Lipid removal in detergents

Abstract

The present invention relates to lipid removal enhancers that can be used alone or in conjunction with lipases in detergents for removing lipid stains, such as fats and oils, on surfaces, such as textiles, with an increased benefit-risk ratio.

Description

[0001] Reference to the Sequence Listing

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

[0003] The present invention relates to detergent compositions that comprise compounds capable of removing lipids from fabrics during the cleaning or laundering of the fabrics. Background Art

[0004] The ability of detergents to remove or reduce stains from textile surfaces is clearly of concern to consumers, and various surfactant components play a role in this process. However, there is a desire to improve the effectiveness of detergents. Some stains such as fats (lipids) can be difficult to remove, and lipases are traditionally added to improve fat removal. A potential disadvantage when using lipases is the formation and release of short-chain fatty acids (such as butyric acid and hexanoic acid), resulting in a perception of malodor. This is a potential problem for consumers who desire increased fat removal without a corresponding increase in malodor generation. The ratio between lipid removal and malodor generation is called the benefit-risk ratio, and in short, an increase in the benefit-risk ratio is desired. Additionally, since lipases are proteins, there is a risk that they will denature in compositions containing high detergent concentrations, such as concentrated fabric detergent compositions. Further, lipases (being proteins) are susceptible to proteolysis by proteases present in the detergent composition.

[0005] WO 2014 / 095618 (Unilever) discloses fabric cleaning compositions comprising a combination of one or more enzymes and arginine.

[0006] DE1942236 discloses the use of arginine and other amino acids for protein removal during washing.

[0007] None of the prior art discloses a laundry detergent comprising lysine, sodium stearoyl lactate, or an ester of lysine or arginine, and in particular they do not disclose the use of said esters for obtaining an increased benefit-risk ratio. Summary of the Invention

[0008] The inventors of the present invention have surprisingly found a number of lipid removal enhancers that can be used alone or in combination with lipases in detergents for removing lipid stains (such as fats and oils) from surfaces such as textiles, with an increased benefit-risk ratio and to a greater extent than arginine. The group of lipid removal enhancers covered by the present invention comprises esters of the two amino acids lysine (Lys, K) and arginine (Arg, R), and lysine and stearoyl lactate esters.

[0009] The present invention relates to a detergent composition comprising one or more of said lipid removal enhancers. The detergent composition may further comprise a lipase and additional enzymes.

[0010] In a further aspect, the present invention relates to the use of lysine, stearoyl lactylate, and the esters of lysine or arginine in a detergent composition for removing lipid stains such as fats and oils.

[0011] Such detergent compositions have several potential advantages, particularly very low odor generation and thus (also when used in combination with lipase), an increased benefit-risk ratio. In addition, they are less prone to proteolytic degradation during storage and are less sensitive to high detergent concentrations. It is also clear from the experimental data that lipid removal can be maintained at reduced detergent levels, resulting in less detergent use and improved sustainability.

[0012] Accordingly, the present invention discloses a detergent composition comprising:

[0013] a. at least one detergent component;

[0014] b. a lipid removal enhancer selected from the group consisting of lysine, stearoyl lactylate, C 1 to C 5 esters of lysine and C 1 to C 5 esters of arginine

[0015] c. optionally one or more enzymes.

[0016] Definitions

[0017] For the purposes of this detailed description, the following definitions apply. Note that the singular forms "a / an" and "the" include plural referents unless the context clearly dictates otherwise.

[0018] All technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs, unless otherwise defined or clearly indicated by the context.

[0019] All component levels provided herein are referenced to the active level of the component, unless otherwise defined or clearly indicated by the context.

[0020] Unless otherwise indicated, all percentages and ratios of components are by weight. Unless otherwise indicated, all percentages are based on the total composition.

[0021] Benefit-risk ratio

[0022] The benefit-risk ratio (B / R ratio) is the ratio between lipid removal and malodor generation, where malodor generation is measured as the amount of butyric acid released from a CS-10 cloth sample washed under the same conditions as the textile with a lipid stain.

[0023] C of lysine and arginine 1 -C 5 ester

[0024] Esters of lysine and arginine are derivatives of two amino acids in which the -OH group of the C-terminal carboxyl group has been replaced by an -OR group, where R is an alkyl or aryl group containing one to five carbon atoms. Preferably, R is an alkyl group containing one to five carbon atoms, and the alkyl group may be straight-chain or branched-chain.

[0025] Detergent component

[0026] The term "detergent component" means a detergent adjunct ingredient different from the lipid removal enhancer of the present invention. The exact nature of these additional cleaning or adjunct components, and their level of incorporation, will depend on the physical form of the composition and the nature of the operation in which the composition will be used. Suitable detergent components include, but are not limited to, the components described below, such as surfactants, builders and cobuilders, flocculation aids, chelating agents, dye transfer inhibitors, enzymes (not the enzymes of the present invention), enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, hydrogen peroxide sources, preformed peracids, polymeric agents, clay soil release / antiredeposition agents, brighteners, antifoaming agents, dyes, fragrances, structural elasticizers, fabric softeners, carriers, hydrotropes, fabric colorants, defoamers, dispersants, processing aids, and / or pigments. Detergent compositions will typically contain at least one surfactant and additional components, such as at least one builder and / or at least one bleaching component.

[0027] Detergent composition

[0028] The term "detergent composition" refers to a composition for removing unwanted compounds from articles to be cleaned, such as textiles, tableware, and hard surfaces. Detergent compositions can be used, for example, to clean textiles, tableware, and hard surfaces, for both household and industrial cleaning and / or for fabric care. These terms encompass any materials / compounds selected for the desired specific type of cleaning composition and product form (e.g., liquid, gel, powder, granule, paste, or spray composition), and include but are not limited to detergent compositions (e.g., liquid and / or solid laundry detergents and fine fabric detergents; hard surface cleaning formulations, such as for glass, wood, plastic, ceramic, and metal countertops and windows; carpet cleaners; oven cleaners; fabric fresheners; fabric softeners; and textile and clothing pretreatments, along with dish detergents). In addition to containing the lipid removal enhancer of the present invention, the detergent formulation can also contain one or more additional enzymes (such as amylase, protease, peroxidase, cellulase, β-glucanase, xyloglucanase, hemicellulase, xylanase, xanthanase, xanthan lyase, lipase, acyltransferase, phospholipase, esterase, laccase, catalase, arylesterase, amylase, α-amylase, glucoamylase, cutinase, pectinase, pectin lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, carrageenase, pullulanase, tannase, arabinosidase, hyaluronidase, chondroitinase, xyloglucanase, xylanase, pectin acetylesterase, polygalacturonase, rhamnogalacturonase, other endo-β-mannanases, exo-β-mannanases (GH5 and / or GH26), licheninase, phosphodiesterase, pectin methyl esterase, cellobiohydrolase, transglutaminase, nuclease, and combinations thereof, or any mixture thereof), and / or detergent components, such as surfactants, hydrotropes, builders, co-builders, chelating agents or chelating reagents, bleaching systems or bleaching components, polymers, fabric colorants, fabric conditioners, foam boosters, foam suppressants, dispersants, dye transfer inhibitors, optical brighteners, fragrances, soil opacifiers, optical brighteners, bactericides, fungicides, soil suspending agents, soil release polymers, anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, and solubilizers. Detergent compositions can contain one or more detergent components of any type. In particular, the detergent composition can be suitable for household or industrial laundry, i.e., laundry detergents. For further details, see the detergent composition paragraph.

[0029] Improved washing performance

[0030] The term "improved washing performance" is defined herein as an increased washing performance of a compound (lipid removal enhancer or lipase or a combination thereof) in a detergent composition relative to the washing performance of a reference.

[0031] Laundry:

[0032] According to the present invention, the term includes textiles, clothes, linen, etc., and can be made of any material, which includes yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile materials, fabrics made of these materials and products made of these fabrics (e.g., clothing and other articles). The textile or fabric can be in the form of knitted goods, woven fabrics, denim, non-woven fabrics, felt, yarns, and terry cloth. The textile can be cellulose-based, such as natural cellulose products, including cotton, linen / flax, jute, ramie, sisal or coir, or man-made cellulose products (e.g., derived from wood pulp), including viscose / rayon, acetate fiber (tricell), lyocell or blends thereof. The textile or fabric can also be non-cellulose-based, such as natural polyamides, including wool, camel hair, cashmere, mohair, rabbit hair and silk, or synthetic polymers such as nylon, aramid, polyester, acrylate, polypropylene and spandex / elastane, or blends thereof and blends of cellulose-based fibers and non-cellulose-based fibers. Examples of blends are blends of cotton and / or rayon / viscose with one or more accompanying materials, such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and / or cellulose-containing fibers (e.g., rayon / viscose, ramie, linen / flax, jute, acetate fiber, lyocell). The fabric can be conventional washable clothing, such as soiled household clothing. When the terms fabric or clothing are used, it is intended to also include the broad term textile. In the context of the present invention, the term "clothing" also encompasses fabrics.

[0033] Lipase

[0034] The terms "lipase / lipase enzyme", "lipolytic enzyme", "lipid esterase", "lipolytic polypeptide" and "lipolytic protein" refer to enzymes in the EC 3.1.1 class as defined by enzyme nomenclature. It can have lipase activity (triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74), sterol esterase activity (EC 3.1.1.13) and / or wax ester hydrolase activity (EC 3.1.1.50). For the purposes of the present invention, lipase activity (i.e., the hydrolytic activity of lipase) can be determined using pNP assays with substrates of different chain lengths as described in the experiments.

[0035] Lipid

[0036] Lipids are fatty, waxy, or oily compounds that are insoluble in polar solvents such as water. Lipids include fats (such as lard) and oils.

[0037] Lipid removal enhancer

[0038] In the context of the present invention, a lipid removal enhancer refers to a non-enzymatic compound that enhances lipid removal when used alone or in combination with a lipase. Compared with the absence of a lipid removal enhancer under the same test conditions, the effect of the lipid removal enhancer is more lipid removal. According to the present invention, this performance can be determined as the percentage of fat removal (%) as described in the examples.

[0039] Malodor

[0040] Malodor (or bad smell) is measured as the amount of butyric acid released from the CS-10 cloth sample.

[0041] Sequence identity

[0042] The relatedness between two amino acid sequences is described by the parameter "sequence identity". For the purposes of the present invention, the Needleman–Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. [Journal of Molecular Biology] 48:443-453) is used to determine the sequence identity between two amino acid sequences, which is implemented as the Needle program of the EMBOSS software package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. [Trends in Genetics] 16:276-277, preferably version 5.0.0 or later). The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (the EMBOSS version of BLOSUM62) substitution matrix. The output of "longest identity" marked by Needle (obtained using the -nobrief option) is used as the percentage of identity and is calculated as follows:

[0043] (Identical residues × 100) / (Alignment length - Total number of gaps in the alignment)

[0044] Textile

[0045] The term "textile" means any textile material, which includes yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile materials, fabrics made from these materials, and products made from fabrics (e.g., clothing and other items). Textiles or fabrics can be in the form of knitted goods, woven fabrics, denim, non-woven fabrics, felt, yarns, and terry cloth. Textiles can be cellulose-based, such as natural cellulose products, including cotton, linen / flax, jute, ramie, sisal, or coir, or man-made cellulose products (e.g., derived from wood pulp), including viscose / rayon, acetate fiber (triacetate), lyocell, or blends thereof. Examples of blends are blends of cotton and / or rayon / viscose with one or more accompanying materials, such as wool, synthetic fibers (e.g., polyamide fibers, acrylic fibers, polyester fibers, polyvinyl chloride fibers, polyurethane fibers, polyurea fibers, aramid fibers), and / or cellulose-containing fibers (e.g., rayon / viscose, ramie, linen / flax, jute, acetate fiber, lyocell). Fabrics can be conventional washable clothing, such as soiled household clothing. When the terms fabric or clothing are used, it is intended to also include the broad term textile.

[0046] Variant

[0047] The term "variant" means a polypeptide having lipase activity that contains single or multiple amino acid substitutions, deletions, and / or insertions at one or more (e.g., several) positions of a parental lipase.

[0048] Washing liquor

[0049] The term "washing liquor" refers to an aqueous solution containing a detergent composition in a diluted form, such as but not limited to a detergent solution containing a laundry detergent composition in a diluted form, such as the washing liquor in the process of laundry washing.

[0050] Washing performance : The ability to remove or reduce clothing stains, especially lipid stains. Detailed Description

[0051] The present invention relates to the use of lipid removal enhancers in detergents, especially laundry detergents. The lipid removal enhancers are selected from the group consisting of lysine, stearoyl lactate, and esters of lysine or arginine. Another aspect of the present invention is the use of the lipid removal enhancers in detergent compositions for removing lipid stains (such as fats and oils), especially for removing lipid stains on textiles.

[0052] The stearoyl lactylate can be used in any available form, but the preferred form is the non-toxic salt of stearoyl lactylate, such as sodium stearoyl lactylate (SLS).

[0053] Both lysine and arginine can exist in two stereoisomeric forms called D and L. In the context of the present invention, when referring to lysine and arginine and esters of amino acids, both D and L forms are encompassed. The present invention also encompasses mixtures of the two isomeric forms in any ratio.

[0054] The preferred lysine esters used as lipid removal enhancers are C 1 to C 5 esters of lysine: methyl, ethyl, 1-propyl, 2-propyl, 1-butyl, 2-butyl, 2-methyl-2-propyl, 2-methylpropyl, pentyl, 1,1-dimethylpropyl, 2,2-dimethylpropyl, 3-methylbutyl, 1-methylbutyl, 1-ethylpropyl, 1,2-methylpropyl, and 2-methylbutyl.

[0055] The preferred arginine esters used as lipid removal enhancers are C 1 to C 5 esters of arginine: methyl, ethyl, 1-propyl, 2-propyl, 1-butyl, 2-butyl, 2-methyl-2-propyl, 2-methylpropyl, pentyl, 1,1-dimethylpropyl, 2,2-dimethylpropyl, 3-methylbutyl, 1-methylbutyl, 1-ethylpropyl, 1,2-methylpropyl, and 2-methylbutyl.

[0056] Preferably, the concentration of the lipid removal enhancer in the detergent is adjusted in such a way that the final concentration of lysine and the esters of lysine and arginine in the wash liquor is in the range of 0.5 mM to 20 mM. In a preferred embodiment, the final concentration of lysine and the esters of lysine and arginine in the wash liquor is in the range of 1 mM to 10 mM.

[0057] Preferably, the concentration of stearoyl lactylate in the detergent is adjusted in such a way that the final concentration in the wash liquor corresponds to sodium stearoyl lactylate in the range of 100 ppm to 400 ppm. In a preferred embodiment, the final concentration in the wash liquor corresponds to sodium stearoyl lactylate in the range of 100 ppm to 300 ppm.

[0058] The effect of using the lipid removal enhancer is to remove or reduce lipid stains (benefit) on textiles during washing, and only very little malodor is generated (risk). The ratio between lipid removal and malodor generation is called the benefit-risk ratio, and both lipid removal and malodor generation can be measured as disclosed in the experimental section.

[0059] In the context of the present invention, when at least the same level of lipid removal (measured as oil or lard removal) is obtained, the malodor is reduced by at least 5-fold, in the range of 5 - 50, preferably at least 10-fold, 15-fold or even 20-fold, compared to the use of lipase. Thus, the benefit-risk ratio is increased by at least the same multiple.

[0060] The dosage of lipase depends on the lipase actually administered, but typically, lipase is administered in the range of 0.1 ppm to 5 ppm (enzyme protein), preferably lipase is administered in the range of 0.1 ppm to 0.4 ppm (enzyme protein).

[0061] The lipid removal enhancer can be used in combination with enzymes in detergents such as amylase, protease, peroxidase, cellulase, β-glucanase, xyloglucanase, hemicellulase, xanthanase, xanthan lyase, lipase, acyltransferase, phospholipase, esterase, laccase, catalase, arylesterase, amylase, α-amylase, glucoamylase, cutinase, pectinase, pectin lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, carrageenase, pullulanase, tannase, arabinosidase, hyaluronidase, chondroitinase, xyloglucanase, xylanase, pectin acetylesterase, polygalacturonase, rhamnogalacturonase, other endo-β-mannanases, exo-β-mannanases (GH5 and / or GH26), lichenase, phosphodiesterase, pectin methyl esterase, cellobiohydrolase, transglutaminase, nuclease, and combinations thereof.

[0062] In particular, the lipid removal enhancer can be used in combination with lipase or cutinase for lipid removal. Suitable lipases and cutinases include those of bacterial or fungal origin. This includes chemically modified mutant enzymes or protein-engineered mutant enzymes. Examples include lipases from Thermomyces, such as the lipase from Thermomyces lanuginosus (formerly named Humicola lanuginosa) as described in EP 258068 and EP 305216; cutinases from Humicola, such as Humicola insolens (WO 96 / 13580); lipases from strains of Pseudomonas (some of these are now renamed Burkholderia), such as Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes (EP 218272), Pseudomonas cepacia (EP 331376), Pseudomonas sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), Pseudomonas wisconsinensis (WO 96 / 12012); GDSL-type Streptomyces lipases (WO 10 / 065455); cutinases from Magnaporthe grisea (WO 10 / 107560); cutinases from Pseudomonas mendocina (US 5,389,536); lipases from Thermobifida fusca (WO 11 / 084412); Geobacillus stearothermophilus lipase (WO 11 / 084417); lipases from Bacillus subtilis (WO 11 / 084599); and lipases from Streptomyces griseus (WO 11 / 150157), Streptomyces pristinaespiralis (WO 12 / 137147) and Pseudomonas mendocina (WO 2022 / 197810). Additionally, lipases from Geotrichum candidum as disclosed in WO 2022 / 162043 can be used.

[0063] When the enzyme is present together with the lipid removal enhancer, the enzyme is present in an amount selected from the group consisting of: 0.002 to 10,000 mg of enzyme protein per liter of wash liquor, 0.005 to 5,000 mg of enzyme protein, 0.01 to 5,000 mg of enzyme protein, 0.05 to 5,000 mg of enzyme protein, 0.05 to 1,500 mg of enzyme protein, 0.1 to 1,000 mg of enzyme protein, 0.1 to 500 mg of enzyme protein, and 0.1 to 100 mg of enzyme protein.

[0064] Detergent composition

[0065] In one embodiment, the present invention relates to detergent compositions that comprise a combination of the lipid removal enhancer of the present invention with one or more additional cleaning composition components. The selection of the additional components is within the ability of the person skilled in the art and includes conventional ingredients, including the exemplary non-limiting components set forth below. Additional optional detergent components include, alone or in combination, corrosion inhibitors, shrinkage inhibitors, anti-soil redeposition agents, anti-wrinkle agents, bactericides, binders, corrosion inhibitors, disintegrants / disintegration reagents, dyes, enzyme stabilizers (including boric acid, borates, CMC, and / or polyols such as propylene glycol), fabric conditioners (including clays), fillers / processing aids, optical brighteners / fluorescent whitening agents, foam boosters, foam (bubble) regulators, fragrances, soil suspending agents, softeners, defoamers, dulling inhibitors, and wicking agents. Any ingredients known in the art for use in laundry detergents can be utilized. The selection of such ingredients is entirely within the skill of the person skilled in the art.

[0066] For textile care, the selection of components can include the following considerations: the type of textile to be cleaned, the type and / or degree of soil, the temperature at which cleaning is carried out, and the formulation of the detergent product. 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 understood by the person skilled in the art, a component can comprise additional functionality.

[0067] In one embodiment, the present invention relates to liquid laundry detergent compositions that comprise a combination of the lipid removal enhancer of the present invention with one or more additional laundry detergent composition components (in particular, proteases). In another embodiment, the present invention encompasses auxiliary products for use in laundry washing, such as pre-spotting agents or soil release boosters. The present invention also relates to ADW (automatic dishwashing) compositions that comprise a combination of the lipid removal enhancer of the present invention with one or more additional ADW composition components. The selection of the additional components is within the ability of the person skilled in the art and includes conventional ingredients, including the exemplary non-limiting components set forth below.

[0068] The concentration of the detergent in the wash liquor can be adjusted according to regional requirements (such as water hardness) and the wash load, but typically the concentration ranges from 0.5 g / L of wash liquor to 5 g / L of wash liquor, particularly in the range from 0.5 g / L of wash liquor to 2.5 g / L of wash liquor, and the detergent composition tends to be more concentrated, so a lower amount of detergent is required per liter of wash liquor.

[0069] Surfactant

[0070] Typically, the detergent composition comprises one or more surfactants (by weight of the composition) in the range of: 0% to 50%, preferably 2% to 40%, more preferably 5% to 35%, more preferably 7% to 30%, most preferably 10% to 25%, even most preferably 15% to 20%. In a preferred embodiment, the detergent is a liquid or powder detergent which comprises less than 40% by weight, preferably less than 30% by weight, more preferably less than 25% by weight, even more preferably less than 20% by weight of surfactant. The composition may comprise 1% to 15% by weight, preferably 2% to 12%, 3% to 10%, most preferably 4% to 8%, even most preferably 4% to 6% of one or more surfactants. Preferred surfactants are anionic surfactants, nonionic surfactants, cationic surfactants, zwitterionic surfactants, amphoteric surfactants and mixtures thereof. Suitable anionic surfactants are well known in the art and may include fatty acid carboxylates (soaps), branched, straight and random chain alkyl sulfates or fatty alcohol sulfates or primary alcohol sulfates or alkylbenzene sulfonates (such as LAS and LAB) or phenylalkanesulfonates or alkenyl sulfonates or alkenylbenzene sulfonates or alkyl ethoxysulfates or fatty alcohol ether sulfates or alpha-olefin sulfonates or dodecenyl / tetradecenyl succinates. The anionic surfactant may be alkoxylated. The detergent composition may also comprise 1 wt% to 10 wt% of a nonionic surfactant, preferably 2 wt% to 8 wt%, more preferably 3 wt% to 7 wt%, even more preferably less than 5 wt% of a nonionic surfactant. Suitable nonionic surfactants are well known in the art and may include alcohol ethoxylates, and / or alkyl ethoxylates, and / or alkylphenol ethoxylates, and / or glucamides (such as fatty acid N-glucosyl N-methylamides), and / or alkyl polyglucosides and / or mono- or diethanolamides or fatty acid amides. The detergent composition may also comprise 0 wt% to 10 wt% of a cationic surfactant, preferably 0.1 wt% to 8 wt%, more preferably 0.5 wt% to 7 wt%, even more preferably less than 5 wt% of a cationic surfactant. Suitable cationic surfactants are well known in the art and may include alkyl quaternary ammonium compounds, and / or alkyl pyridinium compounds and / or alkyl quaternary phosphonium compounds and / or alkyl trithionium compounds. The composition preferably comprises an amount of surfactant which provides 100 ppm to 5,000 ppm surfactant in the wash liquor during a laundry wash. The composition typically forms a wash liquor upon contact with water, the wash liquor comprising 0.5 g / l to 10 g / l of the detergent composition.Many suitable surface-active compounds are available and well described in the literature, e.g., as described by Schwartz, Perry, and Berch in "Surface-Active Agents and Detergents", Volumes I and II. Also preferred are bio-based surfactants, which can be wholly bio-based (bio-based carbon > 95% in total carbon according to European standard EN 17035). As used herein, bio-based surfactants are composed entirely or mostly of biological products or renewable agricultural or forestry materials and / or commercial or industrial products (other than food or feed) established by European standard EN 16575:2014. In particular, rhamnolipids and sophorolipids can be used as detergent components.

[0071] Solvent system

[0072] To dissolve the surfactant and other detergent components, a solvent system is required. Solvents are typically water, alcohols, polyols, sugars, and / or mixtures thereof. Preferred solvents are water, glycerol, sorbitol, propylene glycol (MPG, 1,2-propylene glycol or 1,3-propylene glycol), dipropylene glycol (DPG), polyethylene glycol family (PEG300 - 600), hexylene glycol, inositol, mannitol, ethanol, isopropanol, n-butoxypropoxypropanol, ethanolamines (monoethanolamine, diethanolamine, and triethanolamine), sucrose, dextrose, glucose, ribose, xylose, and related mono- and di-pyranosides and furanosides. The solvent system is typically present in a total amount of 5% - 90%, 5% - 60%, 5% - 40%, 10% - 30% by weight.

[0073] Hydrotrope

[0074] Hydrotropes are compounds that dissolve hydrophobic compounds in an aqueous solution (or conversely, dissolve polar substances in a non-polar environment). Typically, hydrotropes have both hydrophilic and hydrophobic characteristics (the so-called amphiphilic properties known from surfactants), however, the molecular structure of hydrotropes generally does not favor spontaneous self-aggregation, see e.g., the review by Hodgdon and Kaler (2007), Current Opinion in Colloid & Interface Science 12:121 - 128. Detergents can contain 0% - 10% by weight, such as 0% - 5% by weight, or about 0.5% to about 5%, or about 3% to about 5% of hydrotropes.

[0075] Builders and cobuilders

[0076] The detergent composition may contain from about 0% to 65%, 0% to 20%; or 0.5% to 5% of a detergent builder or cobuilder, or a mixture thereof. In dishwashing detergents, the level of builder is typically 10% to 65%, especially 20% to 40%. The builder and / or cobuilder can be, in particular, a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and / or cobuilder known in the art for use in laundry detergents can be utilized.

[0077] Bleaching system

[0078] The detergent may contain from 0% to 30% by weight, such as from about 1% to about 20% of a bleaching system. Any bleaching system known in the art for use in laundry detergents can be utilized.

[0079] Polymer

[0080] The detergent may contain from 0% to 10% by weight, such as 0.5% to 5%, 2% to 5%, 0.5% to 2%, or 0.2% to 1% of a polymer. Any polymer known in the art for use in detergents can be utilized. The polymer can act as a cobuilder as mentioned above, or can provide anti-redeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning, and / or defoaming properties. Some polymers can have more than one of the above-mentioned properties and / or more than one of the motifs mentioned below.

[0081] Fabric toner

[0082] The detergent composition of the present invention may further include a fabric toner, such as a dye or pigment, which can be deposited on the fabric when the fabric comes into contact with the wash liquor containing the detergent composition when formulated in the detergent composition, and thus changes the color of the fabric by absorption / reflection of visible light.

[0083] Dispersant

[0084] The detergent composition of the present invention may also contain a dispersant. In particular, powdered detergents may contain a dispersant. Suitable water-soluble organic materials include homopolymeric or copolymeric acids or their salts, where the polycarboxylic acid contains at least two carboxyl groups separated from each other by no more than two carbon atoms. Suitable dispersants are described, for example, in Powdered Detergents, Surfactant science series, Volume 71, Marcel Dekker, Inc.

[0085] Dye transfer inhibitor

[0086] The detergent composition of the present invention may further comprise one or more dye transfer inhibitors. Suitable polymeric dye transfer inhibitors include, but are not limited to, polyvinylpyrrolidone polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinyl oxazolidone and polyvinylimidazole, or mixtures thereof. When present in the subject composition, the dye transfer inhibitor may be present at a level of from about 0.0001% to about 10%, from about 0.01% to about 5%, or even from about 0.1% to about 3% by weight of the composition.

[0087] Soil release polymer

[0088] The detergent composition of the present invention may further comprise one or more soil release polymers which assist in removing soil from fabrics such as cotton and polyester-based fabrics, particularly hydrophobic soil from polyester-based fabrics. Soil release polymers can be, for example, polymers based on nonionic or anionic terephthalic acid, polyvinylcaprolactam and related copolymers, vinyl graft copolymers, polyester polyamides, see, for example, Powdered Detergents, Surfactant science series, Volume 71, Chapter 7, Marcel Dekker, Inc. Another type of soil release polymer is an amphiphilic alkoxylated oil soil cleaning polymer comprising a core structure and a plurality of alkoxylated groups attached to the core structure. The core structure can comprise a polyalkylimine structure or a polyalkanolamine structure, as detailed in WO 2009 / 087523 (incorporated herein by reference). In addition, random graft copolymers are suitable soil release polymers. Suitable graft copolymers are described in more detail in WO2007 / 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 those described in EP1867808 or WO 2003 / 040279 (both incorporated herein by reference). Suitable cellulose polymers include cellulose, cellulose ethers, cellulose esters, cellulose amides, and mixtures thereof. Suitable cellulose polymers include anionically modified cellulose, nonionically modified cellulose, cationically modified cellulose, zwitterionically modified cellulose, and mixtures thereof. Suitable cellulose polymers include methyl cellulose, carboxymethyl cellulose, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, ester carboxymethyl cellulose, and mixtures thereof.

[0089] Antiredeposition agent

[0090] The detergent composition of the present invention may further comprise one or more anti - redeposition agents such as carboxymethyl cellulose (CMC), polyvinyl alcohol (PVA), polyvinylpyrrolidone (PVP), polyethylene oxide and / or polyethylene glycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, and ethoxylated polyethyleneimine. The cellulose - based polymers described above under soil - releasing polymers may also act as anti - redeposition agents.

[0091] Rheology modifier

[0092] Rheology modifiers are structurants or thickeners, different from viscosity reducers. Rheology modifiers are selected from the group consisting of: non - polymeric crystals, hydroxy - functional materials, polymeric rheology modifiers, which impart shear - thinning characteristics to the aqueous liquid matrix of the liquid detergent composition. The rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example, as shown in EP 2169040.

[0093] Other suitable adjuvant materials

[0094] Other auxiliary agent materials include but are not limited to shrink - proofing agents, anti - wrinkle agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, fragrances, pigments, and defoaming agents.

[0095] Additional enzymes

[0096] The detergent additive together with the detergent composition may comprise one or more [additional] enzymes such as hydrolases (EC 3.-.-.-), such as hydrolases acting on ester bonds (EC 3.1.-.-), glycosidases (EC 3.2.-.-), and hydrolases acting on peptide bonds (EC 3.4.-.-), oxidoreductases (EC 1.-.-.-), such as laccase (EC 1.10.-.-) or peroxidase (EC 1.11.-.-), or lyases (EC 4.-.-.-), such as carbon - oxygen lyases (EC 4.2.-.-). In certain embodiments, the detergent composition may comprise one or more enzymes such as protease, lipase, cutinase, amylase, carbohydrase, cellulase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase (e.g., laccase), and / or peroxidase.

[0097] Generally, the properties of the one or more enzymes selected should be compatible with the selected detergent (i.e., optimal pH, compatibility with other enzyme components or non - enzyme components, etc.), and the one or more enzymes should be present in an effective amount.

[0098] Cellulase

[0099] Suitable additional cellulases include those of bacterial or fungal origin. This includes chemically modified mutants or protein-engineered mutants. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, and Acremonium, such as the fungal cellulases produced by Humicola insolens, Myceliophthora thermophila, and Fusarium oxysporum as disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, and WO 89 / 09259.

[0100] Mannanase

[0101] Mannanases have endo-1,4-β-mannosidase activity (EC 3.2.1.78) for catalyzing the hydrolysis of 1,4-β-D-mannosidic linkages in mannans, galactomannans, and glucomannans. According to CAZy (www.cazy.org), endo-1,4-β-mannanases have been found in glycoside hydrolase families 5, 26, and 113. Suitable mannanases include those of bacterial or fungal origin. This includes chemically or genetically modified mutants. The mannanase can be an alkaline mannanase of family 5 or 26. It can be a wild type from the genus Bacillus or Humicola, in particular Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, or Humicola insolens. Suitable mannanases are described in WO 1999 / 064619. A commercially available mannanase is Mannaway (Novozymes A / S).

[0102] Protease

[0103] A protease is an enzyme that hydrolyzes peptide bonds. It includes any enzyme belonging to the EC 3.4 enzyme group (including each of its thirteen subclasses) (http: / / en.wikipedia.org / wiki / Category:EC_3.4). The EC numbers refer to the 1992 Enzyme Nomenclature of the NC-IUBMB in San Diego, California, Academic Press, including Supplements 1-5 published separately in: Eur. J. Biochem. [European Journal of Biochemistry] 1994, 223, 1-5; Eur. J. Biochem. [European Journal of Biochemistry] 1995, 232, 1-6; Eur. J. Biochem. [European Journal of Biochemistry] 1996, 237, 1-5; Eur. J. Biochem. [European Journal of Biochemistry] 1997, 250, 1-6; and Eur. J. Biochem. [European Journal of Biochemistry] 1999, 264, 610-650. The term "subtilisin" refers to the subgroup of serine proteases according to Siezen et al., Protein Eng. [Protein Engineering] 4 (1991) 719-737 and Siezen et al., Protein Science [Protein Science] 6 (1997) 501-523. Serine proteases or serine peptidases are a subgroup of proteases characterized by having a serine at the active site that forms a covalent adduct with the substrate. Additionally, subtilisins (and serine proteases) are characterized by having, in addition to serine, two active site amino acid residues, namely histidine and aspartic acid residues. Subtilisins can be divided into six subclasses, namely, the subtilisin protease family, the thermitase family, the proteinase K family, the lantibiotic peptidase family, the kexin family, and the pyrolysin family. The term "protease activity" means proteolytic activity (EC 3.4).

[0104] Suitable proteases include those from bacterial, fungal, plant, viral or animal sources, such as plant or microbial sources. Microbial sources are preferred. Include chemically modified mutants or protein-engineered mutants. It can be an alkaline protease, such as a serine protease or a metalloprotease. Serine proteases can be, for example, of the S1 family (such as trypsin) or the S8 family (such as subtilisin). Metalloproteases can be, for example, thermolysin from the M4 family or other metalloproteases, such as those from the M5, M7 or M8 families.

[0105] Lipase and cutinase

[0106] Suitable lipases and cutinases include those of bacterial or fungal origin. This includes chemically modified mutant enzymes or protein-engineered mutant enzymes. Examples include lipases from Thermomyces, such as those from Thermomyces lanuginosus (formerly Humicola lanuginosa) as described in EP 258068 and EP305216; cutinases from Humicola, such as Humicola insolens (WO 96 / 13580); lipases from strains of the genus Pseudomonas (some of these are now reclassified as Burkholderia), such as Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes (EP 218272), Pseudomonas cepacia (EP331376), Pseudomonas sp. strain SD705 (WO 95 / 06720 and WO 96 / 27002), Pseudomonas wisconsinensis (WO96 / 12012); GDSL-type Streptomyces lipases (WO 10 / 065455); cutinases from Magnaporthe oryzae (WO10 / 107560); cutinases from Pseudomonas mendocina (US 5,389,536); lipases from Thermomyces lanuginosus (WO 11 / 084412); Geobacillus stearothermophilus lipases (WO 11 / 084417); lipases from Bacillus subtilis (WO 11 / 084599); and lipases from Streptomyces griseus (WO 11 / 150157) and Streptomyces pristinaespiralis (WO 12 / 137147). Additionally, lipases from Geotrichum candidum as disclosed in WO 2022 / 162043 can be used.

[0107] Amylase

[0108] Suitable amylases that can be used together with the endoglucanases of the present invention can be α-amylases or glucoamylases and can be of bacterial or fungal origin. This includes chemically modified mutants or protein-engineered mutants. Amylases include, for example, α-amylases obtained from strains of the genus Bacillus, such as specific strains of Bacillus licheniformis (more detailedly described in GB 1,296,839).

[0109] Peroxidase / oxidase

[0110] The peroxidase is a peroxidase included in the enzyme classification EC 1.11.1.7 as elaborated by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom that exhibits peroxidase activity.

[0111] Suitable peroxidases include those of plant, bacterial or fungal origin. This includes chemically modified mutants or protein-engineered mutants. Examples of useful peroxidases include peroxidases from Coprinopsis, such as from Coprinopsis cinerea (EP 179,486), and variants thereof, such as those described in WO 93 / 24618, WO 95 / 10602 and WO 98 / 15257.

[0112] Nuclease

[0113] Suitable nucleases include deoxyribonucleases (DNases) and ribonucleases (RNases), which are any enzymes that catalyze the hydrolytic cleavage of phosphodiester bonds in the DNA or RNA backbone to degrade DNA and RNA, respectively. Preferred DNases can be selected from any of the enzyme classes E.C. 3.1.21.X, where X = 1, 2, 3, 4, 5, 6, 7, 8 or 9.

[0114] DNase polypeptides are typically microbial enzymes, preferably of fungal or bacterial origin, or genetically engineered variants of microbial DNases.

[0115] Lichenase

[0116] Suitable lichenases (lichenanases) include enzymes that catalyze the hydrolysis of β-1,4-glycosidic bonds to produce β-glucans. Lichenases (or lichenanases) (e.g., EC 3.2.1.73) hydrolyze the (1,4)-β-D-glycosidic bonds in β-D-glucans containing (1,3)- and (1,4)-bonds and can act on lichenin and cereal β-D-glucans.

[0117] Xylanase

[0118] Xanthan gum is a natural polysaccharide composed of different sugars that are linked by several different bonds, such as b-D-mannosyl-b-D-1,4-glucuronosyl bonds and b-D-glucosyl-b-D-1,4-glucosyl bonds. Xanthan gum is at least partially soluble in water and forms a highly viscous solution or gel. Complete enzymatic degradation of xanthan gum requires several enzyme activities, including xanthan lyase activity and endo-β-1,4-glucanase activity, preferably a GH9 endoglucanase. Xanthan lyase is an enzyme that cleaves the b-D-mannosyl-b-D-1,4-glucuronosyl bond of xanthan gum, while the GH9 endoglucanase catalyzes the hydrolysis of glycosidic bonds to release smaller sugars.

[0119] Enzyme formulations

[0120] Liquid enzyme formulation

[0121] The lipid removal enhancer of the present invention can be formulated into a liquid enzyme formulation, which is generally a pourable composition, although it may also have a high viscosity. The physical appearance and properties of the liquid enzyme formulation can vary greatly - for example, they may have different viscosities (gel-like to aqueous), colored, uncolored, transparent, hazy, and even have solid particles (such as in slurries and suspensions). The minimum components are the lipid removal enhancer of the present invention that makes it a liquid and the solvent system. In addition to the lipid removal enhancer of the present invention, the liquid enzyme formulation can also contain other enzyme activities, such as protease, amylase, lipase, cellulase, and / or nuclease (e.g., DNase, RNase) activities.

[0122] The solvent system can include water, polyols (such as glycerol, (mono-, di- or tri-) propylene glycol, (mono-, di- or tri-) ethylene glycol, sugar alcohols (e.g., sorbitol, mannitol, erythritol, galactitol, inositol, xylitol or ribitol), polypropylene glycol, and / or polyethylene glycol), ethanol, sugars, and salts. Usually, the solvent system also includes preservatives and / or other stabilizers.

[0123] The liquid enzyme formulation can be prepared by mixing the solvent system and an enzyme concentrate (or enzyme particles to obtain a slurry / suspension) with the desired purity.

[0124] In an embodiment, the liquid enzyme composition comprises:

[0125] (a) at least 0.01% w / w active enzyme protein,

[0126] (b) at least 0.5% w / w polyol,

[0127] (c) water, and

[0128] (d) optionally a preservative.

[0129] The lipid removal enhancer of the present invention in the liquid composition of the present invention can be stabilized using conventional stabilizers. Examples of stabilizers include but are not limited to sugars, such as glucose, fructose, sucrose, or trehalose; adding salts to increase the ionic strength; divalent cations (e.g., Ca 2+ or Mg 2+ ); and enzyme inhibitors, enzyme substrates, or various polymers (e.g., PVP). Selecting the optimal pH for the formulation can be very important for enzyme stability. The optimal pH depends on the specific enzyme but is generally in the range of pH 4 - 9. In some cases, surfactants such as nonionic surfactants (e.g., alcohol ethoxylates) can improve the physical stability of the enzyme formulation.

[0130] One embodiment of the present invention relates to a composition comprising a lipid removal enhancer of the present invention, wherein the composition further comprises:

[0131] (i) a polyol, preferably selected from glycerol, (mono-, di- or tri-) propylene glycol, (mono-, di- or tri-) ethylene glycol, polyethylene glycol, sugar alcohols, sorbitol, mannitol, erythritol, galactitol, inositol, xylitol and ribitol;

[0132] (ii) optionally an additional enzyme, preferably selected from proteases, amylases or lipases,

[0133] (iii) optionally a surfactant, preferably selected from anionic and nonionic surfactants,

[0134] (iv) optionally a divalent cation, a polymer, or an enzyme inhibitor.

[0135] (v) optionally having a pH in the range of 4 - 9; and

[0136] (vi) water.

[0137] A slurry or dispersant of an enzyme is typically prepared by dispersing small particles of the enzyme (e.g., spray-dried particles) in a liquid medium in which the enzyme is slightly soluble (e.g., a liquid nonionic surfactant or a liquid polyethylene glycol). The powder can also be added in an amount to an aqueous system so that not all of it goes into solution (above the solubility limit). Another form is a crystal suspension, which can also be an aqueous liquid (see, for example, WO 2019 / 002356). Another method of preparing such a dispersant is by preparing a water-in-oil emulsion, where the enzyme is in the aqueous phase and water is evaporated from the droplets. Such a slurry / suspension can be physically stabilized (to reduce or avoid sedimentation) by adding a rheology modifier (such as fumed silica or xanthan gum), typically to achieve shear-thinning rheology.

[0138] Granular enzyme formulation

[0139] The lipid removal enhancer of the present invention can also be formulated with enzymes into a solid / granular enzyme formulation. Dust-free granules can be produced, for example, as disclosed in US 4,106,991 and US 4,661,452, and can optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycol, PEG) with an average molecular weight of 1000 to 20000; ethoxylated nonylphenols having 16 to 50 ethylene oxide units; ethoxylated fatty alcohols, where the alcohol contains 12 to 20 carbon atoms and where there are 15 to 80 ethylene oxide units; fatty alcohols; fatty acids; and mono-, di-, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluidized bed techniques are given in GB 1483591.

[0140] The lipid removal enhancer of the present invention can be formulated as granules, for example as co-granules combining the lipid removal enhancer with an enzyme or a beneficial agent such as MnTACN or other bleaching components. Examples of such additional enzymes include proteases, amylases, lipases, cellulases, and / or nucleases (such as DNases, RNases). Then, each enzyme will be present in a plurality of granules, which ensure a more uniform distribution of the enzyme in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes. A method for producing multi-enzyme co-granules for the detergent industry is disclosed in IP.com Disclosure IPCOM000200739D.

[0141] Examples of the present invention relate to enzyme granules / particles comprising the lipid removal enhancer of the present invention. The granules consist of a core and optionally one or more coatings (outer layers) surrounding the core. Typically, the granule / particle size of the granules (measured as the equivalent spherical diameter (volume-based average particle size)) is 20 - 2000 μm, especially 50 - 1500 μm, 100 - 1500 μm or 250 - 1200 μm.

[0142] The core may include additional materials such as fillers, fibrous materials (cellulose or synthetic fibers), stabilizers, solubilizers, suspending agents, viscosity modifiers, light spheres, plasticizers, salts, lubricants, and fragrances. The core may include binders such as synthetic polymers, waxes, fats, or carbohydrates. The core typically contains salts of polyvalent cations, reducing agents, antioxidants, peroxide decomposition catalysts, and / or acidic buffer components as a homogeneous blend. The core may consist of inert particles onto which the enzyme is adsorbed or to the surface of which the enzyme is applied (e.g., by fluidized bed coating). The diameter of the core may be 20 - 2000 μm, especially 50 - 1500 μm, 100 - 1500 μm, or 250 - 1200 μm. The core may be prepared by blending granulating components, for example, by methods including granulation techniques such as crystallization, precipitation, pan - coating, fluidized bed coating, fluidized bed agglomeration, rotary atomization, extrusion, prilling, spheronization, particle size reduction methods, drum granulation, and / or high - shear granulation. Methods for preparing the core can be found in Handbook of Powder Technology; Particle size enlargement by C.E. Capes; Volume 1; 1980; Elsevier. These methods are well - known in the art and have also been described in International Patent Application WO 2015 / 028567, pages 3 - 5, which is incorporated by reference.

[0143] The core of the enzyme granule / particle may be surrounded by at least one coating, for example, to improve storage stability, to reduce dust formation during handling, or for coloring the granule. Optional coatings may include salt coatings or other suitable coating materials such as polyethylene glycol (PEG), methylhydroxy - propylcellulose (MHPC), and polyvinyl alcohol (PVA). Examples of enzyme granules with multiple coatings are shown in WO 93 / 07263 and WO 97 / 23606.

[0144] Such coatings are well - known in the art and have been described previously, for example, in WO 00 / 01793, WO 2001 / 025412, and WO 2015 / 028567, which are incorporated by reference.

[0145] In one aspect, the present invention provides a granule comprising:

[0146] (a) a core containing the lipid - removing enhancer of the present invention and optionally one or more enzymes; and

[0147] (b) Optionally, a (salt) coating consisting of one or more layers surrounding the core.

[0148] Another aspect of the present invention relates to a layered particle comprising:

[0149] (a) A (non - enzyme) core;

[0150] (b) A coating surrounding the core, wherein the coating contains an enzyme;

[0151] (c) Optionally, a (salt) coating consisting of one or more layers surrounding the enzyme - containing coating; and

[0152] (d) The lipid - removal enhancer of the present invention in any one of (a) to (c) above.

[0153] Encapsulated enzyme formulation

[0154] The lipid - removal enhancer of the present invention can also be formulated as part of an encapsulated enzyme formulation ("encapsulate"). This is particularly useful for separating the enzyme from other components when the enzyme is added to, for example, a (liquid) cleaning composition (such as the detergent compositions described below).

[0155] Physical separation can be used to address incompatibilities between one or more enzymes and other components. Incompatibilities can occur if other components react with the enzyme or if other components are substrates of the enzyme. Other enzymes can be substrates of proteases.

[0156] The enzyme can be encapsulated in a matrix, preferably a water - soluble or water - dispersible matrix (such as water - soluble polymer particles), as described in, for example, WO 2016 / 023685. Examples of water - soluble polymer matrices are matrix compositions containing polyvinyl alcohol. Such compositions are also used to encapsulate detergent compositions in unit - dose formats.

[0157] The enzyme can also be encapsulated in core - shell microcapsules, such as those described in WO 2015 / 144784, or described in the IP.com disclosure IPCOM000239419D.

[0158] A variety of techniques known in the art can be used to prepare such core - shell capsules. For example, interfacial polymerization using water - in - oil or oil - in - water emulsions, where the polymer cross - links at the surface of the droplets in the emulsion (the interface between water and oil), thus forming a wall / membrane around each droplet / capsule.

[0159] Unit dose detergents is a generic term covering detergents delivered in single use forms; these can be poly(vinyl alcohol) bags containing liquid or powder detergents in single or multiple chambers, the single or multiple chambers being either all liquid chambers or a mixed model with both liquid and powder chambers. Unit dose detergents can also be compressed tablets with one or more layers (“phases”). Relative to typical mass fraction levels in aqueous HDL, unit dose liquid laundry compositions generally have low water content (<10% w / w); high surfactant content (50% to 65%); and high solvent content (15% to 30% polyol).

[0160] Purification of enzyme in formulation

[0161] The enzymes used in the above enzyme formulations can be purified to any desired purity. This includes high levels of purification, for example achieved by using crystallization methods, but also includes no purification or low levels of purification, for example achieved by using crude fermentation broths, as described in WO 2001 / 025411 or WO 2009 / 152176.

[0162] Formulation of Detergent Products

[0163] The detergent compositions of the present invention can be in any conventional form, such as bars, uniform tablets, tablets with two or more layers, bags with one or more chambers, regular or compressed powders, granules, pastes, gels, or regular, compressed or concentrated liquids.

[0164] One or more detergent enzymes can be included in the detergent composition by adding a separate additive containing one or more enzymes, or by adding a combined additive containing all of these enzymes. The detergent additives of the present invention, i.e., separate additives or combined additives, can be formulated, for example, as granules, liquids, slurries, etc. Preferred detergent additive formulations are granules, particularly dust-free granules; liquids, particularly stabilized liquids; or slurries.

[0165] Dust-free particles can be produced, for example, as disclosed in US 4,106,991 and 4,661,452 and can optionally be coated by methods known in the art. Examples of waxy coating materials are poly(ethylene oxide) products (polyethylene glycol, PEG) with an average molecular weight of 1000 to 20000; ethoxylated nonylphenols having 16 to 50 ethylene oxide units; ethoxylated fatty alcohols, where the alcohol contains 12 to 20 carbon atoms and where 15 to 80 ethylene oxide units are present; fatty alcohols; fatty acids; and monoglycerides, diglycerides, and triglycerides of fatty acids. Examples of film-forming coating materials suitable for application by fluidized bed techniques are given in GB 1483591. Liquid enzyme preparations can be stabilized, for example, by adding polyols (such as propylene glycol), sugars or sugar alcohols, lactic acid or boric acid according to established methods. Protected enzymes can be prepared according to the method disclosed in EP 238,216.

[0166] The pouch can be configured as a single chamber or multiple chambers. It can have any form, shape, and material suitable for holding the composition, for example, not allowing the composition to be released from the pouch before contact with water. The pouch is made of a water-soluble film that encloses the internal volume. The internal volume can be divided into chambers of the pouch. Preferred films are polymeric materials, preferably polymers that form films or sheets. Preferred polymers, copolymers, or derivatives thereof are selected from polyacrylates, and water-soluble acrylate copolymers, methylcellulose, carboxymethylcellulose, sodium dextrin, ethylcellulose, hydroxyethylcellulose, hydroxypropylmethylcellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers and hydroxypropylmethylcellulose (HPMC). Preferably, the level of polymer in the film, such as PVA, is at least about 60%. The preferred average molecular weight will typically be about 20,000 to about 150,000. The film can also be a blend composition that contains a hydrolyzable and water-soluble polymer blend, such as polylactic acid and polyvinyl alcohol (known under trade reference number M8630, as sold by MonoSol LLC, Indiana, USA) plus plasticizers like glycerol, ethylene glycol, propylene glycol, sorbitol, and mixtures thereof. The pouch can contain a solid laundry cleaning composition or partial components and / or a liquid cleaning composition or partial components separated by a water-soluble film. The chamber for the liquid component can be different in composition from the chamber containing the solid. Reference: (US2009 / 0011970 A1).

[0167] The detergent components can be physically separated from each other by chambers in a water-soluble pouch or in different layers of a tablet. Thus, adverse storage interactions between components can be avoided. In the washing solution, different dissolution profiles for each chamber can also cause delayed dissolution of the selected components.

[0168] 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, diols, ethers, and polyols can be included in the aqueous liquid or gel. The aqueous liquid or gel detergent can contain 0%-30% organic solvent. The liquid or gel detergent can be non-aqueous.

[0169] Use in detergents.

[0170] The lipid removal enhancer of the present invention can be added to a detergent composition and thus made a component of the detergent composition.

[0171] The detergent composition of the present invention can be formulated as, for example, a hand or machine laundry detergent composition, the composition including a laundry additive composition suitable for pre-treating stained fabrics or for restoring textiles (e.g., by removing fuzz or pills) to restore some of the visual and tactile properties of the fabric after long-term use to be comparable to new textiles, and a rinse-added fabric softener composition, or be formulated as a detergent composition for general household hard surface cleaning operations, or be formulated for hand or machine dishwashing operations.

[0172] In certain aspects, the present invention provides a detergent additive comprising the lipid removal enhancer of the present invention as described herein.

[0173] Examples

[0174] The present invention is further described in the following examples:

[0175] 1) A detergent composition comprising:

[0176] a. At least one detergent component;

[0177] b. A lipid removal enhancer selected from the group consisting of lysine, stearoyl lactylate, C 1 to C 5 esters of lysine and C 1 to C 5 esters of arginine

[0178] c. Optionally one or more enzymes.

[0179] 2) The composition according to Example 1, wherein the composition is a laundry detergent composition.

[0180] 3) The composition according to embodiment 1(b), wherein the lipid removal enhancer is selected from the group consisting of: methyl ester of lysine, ethyl ester of lysine, 1-propyl ester of lysine, 2-propyl ester of lysine, 1-butyl ester of lysine, 2-butyl ester of lysine, 2-methyl-2-propyl ester of lysine, 2-methylpropyl ester of lysine, pentyl ester of lysine, 1,1-dimethylpropyl ester of lysine, 2,2-dimethylpropyl ester of lysine, 3-methylbutyl ester of lysine, 1-methylbutyl ester of lysine, 1-ethylpropyl ester of lysine, 1,2-methylpropyl ester of lysine, and 2-methylbutyl ester of lysine.

[0181] 4) The composition according to embodiment 1(b), wherein the lipid removal enhancer is selected from the group consisting of: methyl ester of arginine, ethyl ester of arginine, 1-propyl ester of arginine, 2-propyl ester of arginine, 1-butyl ester of arginine, 2-butyl ester of arginine, 2-methyl-2-propyl ester of arginine, 2-methylpropyl ester of arginine, pentyl ester of arginine, 1,1-dimethylpropyl ester of arginine, 2,2-dimethylpropyl ester of arginine, 3-methylbutyl ester of arginine, 1-methylbutyl ester of arginine, 1-ethylpropyl ester of arginine, 1,2-methylpropyl ester of arginine, and 2-methylbutyl ester of arginine.

[0182] 5) The composition according to embodiment 1(b), wherein the lipid removal enhancer is lysine.

[0183] 6) The composition according to embodiment 1(b), wherein the lipid removal enhancer is stearoyl lactate.

[0184] 7) The composition according to embodiment 1, wherein the detergent composition comprises one or more enzymes selected from the group consisting of: lipase, protease, peroxidase, cellulase, β-glucanase, xyloglucanase, hemicellulase, xylanase, xanthanase, xanthan lyase, amylase, acyltransferase, phospholipase, esterase, laccase, catalase, arylesterase, amylase, α-amylase, glucoamylase, cutinase, pectinase, pectin lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, carrageenase, pullulanase, tannase, arabinosidase, hyaluronidase, chondroitinase, xyloglucanase, xylanase, pectin acetylesterase, polygalacturonase, rhamnogalacturonase, other endo-β-mannanases, exo-β-mannanases (GH5 and / or GH26), lichenase, phosphodiesterase, pectin methyl esterase, cellobiohydrolase, transglutaminase, nuclease, and combinations thereof, or any mixture thereof.

[0185] 8) The composition according to embodiment 7, wherein the enzyme is lipase and / or protease.

[0186] 9) Use of the detergent composition according to any one of embodiments 1 to 8 for cleaning a surface such as a textile, the use comprising contacting the surface with the detergent composition.

[0187] 10) A method for cleaning a surface such as a textile, the method comprising contacting the surface with a detergent composition according to any one of embodiments 1 to 8.

[0188] 11) The composition according to embodiment 3, wherein the concentration of the lysine ester is adjusted to obtain a final concentration of the lysine ester in the wash liquor in the range of 0.5 mM to 20 mM, preferably a final concentration in the wash liquor in the range of 1 mM to 10 mM.

[0189] 12) The composition according to embodiment 4, wherein the concentration of the arginine ester is adjusted to obtain a final concentration of the arginine ester in the wash liquor in the range of 0.5 mM to 20 mM, preferably a final concentration in the wash liquor in the range of 1 mM to 10 mM.

[0190] 13) The composition according to embodiment 5, wherein the concentration of lysine is adjusted to obtain a final concentration of the lysine in the wash liquor in the range of 0.5 mM to 20 mM, preferably a final concentration in the wash liquor in the range of 1 mM to 10 mM.

[0191] 14) The composition according to embodiment 6, wherein the concentration of the stearoyl lactate ester is adjusted to obtain a final concentration of the stearoyl lactate ester in the wash liquor corresponding to sodium stearoyl lactate in the range of 100 ppm to 400 ppm, preferably a final concentration in the wash liquor corresponding to sodium stearoyl lactate in the range of 100 ppm to 300 ppm.

[0192] 15) The composition according to embodiments 3 to 5, wherein the lysine and arginine are in the L-form, D-form or a mixture of L-form and D-form in any ratio.

[0193] 16) The composition according to embodiment 1, the composition comprising more than one lipase removal enhancer.

[0194] 17) The composition according to any one of embodiments 1 to 8 or 11 to 16, wherein no lipase is present.

[0195] 18) Use of the composition according to any one of embodiments 1 to 8 or 11 to 17 for improving the benefit-risk ratio of a detergent composition.

[0196] 19) The composition according to any one of embodiments 1 to 8 and 11 to 16 or the use according to any one of embodiments 9, 10 and 18, wherein the lipase, if present, has at least 60%, such as at least 70%, 80%, 85%, 90%, 95%, even 100% sequence identity with any one of lipases of SEQ ID NO:1 or SEQ ID NO:2.

[0197] Example

[0198] Materials and methods

[0199] The following materials and methods were used in the laundry experiments:

[0200] Determination of lipase activity by p-nitrophenyl (pNP) assay

[0201] The hydrolytic activity of lipase can be determined by a kinetic assay using p-nitrophenyl acyl esters as substrates. Each of the substrates p-nitrophenyl butyrate (C4), p-nitrophenyl caproate (C6), p-nitrophenyl decanoate (C10), p-nitrophenyl laurate (C12), and p-nitrophenyl palmitate (C16) (all from Sigma-Aldrich Danmark A / S, Kirkebjerg Allé 84, 2605 Catalog numbers: C3: N-9876, C6: N-0502, C10: N-0252, C12: N-2002, C16: N-2752) in 100 mM stock solutions in DMSO were diluted to a final concentration of 1 mM - 25 mM in assay buffer (50 mM Tris; pH 7.7; 0.4% Triton X 100). In a 96-well NUNC plate (catalog number 260836, Kamstrupvej 90, DK-4000, Roskilde), lipase in 50 mM Hepes; pH 8.0; 10 ppm Triton X-100; + / - 20 mM CaCl2 was added to the substrate solution at the following final protein concentrations: 0.01 mg / ml; 5 x 10 -3 mg / ml; 2.5 x 10 -4 mg / ml; and 1.25 x 10 -4 mg / ml. The p-nitrophenol released by p-nitrophenyl acyl hydrolysis was monitored at 405 nm at 10-second intervals for 5 minutes on a Spectra max 190 (Molecular Devices GmbH, Bismarckring 39, 88400 Biberach an der Riss, Germany).

[0202] Standard detergent

[0203] Two standard detergents have been applied, one containing LAS and one without LAS

[0204] Compound Content of compound (% w / w) Sodium lauryl sulfate (SLS) 2.5 Sodium laureth sulfate (SLES) 8.5 Cocoa soap 4.3 Alcohol ethoxylate (AEO, plant source) 17 <![CDATA[H 2 O(6°dH)]]> Added to 100

[0205] Table 1: Standard detergent I

[0206] Compound Content of compound (% w / w) Linear alkylbenzene sulfonate (LAS) 5 Sodium laureth sulfate (SLES) 10 Alcohol sulfate (AS) 5 Cocoa soap 1 Alcohol ethoxylate 5 <![CDATA[H 2 O(6°dH)]]> Added to 100

[0207] Table 2: Standard Detergent II

[0208] Lipase

[0209] Lipase L1: Thermomyces lanuginosus lipase (TLL) shown in SEQ ID NO:1, which has the following substitutions: T231R + N233R (available from Novozymes A / S, Denmark).

[0210] Lipase LE2: 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 (available from Novozymes A / S, Denmark);

[0211] Lipase GCL1 is a lipase from Geotrichum candidum shown in SEQ ID NO:2

[0212] Textile

[0213] WFK80A, 5 x 5 cm, white or blue knitted cotton fabric sample (obtained from Warwick Equest, Unit 55, Consett Business Park, Consett, County Durham, DH8 6BN, UK)

[0214] CS - 10 (butterfat) stain was obtained from Center For Testmaterials BV, P.O. Box 120, 3133 KT Vlaardingen, the Netherlands.

[0215] Oilcloth sample

[0216] An oil - cloth sample was prepared by adding 25 μL of pure coconut oil to a circular blue WFK80A textile with a diameter of 2 cm, and it was dried, then weighed using a balance for calculating oil removal.

[0217] Lardcloth sample

[0218] For the Mini-LOM method: A lard cloth sample was prepared by melting 25 μL of pure lard and adding it to a circular blue WFK80A textile piece with a diameter of 2 cm, and it was dried, then weighed using a balance for calculating lard removal.

[0219] For TOM: A lard cloth sample was prepared by melting 100 μL of pure lard and adding it to a 5 x 5 cm blue WFK80A textile, and it was dried, then weighed using a balance for calculating lard removal.

[0220] CS-10 cloth sample

[0221] For the Mini-LOM method: A circular cloth sample with a diameter of 2 cm was punched out from a 5 x 5 cm normal cloth sample size to prepare a CS-10 cloth sample (CFT), which was used for odor measurement.

[0222] For TOM: The CS-10 cloth sample (CFT) was used in the washing with a 5 x 5 cm cloth sample size and punched out for odor measurement.

[0223] Lipid removal enhancer

[0224] L-Lysine methyl ester dihydrochloride (CAS No.: 26348-70-9)

[0225] L-Arginine ethyl ester dihydrochloride (CAS No.: 28696-31-3)

[0226] L-Arginine tert-butyl ester dihydrochloride (CAS No.: 87553-73-9)

[0227] L-Lysine (CAS No.: 56-87-1)

[0228] L-Arginine (CAS No.: 1119-34-2)

[0229] Sodium stearoyl lactate (CAS No.: 25383-99-7)

[0230] For ease of reference, the lipid removal enhancer may hereinafter be referred to as

[0231] · Lysine methyl ester

[0232] · Arginine ethyl ester

[0233] · Arginine tert-butyl ester

[0234] · Lysine

[0235] · Arginine

[0236] · SSL

[0237] Washing conditions Mini-LOM-method, standard detergent level

[0238] A washing solution was prepared by dissolving 2.33 g of a standard detergent in 1 L of water having a hardness of 6 °dH. 40 mL of the washing solution was added to a 50 mL test tube.

[0239] Lipase and / or lipid removal enhancer was added to the washing solution according to the table in the example, and then 10 steel balls (5 mm in diameter) / tube and 4 oilcloth samples, 2 CS-10 cloth samples and 6 ballast cloth samples were added to the washing solution.

[0240] The cloth samples were added, and then continuously stirred at 40 rpm for 25 minutes at 20 °C. Rinse with cold water under the faucet in a beaker for 5 min.

[0241] After washing, the cloth samples were dried on filter paper.

[0242] Washing conditions Mini-LOM-method, low detergent level

[0243] A washing solution was prepared by dissolving 0.93 g of a standard detergent in 1 L of water having a hardness of 6 °dH. 40 mL of the washing solution was added to a 50 mL test tube.

[0244] Lipase and / or lipid removal enhancer was added to the washing solution according to the table in the example, and then 10 steel balls (5 mm in diameter) / tube and 4 oilcloth samples, 2 CS-10 cloth samples and 6 ballast cloth samples were added to the washing solution.

[0245] The cloth samples were added, and then continuously stirred at 40 rpm for 25 minutes at 20 °C. Rinse with cold water under the faucet in a beaker for 5 min.

[0246] After washing, the cloth samples were dried on filter paper.

[0247] Washing conditions Terg-o-tometer (TOM) determination

[0248] WFK80A 5 x 5 cm textile pieces were used as ballast. Lipase and enhancer were added combinatorially or separately according to the table below, and then 4 oil or lard cloth samples and ballast pieces were added to the liquid mixture until 30 g. The cloth samples were added, and then continuously stirred at 120 rpm for 15 minutes at 20 °C. Rinse with cold water under the faucet in a beaker for 5 min.

[0249] After washing, the cloth samples were dried on filter paper.

[0250] Oil removal

[0251] The coconut oil cloth samples were dried for 16 hours, then weighed, and the oil removal was calculated based on subtracting the weight of the cloth sample after washing from the weight before washing.

[0252] Lard removal

[0253] The lard cloth samples were dried for 16 hours, then weighed, and the lard removal was calculated based on subtracting the weight of the cloth sample after washing from the weight before washing.

[0254] Odor measurement

[0255] The CS-10 cloth samples were dried for 16 hours and transferred to a gas chromatography vial. After transfer, the vial was sealed.

[0256] The samples were incubated at 30 °C for 24 hours, then heated to 140 °C for 30 minutes, and stored at 20 °C - 25 °C for at least 4 hours before analysis.

[0257] Analysis was performed on a Shimadzu Nexis GC-2030 equipped with a Carboxen PDMS SPME fiber (85 μm). In the head space of the textile piece, sampling from each GC vial was carried out with the SPME fiber at 50 °C for 8 minutes, and then the sampled compounds were injected onto the column (injector temperature = 250 °C). Column flow rate = 2 mL helium / minute. Column temperature gradient: 1 minute = 50 °C, temperature gradient rate 38 °C / min to the end temperature of 240 °C. Retention time 2.25 min. Detection was carried out using a Flame Ionization Dector (FID), and the retention time of butyric acid was identified using a reliable standard. The area of the butyric acid peak was measured and compared with the area of the butyric acid peak obtained with lipase and without a lipid removal enhancer.

[0258] Example 1. Removal of lipids using lysine methyl ester and lipase L1, standard detergent level (mini-LOM)

[0259] The washing performance (oil removal and odor generation) of lipase L1 and lysine methyl ester was measured according to the method with the standard detergent level and the further conditions listed in Table 3 below:

[0260]

[0261]

[0262] Table 3: Removal of lipids at the standard detergent level using a combination of lysine methyl ester and lipase L1.

[0263] Clearly, lysine methyl ester enhances the action of lipase with L1, and at the same time, it unexpectedly becomes apparent that the same level of oil removal can be achieved using 1 mM lysine methyl ester as using lipase, but the production of odor is significantly reduced, thus resulting in an improved benefit - risk ratio.

[0264] It is further noted that the combination of lipase and lysine methyl ester reduces the formation of butyric acid and thus improves the benefit - risk ratio.

[0265] Example 2. Removal of lipids using lysine methyl ester and lipase GCL1, low detergent level (mini - LOM)

[0266] Measure the washing performance (oil removal and odor production) of lipase GCL1 and lysine methyl ester according to the method using low detergent level described above and the further conditions listed in Table 4 below:

[0267]

[0268] Table 4: Removal of lipids using a combination of lysine methyl ester and lipase GCL1 at low detergent level.

[0269] Clearly, lysine methyl ester enhances the action of lipase GCL1, and at the same time, it unexpectedly becomes apparent that a higher level of oil removal can be achieved using 10 mM lysine methyl ester compared to using lipase, but the production of odor is significantly reduced, thus resulting in an improved benefit - risk ratio.

[0270] It is further noted that the combination of lipase and lysine methyl ester does not change the level of butyric acid formation compared to using lipase alone. However, this should be considered in view of the fact that the oil removal has increased almost 4 - fold. Therefore, an improved benefit - risk ratio is obtained.

[0271] Example 3. Removal of lipids using arginine - ethyl ester and lipase GCL1, low detergent level (mini - LOM)

[0272] Measure the washing performance (oil removal and odor production) of lipase GCL1 and arginine ethyl ester according to the method using low detergent level described above and the further conditions listed in Table 5 below:

[0273]

[0274] Table 5: Removal of lipids using a combination of arginine ethyl ester and lipase GCL1 at low detergent level.

[0275] Obviously, arginine-ethyl ester is compatible with lipase GCL1, and the actions of the lipase and the lipid removal enhancer are at least additive. It has also unexpectedly become apparent that at least the same level of oil removal can be achieved using 1 mM lysine methyl ester as with the lipase, but with significantly reduced odor generation, resulting in an improved benefit-risk ratio.

[0276] Example 4. Lipid removal using arginine-ethyl ester and lipases LE 1 and GCL1, low detergent level (mini-LOM)

[0277] The washing performance (oil removal and odor generation) of lipases L1 and GCL1 and arginine tert-butyl ester was measured according to the method using a low detergent level described above and the further conditions listed in Table 6 below:

[0278]

[0279]

[0280] Table 6: Lipid removal using arginine tert-butyl ester in combination with lipases LE 1 and GCL1 at a low detergent level.

[0281] The data show that by adding arginine tert-butyl ester, the same level of oil removal as with the lipase can be achieved, but with significantly reduced odor generation, i.e., an increased benefit-risk ratio.

[0282] Example 5. Lipid removal using sodium stearoyl lactylate, standard detergent level (TOM)

[0283] The washing performance (oil removal) of sodium stearoyl lactylate (SSL) was measured according to the method using a standard detergent level described above and the further conditions listed in Table 7 below, and compared with the use of lipase LE2:

[0284]

[0285]

[0286] Table 7: Lipid removal using SSL at a standard detergent level

[0287] It is clearly evident from the above results that the same level of oil removal can be achieved with SSL as with the lipase.

[0288] Example 6. Oil removal in detergent II (0.8 g detergent / L) using lysine methyl ester and lipase LE 1

[0289] The washing performance (oil removal and odor generation) of lipase L1 and lysine methyl ester was measured according to the Mini-LOM-method using 0.8 g detergent / L and the further conditions listed in Table 8 below:

[0290]

[0291] Table 8: Removal of oil using lysine methyl ester (in the presence and absence of lipase L1)

[0292] It can be clearly seen from the above results that lysine methyl ester improved oil removal both in the presence and absence of lipase. In addition, using lysine methyl ester alone achieved the same level of oil removal as using lipase alone, but with a significantly improved benefit-risk ratio.

[0293] Example 7. Removal of lard in Detergent II using arginine ethyl ester, low detergent level

[0294] Measure the washing performance (lard removal and odor generation) of lipase LE 1 and arginine ethyl ester according to the above TOM-method using low detergent levels and the further conditions listed in Table 9 below:

[0295]

[0296] Table 9: Removal of lard using arginine ethyl ester (in the presence and absence of lipase)

[0297] It can be clearly seen from the results in Table 9 that arginine ethyl ester was able to remove lard from textiles to the same extent as lipase, but with an improved benefit-risk ratio.

[0298] Example 8. Removal of lipids using L-lysine and lipase GCL1, low detergent level

[0299] Measure the washing performance (oil removal) of GCL1 and lysine according to the above Mini-LOM-method using low detergent levels and the further conditions listed in Table 10 below:

[0300]

[0301] Table 10: Removal of oil using lysine (in the presence and absence of lipase)

[0302] The results in Table 10 show that lysine can be used to remove oil from textiles.

[0303] Example 9. Removal of lipids using L-arginine and L-arginine-ethyl ester and lipase GCL1, low detergent level

[0304] Measure the washing performance (oil removal) of lipase GCL1 and arginine / arginine ethyl ester respectively according to the above Mini-LOM-method using low detergent levels and the further conditions listed in Table 11 below:

[0305]

[0306] Table 11: Removal of oil using arginine and arginine ethyl ester (in the presence and absence of lipase)

[0307] The results in Table 11 show that arginine has no effect on the removal of oil in textiles (same level as the detergent without lipase / arginine), while arginine ethyl ester enhances the removal of oil in textiles.

Claims

1. A detergent composition, the detergent composition comprising: a. at least one detergent component; b. Select a lipid removal enhancer from the group consisting of lysine, stearoyl lactate, C 1 to C 5 esters of lysine and C 1 to C 5 esters of arginine c. optionally one or more enzymes.

2. The composition according to claim 1, wherein the composition is a laundry detergent composition.

3. The composition according to claim 1(b), wherein the lipid removal enhancer is selected from the group consisting of: methyl ester, ethyl ester, 1-propyl ester, 2-propyl ester, 1-butyl ester, 2-butyl ester, 2-methyl-2-propyl ester, 2-methylpropyl ester, pentyl ester, 1,1-dimethylpropyl ester, 2,2-dimethylpropyl ester, 3-methylbutyl ester, 1-methylbutyl ester, 1-ethylpropyl ester, 1,2-methylpropyl ester and 2-methylbutyl ester of lysine.

4. The composition according to claim 1(b), wherein the lipid removal enhancer is selected from the group consisting of: methyl ester, ethyl ester, 1-propyl ester, 2-propyl ester, 1-butyl ester, 2-butyl ester, 2-methyl-2-propyl ester, 2-methylpropyl ester, pentyl ester, 1,1-dimethylpropyl ester, 2,2-dimethylpropyl ester, 3-methylbutyl ester, 1-methylbutyl ester, 1-ethylpropyl ester, 1,2-methylpropyl ester and 2-methylbutyl ester of arginine.

5. The composition according to claim 1(b), wherein the lipid removal enhancer is lysine.

6. The composition according to claim 1(b), wherein the lipid removal enhancer is stearoyl lactate.

7. The composition according to claim 1, wherein the detergent composition comprises one or more enzymes selected from the group consisting of: lipase, protease, peroxidase, cellulase, β-glucanase, xyloglucanase, hemicellulase, xanthanase, xanthan lyase, amylase, acyltransferase, phospholipase, esterase, laccase, catalase, arylesterase, amylase, α-amylase, glucoamylase, cutinase, pectinase, pectin lyase, keratinase, reductase, oxidase, phenol oxidase, lipoxygenase, ligninase, carrageenase, pullulanase, tannase, arabinosidase, hyaluronidase, chondroitinase, xyloglucanase, xylanase, pectin acetylesterase, polygalacturonase, rhamnogalacturonase, other endo-β-mannanases, exo-β-mannanases (GH5 and / or GH26), lichenase, phosphodiesterase, pectin methyl esterase, cellobiohydrolase, transglutaminase, nuclease and combinations thereof, or any mixture thereof.

8. The composition according to claim 7, wherein the enzyme is lipase and / or protease.

9. Use of the detergent composition according to any one of claims 1 to 8 for cleaning a surface such as a textile, the use comprising contacting the surface with the detergent composition.

10. A method for cleaning a surface such as a textile, the method comprising contacting the surface with the detergent composition according to any one of claims 1 to 8.

11. The composition according to claim 3, wherein the concentration of the lysine ester is adjusted to obtain a final concentration of the lysine ester in the washing liquid in the range of 0.5 mM to 20 mM, preferably a final concentration in the washing liquid in the range of 1 mM to 10 mM.

12. The composition according to claim 4, wherein the concentration of the arginine ester is adjusted to obtain a final concentration of the arginine ester in the washing liquid in the range of 0.5 mM to 20 mM, preferably a final concentration in the washing liquid in the range of 1 mM to 10 mM.

13. The composition according to claim 5, wherein the concentration of the lysine is adjusted to obtain a final concentration of the lysine in the washing liquid in the range of 0.5 mM to 20 mM, preferably a final concentration in the washing liquid in the range of 1 mM to 10 mM.

14. The composition according to claim 6, wherein the concentration of the stearoyl lactate ester is adjusted to obtain a final concentration of the stearoyl lactate ester in the washing liquid corresponding to sodium stearoyl lactate in the range of 100 ppm to 400 ppm, preferably a final concentration in the washing liquid corresponding to sodium stearoyl lactate in the range of 100 ppm to 300 ppm.

15. The composition according to claim 1, the use according to claim 9 and the method according to claim 10, wherein the composition comprises more than one lipid removal enhancer.

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