CN113056548B

CN113056548B - Detergent composition

Info

Publication number: CN113056548B
Application number: CN201980076305.1A
Authority: CN
Inventors: J·C·本宁霍夫; S·A·德罗斯; M·伊苏波夫; D·A·朗; J·A·利特勒奇尔德-邦德; S·R·史密斯; M·L·汤普森
Original assignee: Unilever IP Holdings BV
Current assignee: Unilever IP Holdings BV
Priority date: 2018-11-20
Filing date: 2019-10-30
Publication date: 2023-05-02
Anticipated expiration: 2039-10-30
Also published as: CN113056548A; ZA202102551B; EP3884025B1; EP3884025A1; WO2020104157A1; BR112021009789A2

Abstract

The present invention provides a detergent composition comprising: (i) 1 to 60 wt% surfactant; and (ii) 0.0005 to 5% by weight of an esterase of enzyme class EC 3.1.1.1 having at least 60% sequence identity to any of SEQ ID NOs 1 to 4; and methods of using the enzymes and the use of the enzymes for improving the cleaning of sebum stains on fabrics.

Description

Detergent composition

Technical Field

The present invention relates to detergent compositions, more particularly to laundry detergent compositions comprising novel esterases.

Background

Sebum is oily soil that remains as a stain that is difficult to remove from clothing being worn. Driven by encouraging users to wash at lower temperatures, challenges for effective sebum removal remain elusive. Sebum is composed of a large number of fats and esters including wax esters, cholesterol esters, squalene and many free fatty acids/alcohols. Sebum is liquid at body temperature, but solid at ambient temperature.

These properties are particularly important for collar/cuff soil removal because liquid body oils are easier to remove from clothing than solids. Current laundry enzymes are unable to degrade all components of sebum, which makes removal from fabrics difficult.

The problem with sebum removal is that detergents, including current commercial enzymes, do not adequately remove sebum.

Disclosure of Invention

We have found that the addition of novel esterases to detergent compositions improves sebum removal from fabrics.

In one aspect, the present invention provides a detergent composition comprising:

(i) 1 to 60 wt%, preferably 2 to 50 wt%, more preferably 3 to 45 wt%, even more preferably 5 to 40 wt%, most preferably 6 to 40 wt% of a surfactant; and

(ii) From 0.0005 to 5% by weight, preferably from 0.005 to 2.5% by weight, more preferably from 0.01 to 1% by weight, of esterases of the enzyme class EC 3.1.1.1 having at least 60% sequence identity with any of SEQ ID NOS.1 to 4.

Preferably, the esterase has at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, even more preferably at least 90%, even more preferably at least 95%, most preferably at least 97%, at least 98% or even at least 99% sequence identity to any of SEQ ID nos. 1 to 4.

Most preferably, the esterase has 100% sequence identity to any of SEQ ID NOs 1 to 4.

Preferably, the detergent composition comprises from 0.1 to 10 wt%, preferably from 0.2 to 9 wt%, more preferably from 0.25 to 8, even more preferably from 0.5 to 6 wt%, most preferably from 1 to 5 wt% soil release polymer, more preferably polyester based soil release polymer.

Preferably, the polyester soil release polymer is a polyethylene terephthalate and/or polytrimethylene terephthalate based soil release polymer, preferably a polytrimethylene terephthalate based soil release polymer. Preferably, the detergent composition comprises an alkoxylated polyamine, preferably in an amount of from 0.1 to 8 wt%, more preferably from 0.2 to 6 wt%, most preferably from 0.5 to 5 wt%.

Preferably, the detergent composition is a laundry detergent composition. Preferably, the laundry detergent composition is a liquid or powder, most preferably a liquid detergent.

Preferably, the surfactant in the detergent composition comprises an anionic surfactant and/or a nonionic surfactant, in one instance both an anionic surfactant and a nonionic surfactant.

Preferred detergent compositions, in particular laundry detergent compositions, further comprise an additional enzyme selected from the group consisting of: esterases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases.

Preferred detergent compositions, especially laundry detergent compositions, further comprise additional ingredients selected from fluorescers, perfumes, hueing dyes and polymers and mixtures thereof.

In another aspect, the invention provides a method of treating a textile substrate having a sebum stain, the method comprising adding an esterase having an enzyme EC 3.1.1.1 with sequence identity of at least 60%, preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, even more preferably at least 90%, even more preferably at least 95%, most preferably at least 97%, at least 98% or even at least 99%, most preferably 100% sequence identity to a detergent composition comprising from 1 to 60% by weight of a surfactant to any of SEQ ID NOs; and subsequently treating the fabric substrate with sebum stains with the composition.

In a further aspect, the present invention provides the use of an esterase of enzyme EC 3.1.1.1 having at least 60%, preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, even more preferably at least 90%, even more preferably at least 95%, most preferably at least 97%, at least 98% or even at least 99% sequence identity, most preferably 100% sequence identity to any of SEQ ID nos. 1 to 4 for improving the cleaning of sebum stains on a fabric.Detailed description of the preferred embodiments A kind of electronic device with high-pressure air-conditioning system

The indefinite article "a" or "an" as used herein and its corresponding definite article "the" means at least one, or one or more, unless specified otherwise.

Unless otherwise specified, all% content of ingredients in the compositions (formulations) listed herein are based on the weight% of the total formulation.

It should be understood that any reference to a preferred ingredient of a detergent composition is contemplated as a subject matter which may be combined with any other preferred ingredient of the detergent compositions disclosed herein.

The detergent composition may take any suitable form, for example liquid, solid (including powder) or gel.

The detergent composition may be applied to any suitable substrate. A particularly preferred substrate is a fabric. Particularly preferred detergent compositions are laundry detergent compositions.

The laundry detergent composition may take any suitable form. The preferred form is a liquid or powder, with liquid being most preferred.

Sequence information

The sequences disclosed herein are SEQ ID NOs 1 to 4.

SEQ ID 1 is from Thermogutta terrifontis.

The sequence is as follows:

maqrvkittt atpgeielaf edtgtglpvl lvhgfpldrt mwkaqreelc defrvivpdl rgfgesqvip gvatmeamad dlaglcnhlg ltgkivlggl smggyvafaf arkyrdrlag lilcdtrarp dspeakenrr rvaervrreg pgfiaeemip rlccestfrn hpeviekirq milsappegv aaaalgmaer pdstdllpal scptlvlvgq fdaisppeem eamartipqs qfvvipdagh lppmeqperv tqairewlrk vhte

SEQ ID 2 is from Thermogutta terrifontis.

The sequence is as follows:

maqrvkittt atpgeielaf edtgtglpvl lvhgfpAdrt mwkaqreelc defrvivpdl rgfgesqvip gvatmeamad dlaglcnhlg ltgkivlggl smggyvafaf arkyrdrlag lilcdtrarp dspeakenrr rvaervrreg pgfiaeemip rlccestfrn hpeviekirq milsappegv aaaalgmaer pdstdllpal scptlvlvgq fdaisppeem eamartipqs qfvvipdagh lppmeqperv tqairewlrk vhte

The sequence is a mutant of SEQ ID 1, differing at position 37.

SEQ ID 3 is from Thermogutta terrifontis.

The sequence is as follows:

maqrvkittt atpgeielaf edtgtglpvl lvhgfpldrt mwkaqreelc defrvivpdl rgfgesqvip gvatmeamad dlaglcnhlg ltgkivlggl smggyvafaf arkyrdrlag lilcdtrarp dspeakenrr rvaervrreg pgfiaeemip rlccestfrn hpeviekirq milsappegv aaaalgmaer pdstdllpal scptlvlvgq fdaisppeem eamartipqs qfvvipdagh Appmeqperv tqairewlrk vhte

the sequence is a mutant of SEQ ID 1, differing at position 251.

SEQ ID 4 is from Archaeoglobus fulgidus.

The sequence is as follows:

MLERVFIDVDGVKVSLLKGRERKVFYIHSSGSDATQWVNQLTAIGGYAIDLPNHGQSDTVEVNSVDEYAYYASESLKKTVGKAVVVGHSLGGAVAQKLYLRNPEICLALVLVGTGARLRVLPEILEGLKKEPEKAVDLMLSMAFASKGEEYEKKRREFLDRVDVLHLDLSLCDRFDLLEDYRNGKLKIGVPTLVIVGEEDKLTPLKYHEFFHKHIPNSELVVIPGASHMVMLEKHVEFNEALEKFLKKVGV

lipase enzyme

The esterase has at least 60% sequence identity to any of SEQ ID NOs 1 to 4.

Preferably, the esterase has at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, even more preferably at least 90%, even more preferably at least 95%, most preferably at least 97%, at least 98%, or even at least 99% sequence identity to any of SEQ ID nos. 1 to 4.

Esterases can be described as belonging to the class of enzymes EC 3.1.1.1, called carboxyesterases.

Preferred esterases are from Thermogutta terrifontis or Archaeoglobus fulgidus.

Surface active agent

The detergent composition comprises a surfactant (which may comprise a single surfactant or a mixture of two or more surfactants). The composition comprises from 1 to 60 wt%, preferably from 2 to 50 wt%, more preferably from 3 to 45 wt%, even more preferably from 5 to 40 wt%, most preferably from 6 to 40 wt% surfactant.

The detergent composition (preferably, a laundry detergent composition) comprises an anionic surfactant and/or a nonionic surfactant, preferably both an anionic surfactant and a nonionic surfactant.

Suitable anionic detergent compounds which may be used are typically water-soluble alkali metal salts of organic sulfuric and sulfonic acids having alkyl groups containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher alkyl groups.

Examples of suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, in particular by reacting higher C's, e.g. produced from tallow or coconut oil ₈ To C ₁₈ Those obtained by sulfation of alcohols, alkyl radicals C ₉ To C ₂₀ Sodium and potassium benzenesulfonates, in particular linear secondary alkyl C ₁₀ To C ₁₅ Sodium benzenesulfonate; and sodium alkyl glyceryl ether sulphates, particularly those ethers of higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.

The anionic surfactant is preferably selected from: linear alkylbenzene sulfonates; alkyl sulfate; alkyl ether sulfate; soap; alkyl (preferably methyl) ester sulfonates and mixtures thereof.

Most preferred anionic surfactants are selected from: linear alkylbenzene sulfonates; alkyl sulfate; alkyl ether sulfates and mixtures thereof. Preferably, the alkyl ether sulfate is C having an average of 1 to 3 EO (ethoxylate) units ₁₂ -C ₁₄ N-alkyl ether sulfate.

Sodium Lauryl Ether Sulfate (SLES) is particularly preferred. Preferably, the linear alkylbenzene sulfonate is C ₁₁ To C ₁₅ Sodium alkylbenzenesulfonate. Preferably, the alkyl sulfate is a linear or branched C ₁₂ To C ₁₈ Sodium alkyl sulfate. Sodium dodecyl sulfate is a specialOther preferred (SDS, also known as primary alkyl sulfate).

In liquid formulations, two or more anionic surfactants, such as linear alkylbenzene sulfonates together with alkyl ether sulfates, are preferably present.

In liquid formulations, the laundry composition preferably comprises, in addition to the anionic surfactant, an alkyl ethoxylated nonionic surfactant, preferably 2 to 8 wt% of the alkyl ethoxylated nonionic surfactant.

Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having aliphatic hydrophobic groups and reactive hydrogen atoms (e.g., fatty alcohols, acids or amides) with, in particular, ethylene oxide (alone or with propylene oxide). Preferred nonionic detergent compounds are aliphatic C ₈ To C ₁₈ Condensation products of linear or branched primary or secondary alcohols with ethylene oxide.

Most preferably, the nonionic detergent compound is an alkyl ethoxylated nonionic surfactant which is an average ethoxylated C having 7EO to 9EO units ₈ To C ₁₈ Primary alcohols.

Preferably, the surfactant used is saturated.

Soil release polymers

The soil release polymer is preferably present at a level of 0.1 to 10 wt%. The soil release polymer is preferably included at a level of from 0.2 to 9 wt%, more preferably from 0.25 to 8 wt%, even more preferably from 0.5 to 6 wt%, most preferably from 1 to 5 wt%. Preferably, the soil release polymer is a polyester based soil release polymer. More preferably, the polyester soil release polymer is a polyethylene terephthalate and/or polytrimethylene terephthalate based soil release polymer, most preferably a polytrimethylene terephthalate based soil release polymer.

Suitable polyester-based soil release polymers are described in WO 2014/029479 and WO 2016/005338.

Alkoxylated polyamines

The detergent composition preferably comprises an alkoxylated polyamine. Especially when the detergent composition is in the form of a laundry composition, it is preferred to include an alkoxylated polyamine.

Preferred amounts of the alkoxylated polyamine are from 0.1 to 8% by weight, preferably from 0.2 to 6% by weight, more preferably from 0.5 to 5% by weight. Another preferred content is 1 to 4% by weight.

The alkoxylated polyamine may be linear or branched. It can be branched to the extent that it is a dendrimer. Alkoxylation may generally be ethoxylation or propoxylation, or a mixture of both. When the nitrogen atom is alkoxylated, the preferred average degree of alkoxylation is from 10 to 30, preferably from 15 to 25.

Preferred materials are alkoxylated polyethylenimines, most preferably ethoxylated polyethylenimines, having an average degree of ethoxylation of from 10 to 30, preferably from 15 to 25, wherein the nitrogen atoms are ethoxylated.

Additional enzymes

In addition to the lipase specified, additional enzymes may be present in the detergent composition. It is preferred that additional enzymes are present in the preferred laundry detergent compositions.

Each enzyme, if present, is present in the laundry compositions of the present invention in an amount of from 0.0001 wt% to 0.1 wt%.

The amount of enzyme present in the composition is preferably related to the amount of enzyme as pure protein.

Preferred additional enzymes include those of the following: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases. The preferred additional enzymes include mixtures of two or more of these enzymes.

Preferably, the additional enzyme is selected from: lipases, proteases, cellulases and/or alpha-amylases.

Suitable lipases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful lipases include those from the following: humicola (synonymous thermophilic fungi (Thermomyces)), for example from H.lanuginosa (T.lanuginosus) as described in EP 258 068 and EP 305 216 or from H.insolens as described in WO 96/13580; pseudomonas lipases, for example from Pseudomonas alcaligenes or Pseudomonas pseudoalcaligenes (EP 218 272), pseudomonas cepacia (P.cepacia) (EP 331 376), pseudomonas stutzeri (GB 1,372,034), pseudomonas fluorescens (P.fluoscens), pseudomonas strain SD 705 (WO 95/06720 and WO 96/27002), P.wisconsiensis (WO 96/12012); bacillus lipases are, for example, from Bacillus subtilis (B.subilis) (Dartois et al (1993), biochemica et Biophysica Acta,1131, 253-360), bacillus stearothermophilus (B.stearothermophilus) (JP 64/744992) or Bacillus pumilus (B.pumilus) (WO 91/16422).

Other examples are lipase variants, such as those described in WO 92/05249, WO 94/01541, EP 407225, EP 260 105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202, WO 00/60063.

Preferred commercially available lipases include Lipolase ^TM And Lipolase Ultra ^TM 、Lipex ^TM And lipoclear ^TM (Novozymes A/S)。

The process of the invention may be carried out in the presence of a phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32. As used herein, the term phospholipase is an enzyme active towards phospholipids.

Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in the outer (sn-1) and middle (sn-2) positions and phosphated in the third position; the phosphoric acid in turn may be esterified to an amino alcohol. Phospholipase is an enzyme involved in phospholipid hydrolysis. Can distinguish between multiple types of phospholipase activity, including phospholipase A ₁ And A ₂ Which hydrolyzes one fatty acyl group (in the sn-1 and sn-2 positions, respectively) to form lysophospholipids; and lysophospholipase (or phospholipase B), which can hydrolyze fatty acyl groups remaining in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterases) release diacylglycerol or phosphatidic acid, respectively.

Proteases hydrolyze peptides and bonds within proteins, which in a laundry environment results in enhanced removal of protein or peptide containing stains. Examples of suitable protease families include aspartic proteases; cysteine proteases; glutamate protease; asparagine (aspargine) peptide lyase; serine proteases and threonine proteases. Such protease families are found in the MEROPS peptidase databasehttp://merops.sanger.ac.uk/) Is described in (c). Serine proteases are preferred. Subtilase serine proteases are more preferred. According to Siezen et al, protein Engng.4 (1991) 719-737 and Siezen et al, protein Science 6 (1997) 501-523, the term "subtilase" refers to a subset of serine proteases. Serine proteases are a subset of proteases characterized by having serine at the active site that forms a covalent adduct with a substrate. Subtilases can be divided into 6 sub-categories, namely the Subtilisin (Subtilisin) family, the thermophilic protease (Thermitase) family, the protease K (Proteinase K) family, the lanthionine antibiotic (Lantibiotic) peptidase family, the Kexin family and the Pyrolysin family.

Examples of subtilases are those derived from bacillus such as those described in US7262042 and WO09/021867, alkalophilus, bacillus subtilis, bacillus amyloliquefaciens, bacillus pumilus and bacillus jie, and subtilisin (subtilisin lentus) described in WO89/06279, subtilisin Novo, subtilisin Carlsberg, bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168, and proteinase PD138 described in WO 93/18140. Other useful proteases may be those described in WO92/175177, WO01/016285, WO02/026024 and WO 02/016547. Examples of trypsin-like proteases are trypsin (e.g.of porcine or bovine origin) and Fusarium protease described in WO89/06270, WO94/25583 and WO05/040372, and chymotrypsin from Cellulomonas (Cellumomonas) described in WO05/052161 and WO 05/052146.

Most preferably, the protease is subtilisin (EC 3.4.21.62).

Examples of subtilases are those derived from bacillus such as those described in US7262042 and WO09/021867, alkalophilus, bacillus subtilis, bacillus amyloliquefaciens, bacillus pumilus and bacillus jii, and subtilisin, subtilisin Novo, subtilisin Carlsberg, bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168, and proteinase PD138 described in WO 93/18140. Preferably, the subtilisin is derived from bacillus, preferably bacillus lentus, bacillus alkalophilus, bacillus subtilis, bacillus amyloliquefaciens, bacillus pumilus and bacillus gibsonii, as described in US 6,312,936 B1,US 5,679,630,US 4,760,025,US7,262,042 and WO 09/021867. Most preferably, the subtilisin is derived from bacillus gibsonii or bacillus lentus.

Suitable commercially available proteases include those under the trade name

DuralaseTm、DurazymTm、/>

Ultra、/>

Ultra、

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those sold, all of which can be regarded as +. >

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(Novozymes A/S) sales.

The compositions may use cutinase (cutinase) classified under EC 3.1.1.74. The cutinase used according to the invention may be of any origin. Preferably, the cutinase has a microbial origin, in particular a bacterial, fungal or yeast origin.

Suitable amylases (α and/or β) include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, the alpha-amylase obtained from a particular strain of Bacillus, such as Bacillus licheniformis as described in more detail in GB 1,296,839, or a strain of Bacillus as disclosed in WO 95/026397 or WO 00/060060. A commercially available amylase is Duramyl ^TM 、Termamyl ^TM 、Termamyl Ultra ^TM 、Natalase ^TM 、Stainzyme ^TM 、Amplify ^TM 、Fungamyl ^TM and BAN ^TM (Novozymes A/S)、Rapidase ^TM And Purastar ^TM (from Genencor International inc.).

Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the following: bacillus, pseudomonas, humicola, fusarium, thielavia, acremonium, fungal cellulases produced, for example, from specific Humicola, thielavia, myceliophthora thermophila and Fusarium oxysporum disclosed in U.S. Pat. No. 4,435,307, U.S. Pat. No. 5,648,263, U.S. Pat. No. 5,691,178, U.S. Pat. No. 5,776,757, WO 89/09259, WO 96/029397 and WO 98/0123307. Commercially available cellulases include Celluzyme ^TM 、Carezyme ^TM 、Celluclean ^TM 、Endolase ^TM 、Renozyme ^TM (Novozymes A/S)、Clazinase ^TM and Puradax HA ^TM (Genencor International Inc.) and KAC-500 (B) ^TM (Kao Corporation)。Celluclean ^TM Is preferred.

Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from the genus Coprinus, e.g.from Coprinus cinereus, and variants thereof, such as those described in WO 93/24618, WO 95/10602 and WO 98/15257. Commercially available peroxidases include Guardzyme ^TM And Novozym ^TM 51004(Novozymes A/S)。

Additional suitable enzymes are discussed in WO2009/087524, WO2009/090576, WO2009/107091, WO2009/111258 and WO 2009/148983.

The aqueous solution used in the method preferably has enzymes present. The enzyme is preferably present in the aqueous solution used in the process in a concentration in the range of 0.01 to 10ppm, preferably 0.05 to 1 ppm.

Enzyme stabilizer

Any enzyme present in the composition may be stabilised using conventional stabilisers, for example polyols such as propylene glycol or glycerol; sugar or sugar alcohol; lactic acid; boric acid or boric acid derivatives, for example aromatic borates, or phenylboronic acid derivatives, such as 4-formylphenylboronic acid, and the compositions may be formulated as described, for example, in WO 92/19709 and WO 92/19708.

Additional materials

Additional optional but preferred materials that may be included in the detergent composition (preferably, a laundry detergent composition) include fluorescers, perfumes, hueing dyes, polymers and chelating agents.

Fluorescent agent

The composition preferably comprises a fluorescent agent (optical brightener). Fluorescent agents are well known and many such fluorescent agents are commercially available. Typically, these fluorescent agents are supplied and used in the form of their alkali metal salts, e.g., sodium salts.

The total amount of one or more fluorescent agents used in the composition is generally from 0.0001 to 0.5 wt%, preferably from 0.005 to 2 wt%, more preferably from 0.01 to 0.1 wt%.

Preferred classes of fluorescers are: stilbene biphenyl compounds, such as Tinopal (trade mark) CBS-X, diamine stilbenedisulfonic acid compounds, such as Tinopal DMS pure Xtra and Blankophor (trade mark) HRH, and pyrazoline compounds, such as Blankophor SN.

Preferred fluorescers are those having CAS-No 3426-43-5; CAS-No 35632-99-6; CAS-No 24565-13-7; CAS-No 12224-16-7; CAS-No 13863-31-5; CAS-No 4193-55-9; CAS-No 16090-02-1; CAS-No 133-66-4; CAS-No 68444-86-0; fluorescent agent of CAS-No 27344-41-8.

Most preferred fluorescent agents are: sodium 2- (4-styryl-3-sulfophenyl) -2H-naphtho (napthol) [1,2-d ] triazole, disodium 4,4' -bis { [ (4-anilino-6- (N-methyl-N-2-hydroxyethyl) amino-1, 3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' -disulphonate, disodium 4,4' -bis { [ (4-anilino-6-morpholino-1, 3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' -disulphonate and disodium 4,4' -bis (2-sulfostyryl) biphenyl.

The aqueous solution used in the method has a fluorescent agent present. The fluorescent agent is preferably present in the aqueous solution used in the method in a range of 0.0001g/L to 0.1g/L, more preferably 0.001 to 0.02g/L.

Spice

The composition preferably comprises a perfume. Many suitable examples of fragrances are provided in CTFA (Cosmetic, toiletry and Fragrance Association) 1992International Buyers Guide published by CFTA Publications and OPD 1993Chemicals Buyers Directory 80th Annual Edition published by Schnell Publishing co.

Preferably, the perfume comprises at least one of the following notes (compounds): alpha-isoamyl ionone, benzyl salicylate; citronellol; coumarin; hexyl cinnamaldehyde; linalool; ethyl 2-methylpentanoate; octanal; benzyl acetate; 3, 7-dimethyl-1, 6-octadien-3-ol 3-acetate; 2- (1, 1-dimethylethyl) -cyclohexanol 1-acetate; delta-damascone (damascone); beta-ionone; tricyclodecenyl acetate (verdyl acetate); dodecanal; hexyl cinnamaldehyde (hexyl cinnamic aldehyde); cyclopentadecanolide; 2-phenylethyl phenylacetate; amyl salicylate; beta-caryophyllene; ethyl undecylenate; geranyl anthranilate; alpha-irone; beta-phenylethyl benzoate; α -santalol; cedrol; cypress acetate; cedarformate (cedryl format); cyclohexyl salicylate; gamma-dodecalactone, and beta-phenethyl phenyl acetate.

Useful components of fragrances include both materials of natural and synthetic origin. They include single compounds and mixtures. Specific examples of such components can be found in the prior literature, for example, fenaroli's Handbook of Flavor Ingredients,1975, crc Press; jacobs, synthetic Food Adjuncts,1947,Van Nostrand edit; or S.arctander, perfume and Flavor Chemicals,1969, montclair, N.J. (USA).

It is common for a variety of perfume components to be present in the formulation. In the compositions of the present invention, it is envisaged that there will be four or more, preferably five or more, more preferably six or more, or even seven or more different perfume components.

Preferably 15 to 25% by weight of the perfume mixture is a top note. The top note is defined by Poucher (Journal of the Society of Cosmetic Chemists 6 (2): 80[1955 ]). Preferred top notes are selected from citrus oils, linalool, linalyl acetate, lavender, dihydromyrcenol, rose oxide and cis-3-hexanol.

A list of fragrance ingredients (fragrances) has been published by the international daily fragrance and fragrance society in 2011. (http:// www.ifraorg.org/en-us/ingredients#.U7Z4hPldWzk)

The international daily fragrance institute provides a database of fragrances (fragrances) with safety information.

The fragrance stick may be used to suggest whiteness and brightness benefits of the present invention.

Some or all of the perfume may be encapsulated, typical perfume components which facilitate encapsulation include those having a relatively low boiling point, preferably those having a boiling point of less than 300 ℃, preferably 100-250 ℃. It is also advantageous to encapsulate perfume components having a low Clog P (i.e. those that will have a higher tendency to be dispensed into water), preferably having a Clog P of less than 3.0. Materials having a relatively low boiling point and relatively low CLog P have been referred to as "delayed fragrance" perfume ingredients and comprise one or more of the following materials: allyl caproate, amyl acetate, amyl propionate, anisaldehyde, anisole, benzaldehyde, benzyl acetate, benzyl acetone, benzyl alcohol, benzyl formate, benzyl isovalerate, benzyl propionate, beta-gamma hexenol, camphorum gum, levo-carvone, d-carvone, cinnamyl alcohol, cinnamyl formate (cinamyl format), cis-jasmone, cis-3-hexenyl acetate, cumyl alcohol, cyclic c, dimethylbenzyl alcohol, dimethylbenzyl methanol acetate, ethyl acetoacetate, ethyl amyl ketone, ethyl benzoate, ethyl butyrate, ethylhexyl ketone, ethyl phenyl acetate, eucalyptol, eugenol, fenchyl acetate, flor acetate, frene (tricyclodecenyl propionate) geraniol, hexenol, hexenyl acetate, hexyl formate, solanol (hydratropic alcohol), hydroxycitronellal, indenone, isoamyl alcohol, isomenthone, and isopulegol acetate (isopulegyl acetate), isoquinolone, ligustral, linalool oxide, linalyl formate, menthone, menthylacetophenone (menthyl acetphenone), methyl amyl ketone, methyl amyl alcohol, linalool acetate, and combinations thereof methyl anthranilate, methyl benzoate, methylbenzyl acetate (methyl benyl acetate), methyl eugenol, methyl heptenone, methyl heptynyl carbonate (methyl heptine carbonate), methyl heptynyl ketone, methyl hexyl ketone, methyl phenyl methyl acetate, methyl salicylate, methyl-n-methyl anthranilate, nerol, octanol, p-cresol methyl ether, P-methoxyacetophenone, p-methylacetophenone, phenoxyethanol, phenylacetaldehyde, phenylethyl acetate, phenylethyl alcohol, phenylethyl dimethyl methanol, isoprene acetate, propyl borate (propyl borate), menthone, rose oxide (rose oxide), safrole, 4-terpinenol (4-terpineol), alpha-terpinenol and/or phenylacetaldehyde dimethanol acetal (viridine). It is common for a variety of perfume components to be present in the formulation. In the compositions of the present invention, it is envisaged that there will be four or more, preferably five or more, more preferably six or more, or even seven or more different perfume components present in the perfume from the given list of delayed release perfumes given above.

Another group of fragrances that may be used with the present invention are so-called "aromatherapy" materials. These include many components that are also used in perfumes, including components of essential oils such as sage, eucalyptus, geranium, lavender, nutmeg dried skin (Mace) extract, neroli, nutmeg, spearmint, sweet violet leaf and valerian.

It is preferred that the laundry treatment composition is free of peroxygen bleach, for example sodium percarbonate, sodium perborate and peracid.

Shading dye

Preferably, when the composition is a laundry detergent composition, then it comprises a hueing dye. Preferably, the hueing dye is present at 0.0001 to 0.1% by weight of the composition.

Dyes are described in Color Chemistry Synthesis, properties and Applications of Organic Dyes and Pigments, (H Zollinger, wiley VCH, zulrich, 2003) and Industrial Dyes Chemistry, properties applications (K Hunger (ed), wiley-VCH Weinheim 2003).

Hueing dyes for laundry compositions preferably have a maximum absorption in the visible range (400-700 nm) of greater than 5000L mol ^-1 cm ^-1 Preferably greater than 10000L mol ^-1 cm ^-1 Is a refractive index of the optical fiber. The dye is blue or violet in color.

Preferred hueing dye chromophores are azo, azine, anthraquinone and triphenylmethane.

Azo, anthraquinone, phthalocyanine and triphenylmethane dyes are preferably either net anionic or uncharged. Azine preferably has a net anionic or cationic charge. During the wash or rinse step of the wash process, blue or violet hues are deposited onto the fabric, thereby providing a visible hue to the fabric. In this regard, the dye imparts a blue or violet color to the white cloth with a hue angle of 240 to 345, more preferably 250 to 320, most preferably 250 to 280. The white cloth used in this test was bleached, non-mercerized woven cotton sheet.

Hueing dyes are discussed in WO 2005/003274, WO 2006/032327 (Unilever), WO 2006/032397 (Unilever), WO 2006/045275 (Unilever), WO 2006/027086 (Unilever), WO 2008/017570 (Unilever), WO 2008/141880 (Unilever), WO 2009/132870 (Unilever), WO 2009/141173 (Unilever), WO 2010/099997 (Unilever), WO 2010/102861 (Unilever), WO 2010/148624 (Unilever), WO 2008/087497 (P & G), WO 2011/011799 (P & G), WO 2012/054820 (P & G), WO 2013/142495 (P & G) and WO 2013/151970 (P & G).

The monoazo dye preferably contains a heterocyclic ring, and most preferably is a thiophene dye. The monoazo dye is preferably alkoxylated and is preferably uncharged or anionically charged at ph=7. Alkoxylated thiophene dyes are discussed in WO/2013/142495 and WO/2008/087497. Preferred examples of thiophene dyes are shown below:

The disazo dye is preferably a sulphonated disazo dye. Preferred examples of sulphonated bisazo compounds are direct violet 7, direct violet 9, direct violet 11, direct violet 26, direct violet 31, direct violet 35, direct violet 40, direct violet 41, direct violet 51, direct violet 66, direct violet 99 and alkoxylated forms thereof. Alkoxylated bisazo dyes are discussed in WO2012/054058 and WO 2010/151906.

Examples of alkoxylated bisazo dyes are:

thiophene dyes are available from Milliken under the trade names Liquitint Violet DD and Liquitint Violet ION.

The azine dye is preferably selected from sulphonated phenazine dyes and cationic phenazine dyes. Preferred examples are acid blue 98, acid violet 50, dyes with cas numbers 72749-80-5, acid blue 59, and phenazine dyes selected from the group consisting of:

wherein:

X ₃ selected from: -H; -F; -CH ₃ ；-C ₂ H ₅ ；-OCH ₃ The method comprises the steps of carrying out a first treatment on the surface of the and-OC ₂ H ₅ ；

X ₄ Selected from: -H; -CH ₃ ；-C ₂ H ₅ ；-OCH ₃ The method comprises the steps of carrying out a first treatment on the surface of the and-OC ₂ H ₅ ；

Y ₂ Selected from: -OH; -OCH ₂ CH ₂ OH；-CH(OH)CH ₂ OH；-OC(O)CH ₃ The method comprises the steps of carrying out a first treatment on the surface of the And C (O) OCH ₃ 。

Hueing dye is present in the composition in the range of 0.0001 to 0.5 wt%, preferably 0.001 to 0.1 wt%. Depending on the nature of the hueing dye, there is a preferred range depending on the effectiveness of the hueing dye, which depends on the class and the specific effectiveness within any particular class. As described above, the hueing dye is a blue or violet hueing dye.

Mixtures of hueing dyes may be used.

The hueing dye is most preferably a reactive blue anthraquinone dye covalently linked to an alkoxylated polyethylenimine. The alkoxylation is preferably selected from the group consisting of ethoxylation and propoxylation, most preferably propoxylation. Preferably, 80 to 95 mole% of the N-H groups in the polyethyleneimine are replaced by isopropanol groups by propoxylation. Preferably, the polyethyleneimine has a molecular weight of 600 to 1800 prior to reaction with the dye and propoxylation.

An example structure of a preferred reactive anthraquinone covalently linked to a propoxylated polyethylenimine is:

(Structure I).

Polymer

The composition may comprise one or more additional polymers. Examples are carboxymethyl cellulose, poly (ethylene glycol), poly (vinyl alcohol), polycarboxylic esters such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.

Chelating agent

The chelating agent may be present or absent from the detergent composition. If present, the chelating agent is present in an amount of 0.01 to 5 wt.%.

Examples of phosphonic acid (or salt thereof) chelating agents are: 1-hydroxyethylidene-1, 1-diphosphonic acid (HEDP); diethylenetriamine penta (methylenephosphonic acid) (DTPMP); hexamethylenediamine tetra (methylenephosphonic acid) (HDTMP); aminotri (methylenephosphonic Acid) (ATMP); ethylenediamine tetra (methylenephosphonic acid) (EDTMP); tetramethylenediamine tetra (methylenephosphonic acid) (TDTMP); and phosphinobutanetricarboxylic acid (PBTC).

Examples

The invention will be illustrated by the following non-limiting examples.

Examples

Cloning including sequence information&Expression TtEst Thermogutta terrifontis:

the DNA sequence encoding the protein with putative hydrolytic activity was identified using the ANASTASIA halaxy line from the HotZyme database. Amplifying a gene from genomic DNA and using for N-terminal His ₆ The labeled aLICator LIC clone and expression kit (pLATE 31) were used for cloning. Coli ArcticExpress (DE 3) RIL was transformed (heat shock) and used as an expression strain for protein production.

TtEst mutants L37A and L251A were prepared using QuikChange Lightning Site-Directed Mutagenesis Kit according to the manufacturer's instructions. The mutant constructs were overexpressed in the same manner as the native protein.

TtEst(SEQ ID NO 1)

TtEst L37A(SEQ ID NO 2)

TtEst L251A(SEQ ID NO 3)

AfEst2 from Archaeoglobus Esterase of fulgidus:

PCT amplified the gene encoding AF-Est2 (locus marker: AF1537; uniprot accession number: O28735) without its stop codon using chromosomal DNA of A. Fulgidus as a template, and introduced NcoI and XhoI restriction sites, respectively. The resulting PCR product was digested with NcoI and XhoI, the product was purified, and ligated into the protein expression vector pET24d digested with the same restriction enzymes, to give plasmid pWUR365 for expressing the C-terminal 6 x-His-tag AF-Est2 protein. The expression plasmid was used to transform E.coli strain BL21-CodonPlus (DE 3) -RIPL.

AfEst2(SEQ ID NO 4)

Fermentation (harvesting) and purification

TtEst Thermogutta terrifontis:

Protein production was performed in 2L Erlenmeyer flasks with 1L LB medium and the appropriate antibiotics for plasmid selection (ampicillin, 100. Mu.g/mL; gentamicin 20. Mu.g/mL). LB-medium containing only ampicillin was inoculated with 1-3% (v/v) of the preculture and incubated at 37℃and 180rpm until OD was reached ₆₀₀ =0.4. The culture temperature was then reduced to 12℃for 1 hour. Gene expression was induced by adding IPTG to a final concentration of 1mM and performed at 12℃and 180rpm for 2 days. Cells were harvested by centrifugation (4750 Xg, 20min,4 ℃) and stored at-80 ℃.

Cell lysis was performed by resuspending the cell paste in equilibration buffer (25 mM Tris-HCl, pH 8.0, 500mM NaCl,20mM imidazole, 10mL buffer for 1g wet cell weight) and sonicating the cells on ice. Protein purification was performed using a 1mL HisTrap FF (GE Healthcare) column and AKTA purification system (GE Healthcare) for affinity chromatography by polyhistidine-tag. Protein elution was performed via a linear gradient for 30 minutes using buffer with increasing imidazole concentration (25 mM Tris-HCl, pH 8.0, 500mM NaCl,500mM imidazole). The eluted fractions were identified by absorbance (280 nm) and applied to SDS-PAGE. Fractions containing the protein of interest were pooled and dialyzed against 5L of imidazole-free buffer (25 mM Tris-HCl, pH 8.0, 500mM NaCl) overnight. The dialyzed protein was supplemented with 0.005% (v/v) sodium azide and 10% (v/v) glycerol for freezing and storage at-80 ℃.

AfEst2: esterases from Archaeoglobus fulgidus

Protein production was performed in Luria-Bertani (LB) medium containing 50. Mu.g/ml of kanamycin, chloramphenicol, and streptomycin, respectively. LB-medium containing kanamycin and chloramphenicol with 1-3% (v/v) preculture was incubated at 37℃and 180rpm until OD was reached ₆₀₀ =0.6. Gene expression was induced by addition of IPTG to a final concentration of 1mM and carried out overnight at 30℃and 180 rpm. Cells were harvested by centrifugation (4750 Xg, 20min,4 ℃) and stored at-80 ℃.

Cell lysis was performed by re-suspending the cell paste in equilibration buffer (25 mM Tris-HCl for a wet cell weight of 1g, pH 8.0,500mM NaCl,20mM imidazole, 10mL buffer) and sonicating the cells on ice. Protein purification was performed using a 1mL HisTrap FF column using an AKTA purifier for affinity chromatography by polyhistidine-tag. Protein elution was performed via a linear gradient for 30 minutes using buffer with increasing imidazole concentration (25 mM Tris-HCl, pH 8.0,500mM NaCl,500mM imidazole). The eluted fractions were identified by absorbance (280 nm) and applied to SDS-PAGE. Fractions containing the protein of interest were pooled and dialyzed against 5L of imidazole-free buffer (25 mM Tris-HCl, pH 8.0,500mM NaCl) overnight. The dialyzed protein was supplemented with 0.005% (v/v) sodium azide and 10% (v/v) glycerol for freezing and storage at-80 ℃.

Biological analysis

Determination of protein concentration

The total protein content of the enzyme samples was estimated by using Sigma-Aldrich BCA assay kit and working reagents were prepared as indicated in the user manual. BCA reagent was prepared by mixing solution A [1% (w/v) sodium salt form of bicinchoninic acid, 2% (w/v) sodium carbonate, 0.16% (w/v) sodium tartrate, 0.4% (w/v) sodium hydroxide, 0.95% (w/v) sodium bicarbonate, pH11.5] with solution B [4% (w/v) copper sulfate ] at a ratio of 50:1 (v/v). Serial dilutions of bovine serum albumin (2 mg/mL) were performed in deionized water to generate a 7-point standard curve. To perform this assay, BCA reagent (200 μl) was added to the wells of a 96-well plate followed by sample protein dilution (20 μl). Microtiter plates (MTPs) were sealed and incubated at 37℃for 30 minutes. After incubation, absorbance at 540nm was measured on a spectrophotometer.

Measurement of esterase purityProtein samples containing esterases (20. Mu.L) were prepared with SDS-PAGE loading buffer and heated at 70℃for 10 min, then run on a 4-12% NuPage Bis-Tris gel containing MOPS buffer at 170V. PageRulerPlus molecular weight markers were run along with the samples to determine molecular mass. Then according to the manufacturer's protocol, gelCode Blu is used e Safe Protein Stain staining was performed on each gel.

Biochemical assay of esterase Activity

Esterase activity was determined colorimetrically using 4-nitrophenyl valerate (C5) and 4-nitrophenyl dodecanoate (C12) as substrates. 4-Nitrophenyl dodecanoate (25 mg) or 4-Nitrophenyl valerate (18 mg) was dissolved in 10mL of solvent (methanol) to prepare an 8mM stock solution. Prior to performing the assay, 1mL of the stock solution was added to 7mL of acidified water (pH 4.5) to give a final concentration of 1 mM. In a 96 well microtiter plate, 60. Mu.L of dH was added ₂ O, 115. Mu.L Tris-HCl buffer (pH 8.5, 50 mM), 5. Mu.L diluted enzyme solution and 20. Mu.L substrate (multichannel at the end). For blank, use dH ₂ O replaces the enzyme solution. After addition of the reagent, the release of the product (4-nitrophenol) was monitored at 405nm for 15 minutes at ambient temperature.

Application test

Composition of model human sebum and application to fabricsTable 1A shows the composition of human-like sebum to be used in the washing study, which is comparable to human sebum analyzed in the literature (table 1B). Macrolex violet dye (0.4% w/w) was added to the model sebum and then 100 μl was applied to a 10 x 10cm sample of poly cotton pre-heated to 60 ℃. Wicking (wicking) of the stain was promoted by allowing the stain to dry overnight at 60 ℃, the uniformity of staining was confirmed by colorimetrically determining the SRI value over the whole sample, which was then cut into smaller 30mm diameter circles, enabling assembly in a 6 well microtiter plate for subsequent wash tests.

Table 1 (A) composition of the human sebum-like product tested. The composition of human sebum proposed by Nikkari1974, in Ro2005, stefaniak 2010 is shown In comparison (B). Model human sebum-like was designed to simulate literature descriptions.

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Washing study of enzyme cleaning Performance against human sebum-like

Pre-wash readings were taken on 30mm diameter sebum stains to measure stain intensity. Washing studies were performed in a volume of 5mL (1 hour at 100rpm in a 6-well plate at 40 ℃) or 100mL (1 hour at 100rpm in a glass bottle at 40 ℃). The enzyme was present at 25mg/L in 2g/L of 7.5% surfactant formulation. The stains are then rinsed three times after washing to completely remove the wash liquor and any residual enzyme. After drying, the stain plates were digitally scanned and their Δe measured. This value is used to represent the cleaning effect and is defined as the color difference between the white cloth and the stained cloth after washing.

Mathematically, Δe is defined as:

ΔE＝[(ΔL)2+(Δa)2+(Δb)2]1/2

where Δl is a measure of the difference in darkness between the wash cloth and the white cloth; Δa and Δb are measures of the difference in red and yellow, respectively, between the two cloths. It is apparent from this equation that the lower the ΔE value, the whiter the cloth. For such color measurement techniques, reference is made to Commission International de l' Eclairage (CIE); recommendation on Uniform Colour Spaces, colour difference equations, psychometric colour terms, supply No.2 to CIE Publication, no.15, color, bureau Central de Ia CIE, paris 1978.

Herein, cleaning effectiveness is expressed in terms of a Soil Release Index (SRI):

SRI＝100-ΔE

the higher the SRI, the cleaner the cloth, sri=100 (white).

Enzyme cleaning performance against human sebum-like

Washing studies in a washing volume of 5mL determined that the esterases of SEQ ID1 to 4, i.e. the enzymes denoted TtEst, ttEst37, ttEst151, afEst2, all showed improved performance for removal of sebum from human beings, compared to control samples comprising a laundry esterase reference (Cutinase) and a laundry Lipase reference (Lipase event). The increase in SRI of 3-5 units for the experimental enzymes shown is a clear visible improvement in cleaning over the control Cutinase, and laundry Lipase reference (livepreference level). The test was performed in triplicate at 40 ℃ for 1 hour. The formulation used contained 7.5% total surfactant.

The increase in SRI of > 3 units is a clearly visible cleaning improvement for the lipases of the invention compared to the Cutinase and Lipex evanit (table 2).

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Table 2: cleaning performance of the esterases of SEQ IDs 1 to 4 (for model human sebum) shown in water or formulation + baseline commercial esterase (Cutinase) or formulation + baseline commercial laundry lipase (Lipex event) compared to the wash control.

Soil Release Index (SRI) indicative of wash performance was measured. The + -statistics relate to 95% confidence levels. This experiment shows that the esterases of SEQ ID1 to 4 have a much better anti-sebum performance than the commercial esterases (Cutinase) and lipases (Lipex Evity).

Enzyme cleaning performance against human sebum-like

A 100ml volume wash study demonstrated that the lipase of SEQ ID 4 showed improved performance for removal of sebum from humans compared to control samples including current commercial esterases (Cutinase) and lipases (Lipex evanit) (table 3). The test was performed in triplicate at 40 ℃ for 1 hour.

The formulation used contained 7.5% total surfactant.

Table 3: cleaning performance of the esterase of SEQ ID 4 (against model human sebum) shown in water or formulation + baseline commercial esterase (Cutinase) or formulation + baseline commercial laundry lipase (Lipex event) compared to the wash control.

Claims

1. A detergent composition comprising:

(i) 1 to 60 wt% of a surfactant; and

(ii) 0.0005 to 5% by weight of an esterase of the enzyme class EC 3.1.1.1 having 100% sequence identity to any of SEQ ID NOS: 3 to 4.

2. The detergent composition of claim 1 comprising from 0.1 to 10 wt% soil release polymer.

3. The detergent composition of claim 2 comprising from 0.2 to 9 wt% soil release polymer.

4. The detergent composition of claim 2 comprising from 0.25 to 8 wt% soil release polymer.

5. The detergent composition of claim 2 comprising from 0.5 to 6 wt% soil release polymer.

6. The detergent composition of claim 2 comprising 1 to 5 wt% soil release polymer.

7. The detergent composition of any of claims 2-6, wherein the soil release polymer is a polyester-based soil release polymer.

8. The detergent composition of claim 7, wherein the polyester-based soil release polymer is a polyethylene terephthalate and/or polytrimethylene terephthalate-based soil release polymer.

9. The detergent composition of claim 8, wherein the polyester-based soil release polymer is a polytrimethylene terephthalate-based soil release polymer.

10. The detergent composition of claim 1, wherein the detergent composition comprises an alkoxylated polyamine.

11. The detergent composition of claim 10, wherein the alkoxylated polyamine is present in an amount of 0.1 to 8 wt%.

12. The detergent composition of claim 10, wherein the alkoxylated polyamine is present in an amount of 0.2 to 6 wt%.

13. The detergent composition of claim 10, wherein the alkoxylated polyamine is present in an amount of 0.5 to 5 wt%.

14. The detergent composition of claim 1, wherein the detergent composition is a laundry detergent composition.

15. The detergent composition of claim 14, wherein the laundry detergent composition is a liquid or powder detergent.

16. The detergent composition of claim 14, wherein the laundry detergent composition is a liquid detergent.

17. A laundry detergent composition according to claim 14, wherein the surfactant comprises an anionic surfactant and/or a nonionic surfactant.

18. The laundry detergent composition according to claim 17, wherein the surfactant comprises both anionic and nonionic surfactants.

19. The detergent composition of claim 1, further comprising an additional enzyme selected from the group consisting of: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases.

20. The detergent composition of claim 1, further comprising an additional ingredient selected from the group consisting of: fluorescent agents, fragrances, hueing dyes and polymers, and mixtures thereof.

21. The detergent composition of claim 1 comprising from 2 to 50 wt% surfactant.

22. The detergent composition of claim 1 comprising 3 to 45 wt% surfactant.

23. The detergent composition of claim 1 comprising from 5 to 40 wt% surfactant.

24. The detergent composition of claim 1 comprising from 6 to 40 wt% surfactant.

25. A detergent composition according to claim 1 comprising from 0.005 to 2.5 wt% of an esterase of enzyme class EC 3.1.1.1 having 100% sequence identity to any of SEQ ID NOs 3 to 4.

26. A detergent composition according to claim 1 comprising from 0.01 to 1% by weight of an esterase of enzyme class EC 3.1.1.1 having 100% sequence identity to any of SEQ ID NOs 3 to 4.

27. A method of treating a fabric substrate having a sebum stain, the method comprising adding an esterase of enzyme class EC 3.1.1.1 having 100% sequence identity to any of SEQ ID NOs 3 to 4 to a detergent composition comprising 1 to 60 wt% of a surfactant; and subsequently treating the fabric substrate with sebum stains with the composition.

28. Use of an esterase of the enzyme class EC 3.1.1.1 having 100% sequence identity to any of SEQ ID nos. 3 to 4 for improving the cleaning of sebum stains on fabrics.