consists of a substitution corresponding to one of the following substitution groups numbered using SEQ ID NO: 1:

[0419] E1C+H198L+N233C

[0420] E1C+H198G+N233C

[0421] E1C+L69V+N233C

[0422] E1C+L69T+N233C

[0423] E1C+L69S+N233C

[0424] E1C+L69H+N233C

[0425] E1C+L69F+N233C

[0426] E1C+L69C+N233C

[0427] E1C+H198Y+N233C

[0428] E1C+H198T+N233C

[0429] E1C+H198G+N233C

[0430] E1C+L227F+N233C

[0431] E1C+L227R+N233C

[0432] E1C+E210T+N233C

[0433] E1C+E210N+N233C

[0434] E1C+V176M+N233C

[0435] E1C+K98T+N233C

[0436] E1C+K98E+N233C

[0437] E1C+E56S+N233C

[0438] E1C+E56Q+N233C

[0439] E1C+E56R+N233C

[0440] E1C+F51M+N233C

[0441] E1C+D27R+F51Y+N233C

[0442] E1C+V2I+N233C

[0443] E1C+V2N+N233C

[0444] E1C+V2K+N233C

[0445] E1C+V2A+N233C

[0446] E1C+D96L+N233C

[0447] E1C+L69R+N233C

[0448] E1C+V2Y+N233C

[0449] E1C+N233C+P256T

[0450] E1C+N233C+D254S

[0451] E1C+T231R+N233C

[0452] E1C+H198S+N233C

[0453] E1C+D111A+N233C

[0454] E1C+D96E+N233C

[0455] E1C+G38A+N233C

[0456] E1C+N33Q+N233C

[0457] E1C+N33K+N233C

[0458] E1C+E210A+N233C

[0459] E1C+E210Q+N233C

[0460] E1C+E210R+N233C

[0461] E1C+H198D+N233C

[0462] E1C+K98R+N233C

[0463] E1C+K98V+N233C

[0464] E1C+F51L+N233C

[0465] E1C+F51I+N233C

[0466] E1C+K237C

[0467] E1C+L227G+N233C

[0468] E1C+E210K+N233C

[0469] E1C+V176L+N233C

[0470] E1C+K98Q+N233C

[0471] E1C+E56K+N233C

[0472] E1C+L147S+N233C+D254S

[0473] E1C+Y220F+N233C

[0474] E1C+K98I+N233C

[0475] E1C+N233C

[0476] E1C+D27R+F51I+E56R+K98E+T231R+N233C

[0477] E1C+D27R+F51I+E56R+K98E+T231R+N233C+D254S

[0478] E1C+D27R+G38A+F51L+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T

[0479] E1C+D27R+G38A+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0480] E1C+D27R+G38R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0481] E1C+D27R+F51L+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T

[0482] E1C+D27R+F51L+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T

[0483] E1C+D27R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T

[0484] E1C+D27R+G38A+F51I+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0485] E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T

[0486] E1C+D27R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T

[0487] E1C+D27R+F51V+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+D254S+P256T

[0488] E1C+D27R+F51V+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0489] E1C+D27R+F51V+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0490] E1C+D27R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0491] E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0492] E1C+F51V+D96E+K98I+D111A+G163S+H198S+Y220F+T231R+N233C+P256T

[0493] E1C+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0494] E1C+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T

[0495] E1C+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+P256T

[0496] E1C+F51V+D96I+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0497] E1C+F51V+K98I+D111A+G163K+H19S+Y220F+T231R+N233C+D254S+P256T

[0498] E1C+F51I+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0499] E1C+D27R+F51L+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0500] E1C+D27R+N33K+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C

[0501] E1C+G38R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0502] E1C+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0503] E1C+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0504] E1C+D27R+G38R+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T.

[0505] 24. A composition as described in paragraphs 1-23, wherein the lipase is

[0506] 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;

[0507] ii) a variant having lipase activity and 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 with the lipase shown in SEQ ID NO: 2;

[0508] iii) a fragment of the lipase according to (i) or (ii) having lipase activity.

[0509] 25. The composition of paragraph 24, wherein the composition comprises or consists of the amino acids of SEQ ID NO: 2.

[0510] 26. A composition as described in paragraph 24 or 25, wherein the lipase is a variant of SEQ ID NO: 2,

[0511] This variant includes:

[0512] (a) corresponding to the following substitutions: 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; N101 D,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

[0513] (b) corresponding to the following substitutions: 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; L 227G+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

[0514] (c) corresponds to the following substitution:

[0515] <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+T252 A+L264A; V60W+T252A+L264A; G61A+T252A+L264A; V60G+T252A+L264A; T72G+T252A+L264A; V60L+T252A+L26 4A; A4R+R233N+T252A; A4R+R233N+L264A; R233N+T252A+L264A; A4R+V60M+L227G; A4R+L227G+R233N; A4R+V6 0M+R233N; V60M+L227G+R233N; V60M+L227G+L264V; V60M+L227G+L264I; V60M+L227G+T252A; A4R+L227A+L26 4A; G23A+N250P+T252I; V60K+N250P+T252I; L97V+N250P+T252I; A150G+N250P+T252I; V202L+N250P+T252I; V228P+N250P+T252I;L227G+N250P+T252I;F211G+N250P+T252I;V142I+N250P+T252I;V60M+L227G+V228Q;A 4L+T252A+L264A; T114E+T252A+L264A; G156A+T252A+L264A; L168E+T252A+L264A; N73G+T252A+L264A; Japanese / or;

[0516] (d) Fees below:

[0517] 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+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

[0518] (e) substitutions corresponding to the following:

[0519] 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

[0520] (f) substitutions corresponding to the following:

[0521] L7F+T91A+A150G+L154V+T252A+L264A; and / or (g) substitutions corresponding to the following: D1C+V202C+R233C+I238C+G245C+T252A+P253C+L264A; and / or A4R+I90V+N94E+D96L+N101P+R233N+T252A+L264A; These corresponding items are of the polypeptide as shown in SEQ ID NO:2.

[0522] 27. The composition of paragraph 26, further comprising one or more substitutions corresponding to:

[0523] A4E; A20T; P29S; A46Q; S58N; T91A; N92D; L93F,I; S105D,E,N; R179G,Q;N 200R; Y220F; L227G; R231K; T244E; Q249E; T252A,S,V; N25S; A38T; R84S; N 94D; V98Q; N101K; D130H; D137G; R232K; T244A,N,K; A249G,R; N250P; T25 2I; D254S; P256T; A257I; L264A; N94V; F95V; L97S; N101E; S105K; D129G; A 134S; 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 (using SEQ ID NO:2).

[0524] 28. The composition of any of paragraphs 26 or 27, comprising substitutions corresponding to:

[0525] A20T+L93F; A4E+A46Q; F51I+T244E; L227G+R233N; L227G+T244E; L227G+T252A; L93I+V98I; N101D+S105D; Q210E+Q249E; R179Q+G212E; R231K+R233K; R233N+T252A; S105D+G212E; S105E+R108Q; S105N+G212D; S105N+G212E; S58N+V60S; T244E+T252A; T252A+I255A; T252S+I255A; and / or T91A+V98I (using SEQ ID NO:2 for numbering).

[0526] 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).

[0527] 30. A composition as described in any of paragraphs 26-29, comprising substitutions corresponding to: A38T+D96H+D137G; A4R+T252A+L264A; D1G+T252A+L264A; D62N+T252A+L264A; D165Q+N250P+T252I; H198S+Y220F+L264A; N101K+S105N+R108E; N94Q+N250P+T 252I; Q210E+T244E+Q249G; Q210E+T252A+L264A; R231K+R232K+R233K; S83T+H198S+D254S; R233N+T252A+L264A; A46Q+T252A+L264A; N39D+T252A+L264A; R24E+V60M+L227G; and / or F51I+T252A+L264A (using SEQ ID NO: 2 for numbering).

[0528] 31. A composition as described in any of paragraphs 26-30, comprising substitutions corresponding to: A4R+R233N+T252A+L264A; A4R+V60M+L227G+R231T; A4R+V60M+L227G+R232V; A4R+V60M+L227G+R233N; E87Q+T91A+D96I+V98Q; G109R+Q210E+T244N+Q249E; L227G+R233N+T 252A+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; and / or R24E+V228P+T252A+L264A (using SEQ ID NO: 2 for numbering).

[0529] 32. The composition of any of paragraphs 26-31, comprising substitutions corresponding to 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 (using SEQ ID NO: 2 for numbering).

[0530] 33. The composition of any of paragraphs 26-32, comprising substitutions corresponding to L7F+N8K+Q210E+L227G+T252A+L264A; 8D+101K+S105G+R108Q+R179E+G212E; N8D+R209Q+Q210E+T244N+N248K+Q249E; V60E+S83T+T91A+H198S+T252A+L264P; or V60M+T91A+Q210E+V228L+T252A+L264Y (using SEQ ID NO: 2 for numbering).

[0531] 34. The composition of any of paragraphs 26-33, comprising substitutions corresponding to V60K+S83T+T91A+H198I+V228L+T252A+L264P; or V60M+A157V+Q210E+L227V+V228A+T252A+L264V (using SEQ ID NO: 2 for numbering).

[0532] 35. The composition of any of paragraphs 26-34, comprising substitutions corresponding to D1E+A4Q+L7F+K11N+S37T+A46K+A133R+V142F+T170S+V202I+Q210E+L227G (using SEQ ID NO: 2 for numbering).

[0533] 36. A composition as described in any one of the preceding paragraphs, wherein the additional enzyme is a protease, a hexosaminidase, a DNA enzyme, an amylase, a cellulase or a combination thereof, such as a combination of a protease and a DNA enzyme and / or a hexosaminidase, or a combination of a protease and an amylase.

[0534] 37. The composition of any of the preceding paragraphs, wherein the composition comprises probiotic spores, and preferably the probiotic spores are derived from Bacillus.

[0535] 38. A composition as described in any of the preceding paragraphs, wherein the composition is formulated as a liquid, gel, paste, bar; powder, tablet, bag with one or more chambers, single or multiple chamber unit dosage form or spray form.

[0536] 39. A composition as described in any of the preceding composition paragraphs, wherein the composition is a hand dishwashing detergent, a professional cleaning detergent, a medical cleaning detergent, or a hard surface cleaner.

[0537] 40. A cleaning composition comprising:

[0538] (a) 1 to 60 wt%, e.g. 3-40 wt%, 5-25 wt% of a surfactant system;

[0539] (b) 1 to 40 wt%, e.g., 3-20 wt%, 5-10 wt% of a solvent, wherein the solvent is 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and combinations thereof; and optionally

[0540] (c) 0.001 to 10 wt% of a lipase, preferably the lipase is as defined in any of the preceding composition paragraphs 14 to 35.

[0541] 41. A cleaning composition as described in paragraph 40, wherein the surfactant system comprises one or more surfactants selected from linear alkylbenzene sulfonic acid (LAS), alcohol ether sulfate (AEOS), alkyl sulfate (AS) especially sodium lauryl sulfate (SLS) and sodium laureth sulfate (SLES), and alcohol ethoxylate (AEO) especially linear alcohol (C 12-15 ) ethoxylate.

[0542] 42. A cleaning composition as described in paragraphs 40-41, wherein the solvent is present at a level of 2-12wt%, such as 2.1-10wt%, 2.2-10wt%, 2.4-8wt%, 2.6-8wt%, 2.8-5wt%, 3-6wt%, 4-6wt%, based on the total weight of the composition, and wherein the solvent comprises: 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 oxo alcohol ethoxylate.

[0543] 43. A composition as described in any one of the preceding composition paragraphs, wherein the composition is a spray-type detergent and has a pH lower than 11, for example in the range of 6-9.5, in the range of 6.5-9, in the range of 6.8-8.5, or in the range of 7-8, more preferably with a neutral pH of 6.5-7.5, such as pH 7.0, 7.1 or 7.

[0544] 44. A composition as described in any one of the aforementioned composition paragraphs, wherein the composition is formulated as a liquid form and has a pH lower than 11, for example in the range of 6-9.5, in the range of 6.5-9, in the range of 6.8-8.5, or in the range of 7-8, more preferably with a neutral pH of 6.5-7.5, such as pH 7.0, 7.1 or 7.

[0545] 45. A method for cleaning an article, the method comprising contacting a surface with a cleaning composition as described in any of the preceding paragraphs, preferably the article is a surface, such as a hard surface, or a textile.

[0546] 46. ​​The method of paragraph 45, wherein the contacting is performed by spraying, wiping, pouring, soaking and / or mopping the surface with the hard surface cleaning composition.

[0547] 47. The method of paragraph 45 or 46, wherein the hard surface is selected from the group consisting of steel surfaces, rubber surfaces, plastic surfaces, glass surfaces, ceramic surfaces, melamine surfaces, wood surfaces, coating surfaces, cement countertops, kitchen countertops, and surfaces of medical devices.

[0548] 48. The method of any of paragraphs 45-47, wherein the lipase is dosed at a concentration of at least 0.0001 mg of enzyme protein per gram of the hard surface cleaning composition, for example, 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.

[0549] 49. A ready-to-use article for cleaning surfaces, such as hard surfaces, comprising any of the preceding cleaning compositions.

[0550] 50. The article of paragraph 49, wherein the article is a rag or a sponge.

[0551] 51. The article of paragraph 49 or 50, wherein the article is impregnated with any of the foregoing hard surface cleaning compositions.

[0552] The present invention is further illustrated in the following non-limiting examples.

[0553] Examples

[0554] Assay I: Determination of lipase activity by p-nitrophenyl (pNP) assay

[0555] The hydrolytic activity of the lipase can be determined by a kinetic assay using p-nitrophenyl acyl esters as substrates. A 100 mM stock solution of each of the following substrates in DMSO can be diluted to a final concentration of 1 mM-25 mM in assay buffer (50 mM Tris; pH 7.7; 0.4% Triton X-100): p-nitrophenyl butyrate (C4), p-nitrophenyl hexanoate (C6), p-nitrophenyl decanoate (C10), p-nitrophenyl laurate (C12) and p-nitrophenyl palmitate (C16) (all from Sigma-Aldrich Danmark A / S, Kirkebjerg Allé 84, 2605 Brondby) ); Catalog numbers: C3: N-9876, C6: N-0502, C10: N-0252, C12: N-2002, C16: N-2752). Lipase in 50 mM Hepes (pH 8.0); 10 ppm Triton X-100; + / - 20 mM CaCl2 was added at the following final protein concentrations: 0.01 mg / ml; 5 x 10 -3 mg / ml; 2.5x10 -4 mg / ml and 1.25x10 -4 mg / ml is added to the substrate solution in a 96-well NUNC plate (Cat. No. 260836, Kamstrupvej 90, DK-4000, Roskilde). The p-nitrophenol released by the hydrolysis of p-nitrophenyl acyl can be monitored at 405 nm for 5 minutes at 10 second intervals on a Spectra max190 (Molecular Devices GmbH, Bismarckring 39, 88400 Biberach an der Riss, Germany).

[0556] Materials and methods

[0557] Lipase A: Thermomyces lanuginosus lipase (TLL) shown in SEQ ID NO: 1, which has the following substitutions: E1C+D27R+G38A+F51V+D96E+K98I+D111A+G163K+H198S+Y220F+T231R+N233C+D254S+P256T

[0558] Solvent A : Diethylene glycol monobutyl ether (BuCb) (available from Dow Chemical Company)

[0559] Solvent B : Ethylene glycol ether (EPH) (available from Usolf)

[0560] Standard detergent M1 : 2 wt% of fatty alcohol polyoxyethylene ether-9 (AEO-9). The pH of the standard detergent was adjusted to about 11 or 8.5 using monoethanolamine.

[0561] Commercial detergent : DAWN Powerwash spray detergent (available from Procter & Gamble (P&G)) was used. This detergent contained about 3 wt% of dipropylene glycol butyl ether (DPGBE) solvent.

[0562] Standard Detergent V1: 4 wt% sodium laureth sulfate, 1 wt% alkyl dimethylamine oxide (OA-2), 2.84 wt% ethylene glycol monohexyl ether (C6EO1), 2.78 wt% DPGBE, 3.2 wt% PPG400. Adjust to 100% with water.

[0563] Standard Detergent V2: 4 wt% sodium laureth sulfate, 1 wt% alkyl dimethylamine oxide (OA-2), 2.84 wt% ethylene glycol monohexyl ether (C6EO1), 2.78 wt% DPGBE, 3.2 wt% fatty alcohol polyoxyethylene ether-9 (AEO-9), and adjusted to 100% with water.

[0564] Example 1

[0565] Soil Removal Test for Standard Detergents for Hard Surface Applications

[0566] Six different oils were mixed together in the amounts shown in Table 2 below to prepare an oil mixture. The stainless steel card was weighed to obtain an initial weight (marked as M0). About 0.3 g of the oil mixture was evenly spread on the stainless steel card. The card contaminated with the oil mixture was then aged in an oven at 120° C. for 1 hour and kept dry before use.

[0567] Table 2: Composition of oil mixture

[0568]

[0569] The soiled card was weighed to obtain the weight before washing (marked as M1), and then the soiled card was soaked in a beaker containing different detergent formulations (see Table 3 below) at 35°C for 15min or 7.5min. Then, the card was removed from the beaker and dried at room temperature. The dried card was weighed to obtain the weight after washing (marked as M2).

[0570] The washing performance (or soil removal rate) of different formulations is calculated as:

[0571] (M1-M2) / (M1-M0) x 100%

[0572] Each formulation was replicated three times and the average soil removal rates are summarized in Table 3 below.

[0573] The improvement in scale removal rate (ISR) by adding lipase and / or solvent is calculated as:

[0574] Soil Removal of Standard Detergent with Lipase and / or Solvent - Soil Removal of Standard Detergent Only

[0575] Table 3: Soil removal of different hard surface detergent formulations with or without lipase A

[0576]

[0577] As can be seen from Table 2 above, when the pH of the detergent is reduced from pH 11 to pH 8.5, the soil removal rate decreases (Formulation 2 compared to Formulation 1). At reduced pH, the addition of lipase or solvent to the hard surface standard detergent compensates for part of the loss of washing performance (Formulation 3 or 4 compared to Formulation 2; Formulation 6 or 7 compared to Formulation 2). Surprisingly, when both lipase and solvent are added together to the standard detergent, the soil removal rate is greatly improved and even exceeds the soil removal rate of the initial high pH standard detergent.

[0578] Furthermore, by comparing Formulation 9 or 10 with Formulation 2, it is apparent that incorporating both lipase and solvent into a hard surface detergent can achieve similar cleaning performance in a shorter time (50% shorter), or in other words can improve the cleaning efficiency of the detergent.

[0579] The enhanced cleaning effect due to the synergistic effect of lipase and solvent allows hard surface cleaning detergents to be formulated at low or mild pH (eg, pH 9 or even lower) without compromising cleaning performance compared to conventional high pH formulations.

[0580] Example 2

[0581] Confirmation of the enhanced cleaning effect of commercial detergents

[0582] DAWN Powerwash spray detergent (available from Procter & Gamble) containing solvents such as dipropylene glycol butyl ether and hexyl ethoxylate. 50 ppm of lipase A was added to the detergent.

[0583] Example 2a: Testing of Homemade Greasy Stains

[0584] Preparation of Homemade Greasy Stains :

[0585] 1) Melt butter in a 70℃ water bath.

[0586] 2) Use a pipette to take out 40–100 μL of melted butter and apply it to the brick in a 6-cm diameter circle.

[0587] 3) Use your fingers to spread the stain evenly over the tile surface.

[0588] 4) Wait for about 2-4 hours before washing.

[0589] Washing test :

[0590] 1) A spray detergent containing 50 ppm lipase was prepared.

[0591] 2) Spray detergent with / without lipase onto the stain once (1 full spray).

[0592] 3) Leave at room temperature for 15 min or 1 min (see Table 4 below), then rinse gently under running water for about 20 seconds.

[0593] 4) Prepare a 0.3% Oil Red O (available from Sigma) solution in 75% ethanol.

[0594] 5) Immerse the washed bricks in a 0.3% Oil Red O solution to visualize any remaining greasy stains. The more residual stains there are, the redder the brick will appear.

[0595] 6) Dry the bricks at room temperature.

[0596] 7) The R460nm of the dried bricks was measured using a DigiEye (Model: DigiEye Color Measurement and Imaging System, Serial No. DE0114501). A higher R460nm value indicates a lighter red color of the brick, and therefore a higher level of dirt removal.

[0597] 8) The experiment was repeated 9 times and the average R460nm values ​​are listed in Table 4 below.

[0598] Table 4. Enhanced cleaning demonstrated in solvents containing commercial detergents

[0599]

[0600] The results shown in Table 4 confirm the enhanced cleaning effect described above (improved soil removal levels and improved washing efficiency) and further demonstrate that by using both lipase and solvent, the amount of detergent can be reduced (e.g., by 20%) while still providing even better soil removal performance (Condition 3 compared to 1).

[0601] Example 2b: Testing using the tough technical stain DM-90

[0602] Washing test :

[0603] 1) A spray detergent containing 50 ppm lipase was prepared.

[0604] 2) Detergent with / without lipase was sprayed three times onto a DM-90 stain tile (available from CFT, Center For Testmaterials).

[0605] 3) Leave at room temperature for 15 minutes or 2 minutes (see Table 5 below), then rinse gently under running water for about 20 seconds.

[0606] 4) Dry the bricks at room temperature.

[0607] 5) The R460nm of the dried bricks was measured using DigiEye (Model: DigiEye Color Measurement and Imaging System, Serial No. DE0114501). A higher R460nm value represents a higher level of dirt removal or dirt removal performance.

[0608] 6) Repeat 10 times and list the average R460nm value in Table 5 below. The pictures of 10 repetitions are shown in Figure 1 In. From Figure 1 It can be clearly seen in the figure that under condition 1 or 2, the entire plate is very red, indicating that a lot of stain still remains. In contrast, under condition 3 (where the detergent contains both solvent and lipase), the red area is replaced by a white / grey circle (the area in contact with the detergent), indicating that the stain is removed.

[0609] Table 5. Enhanced cleaning demonstrated in solvents containing commercial detergents

[0610]

[0611] The results shown in Table 5 confirm the enhanced cleaning effect described above and further demonstrate that by using both lipase and solvent, the amount of detergent can be reduced (e.g., by 20%) while still providing even better soil removal performance against tough technical stains (Condition 3 vs. 1).

[0612] Example 3

[0613] Greasy stain removal test for dishwashing standard detergents

[0614] a) Preparation of tallow stain

[0615] 1) Melt the beef tallow in a 70°C water bath.

[0616] 2) Use a pipette to take out 40 μl of melted butter and apply it to a 6-cm diameter circle on the melamine tile.

[0617] 3) Use your fingers to spread the stain evenly over the tile surface.

[0618] 4) Wait about 2-4 hours before washing.

[0619] b) Preparation of mixed greasy stains

[0620] 5) Melt the mixed greasy stains (hot pot base containing beef tallow: salad oil in a ratio of approximately 3:2) in a 70°C water bath.

[0621] 6) Use a pipette to take out 40 μl of the melted mixed greasy stain and apply it to the melamine tile in a 6-cm diameter circle.

[0622] 7) Use your fingers to spread the stain evenly over the tile surface.

[0623] 8) Wait about 2-4 hours before washing.

[0624] Washing performance test

[0625] 1) Standard 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.

[0626] 2) Spray detergent with / without Lipase A on each stain 3 times.

[0627] 3) Leave at room temperature for 15 minutes, then rinse gently under running water for about 10 seconds.

[0628] 4) The tiles with mixed grease stains were dried at room temperature. For tiles stained with tallow, the following steps 5) and 6) were performed to visualize the residual stains before measurement.

[0629] 5) Prepare a 0.3% Oil Red O (available from Sigma) solution in 75% ethanol.

[0630] 6) Immerse the washed tallow bricks in 0.3% Oil Red O solution to visualize residual greasy stains, and dry the bricks at room temperature. The more residual stains, the redder the bricks will appear.

[0631] 7) Measure the R460nm of the dried brick using DigiEye (Model: DigiEye Color Measurement and Imaging System, Serial No. DE0114501). Higher R460nm values ​​represent higher levels of dirt removal or cleaner bricks.

[0632] 8) The experiment was repeated three times and the average R460nm values ​​are listed in Tables 6 to 8 below.

[0633] Table 6 Lipase performance of standard detergent V1

[0634]

[0635] Table 7 Lipase performance of standard detergent V2 on mixed greasy stains

[0636]

[0637] Table 8 Lipase performance of standard detergent V2 on mixed greasy stains

[0638]

[0639]

[0640] From Table 6, Table 7, Table 8 and Figure 2 It is clearly seen that standard detergents V1 and V2 can show significant and consistent lipase performance on greasy stains. The significant cleaning effect of lipase is also visible to the naked eye, see Figure 2 .

[0641] Example 4

[0642] Greasy stain removal test on fabrics

[0643] Preparation of mixed greasy stains

[0644] 1) Melt the mixed greasy stains (hot pot base containing beef tallow: salad oil in a ratio of approximately 3:2) in a 70°C water bath.

[0645] 2) Take out 30 μl of the melted mixed greasy stain with a pipette and apply it on the PCN01 fabric, and use your fingers to spread the stain evenly on the fabric surface; the final circular shape of the stain is about 2.8 cm.

[0646] 3) Wait overnight and then perform the wash test.

[0647] Washing performance test

[0648] 1) Standard detergent V2 with or without 77 ppm lipase A was prepared.

[0649] 2) Spray detergent with / without Lipase A on each stain 3 times.

[0650] 3) Leave at room temperature for 15 minutes, then rinse under running water for about 10 seconds.

[0651] 4) Dry the fabric thoroughly at room temperature.

[0652] 5) The R460nm of the dry fabric was measured using a Datacolor 800V (serial number 8814595). Higher R460nm values ​​represent higher soil removal levels or cleaner fabric.

[0653] 6) The results were repeated three times, and the average R460nm values ​​of the three replicates are listed in Table 9 below.

[0654] Table 9 Synergistic effects on textiles

[0655] R460nm Detergent only, 15min 22.1 Detergent + 77ppm lipase A, 15min 35.8

[0656] According to Table 9, detergents containing the solvent of the present invention can enhance the lipase performance on greasy stains present on textiles.

Claims

1. A hard surface cleaning composition, comprising: (a) 0.1 to 60 wt % of a surfactant system; (b) 0.1 to 40 wt % of a solvent, wherein the solvent is 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10 wt% of lipase.

2. 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 composition of claim 1 or 2, wherein the solvent is selected from ethanol, propanol, isopropanol and butanol, isobutanol, ethylene glycol, diethylene glycol, triethylene glycol, propylene glycol, dipropylene glycol, mixed ethylene glycol-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 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-ethoxyethanol, 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, ethylene glycol ethers, propylene glycol or dipropylene glycol.

4. The composition of any one of claims 1 to 3, wherein 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) a variant having lipase activity and 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 with a lipase as shown in SEQ ID NO: 1, 2, 3, 4, 5, 6 or 7; iii) a fragment of the lipase according to (i) or (ii) having lipase activity.

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

6. The composition of any one of claims 1-5, wherein 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% but less than 100% sequence identity to SEQ ID NO: 1, and comprises substitutions at positions corresponding to T231R+N233R, and 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: 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.

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

1.

8. The composition of any one of claims 1-7, 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% but less than 100% sequence identity to SEQ ID NO: 1, and comprises or consists of a substitution corresponding to one of the following substitution groups numbered using SEQ ID NO: 1: 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+N233CE1C+E56Q+N233CE1C+E56R+N233CE1C+F51M+N233CE1C+D27R+F51Y+N233CE1C+V2I+N233CE1C+V2N+N233CE1C+V2K+N233CE1C+V2A+N233CE1C+D96L+N233CE1C+L69R+N233CE1C+V2Y+N233CE1C+N233C+P256TE1C+N233C+D254SE1C+T231R+N233CE1C+H198S+N233CE1C+D111A+N233CE1C+D96E+N233CE1C+G38A+N233CE1C+N33Q+N233CE1C+N33K+N233CE1C+E210A+N233CE1C+E210Q+N233CE1C+E210R+N233CE1C+H198D+N233CE1C+K98R+N233CE1C+K98V+N233CE1C+F51L+N233CE1C+F51I+N233CE1C+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.

9. The composition of any one of claims 1 to 8, wherein 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 having lipase activity and 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 with the lipase shown in SEQ ID NO: 2; iii) a fragment of the lipase according to (i) or (ii) having lipase activity.

10. The composition of any one of the preceding claims, wherein the composition comprises or consists of the amino acids of SEQ ID NO:

2.

11. A composition as claimed in any one of the preceding claims, 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. A composition as claimed in any preceding claim, wherein the composition comprises probiotic spores, and preferably the probiotic spores are of Bacillus origin.

13. A composition as claimed in any one of the preceding composition claims, wherein the composition is a spray-type detergent and has a pH below 11, for example in the range of 6-9.5, in the range of 6.5-9, in the range of 6.8-8.5, or in the range of 7-8, more preferably having a neutral pH of 6.5-7.5, such as pH 7.0, 7.1 or 7.

14. A method for cleaning a hard surface, the method comprising contacting the surface with a hard surface cleaning composition as claimed in any preceding claim.

15. A cleaning composition comprising: (a) 1 to 60 wt%, e.g. 3-40 wt%, 5-25 wt% of a surfactant system; (b) 1 to 40 wt%, e.g., 3-20 wt%, 5-10 wt% of a solvent, wherein the solvent is 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 blends, dibasic esters, alcohol ethoxylates such as linear alcohol ethoxylates, branched alcohols or oxo alcohol ethoxylates, and combinations thereof; and optionally (c) 0.001 to 10 wt% of a lipase, preferably the lipase is as defined in any one of the preceding claims 4-10.

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