CN113166689A - Detergent composition - Google Patents

Detergent composition Download PDF

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Publication number
CN113166689A
CN113166689A CN201980076666.6A CN201980076666A CN113166689A CN 113166689 A CN113166689 A CN 113166689A CN 201980076666 A CN201980076666 A CN 201980076666A CN 113166689 A CN113166689 A CN 113166689A
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Prior art keywords
detergent composition
fatty acid
acid amide
surfactant
seq
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CN201980076666.6A
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Chinese (zh)
Inventor
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
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Unilever IP Holdings BV
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Unilever IP Holdings BV
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Publication of CN113166689A publication Critical patent/CN113166689A/en
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    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
    • C11D2111/12—

Abstract

The present invention provides a detergent composition comprising: (i)1 to 60 wt% of a surfactant; and (ii)0.0005 to 5 wt.% of a fatty acid amide hydrolase; and methods of using and use of said enzymes for improved cleaning of sebum stains on fabrics, wherein the fatty acid amide hydrolase has at least 70% sequence identity to SEQ ID No. 1.

Description

Detergent composition
Technical Field
The present invention relates to detergent compositions, more particularly to laundry detergent compositions, comprising novel fatty acid amide hydrolase enzymes.
Background
Sebum is oily dirt that remains as a stain that is difficult to remove from clothing that is worn. The challenge of effective sebum removal remains elusive given the drive to encourage users to wash at lower temperatures. 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 the removal of dirt from the collar/cuff because it is easier to remove liquid body oils from the garment than to remove 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 incorporation of novel fatty acid amide hydrolases in detergent compositions improves sebum removal from fabrics.
In one aspect, the present invention provides a detergent composition comprising:
(i)1 to 60 wt%, preferably 2to 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)0.0005 to 5% by weight, preferably 0.005 to 2.5% by weight, more preferably 0.01 to 1% by weight of a fatty acid amide hydrolase,
wherein the fatty acid amide hydrolase has at least 70% sequence identity to SEQ ID NO 1.
Preferably, the fatty acid amide hydrolase has 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 SEQ ID No. 1.
Most preferably, the fatty acid amide hydrolase has 1100% sequence identity to SEQ ID NO.
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% of a soil release polymer, more preferably a 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 alkoxylated polyamine, preferably at a level 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 anionic and nonionic surfactants.
Preferred detergent compositions, especially laundry detergent compositions, further comprise an additional enzyme selected from the group consisting of: lipases, 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, shading dyes and polymers and mixtures thereof.
In another aspect, the present invention provides a method of treating a fabric substrate having sebum stains, the method comprising adding a fatty acid amide hydrolase having sequence identity to SEQ ID No.1 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% to a detergent composition comprising from 1 to 60% by weight of a surfactant; and subsequently treating the fabric substrate with the sebum stain with the composition.
In another aspect, the present invention provides the use of a fatty acid amide hydrolase for improving the cleaning of sebum stains on fabrics, wherein the fatty acid amide 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%, most preferably 100% to improve the cleaning of sebum stains on fabrics.Detailed Description
As used herein, the indefinite article "a" or "an" and its corresponding definite article "the" mean at least one, or one or more, unless otherwise specified.
All content% of ingredients in the compositions (formulations) listed herein are% by weight based on the total formulation, unless otherwise specified.
It is to be understood that any reference to a preferred ingredient of a detergent composition is contemplated as 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 a 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 a powder, with a liquid being most preferred.
Sequence information
The sequence disclosed herein is SEQ ID NO 1.
SEQ ID1 is from Dictyostelium purpureum.
The sequence is as follows:
MSLSSSTTNSNSKNKKGNHKSDKVYDLTPYDAPRLQGFLLKSTVFLCESHYLKNSFLSTLYVKNKVPVITQFNTDNMPTFYPIVEKQPEGDFKFKKYFAEDIFLDQNLIDICQSSSQNESSSSSSSSNINIPENNSIFIYNKLYKSNKASPNDILNNFIEVKNHSDEQSPPLAAFIKVLESDIKEQANQSSERWKNKEPLSILDGVPISIKDELDQIGYHTTCGTTFLSKCYPNVKEEDSFVAKKLRERGAILVGKNNMHEIGISTLGYNTHFGFTRNPYNINHYPGGSSSGSAASVSSGLNPISIGCDGGGSIRVPASLCGVVGIKPTFARVSHGGVFELCYSVGHIGPIGSCVVDTAVGYACIAGADPKDPQSVTAEQLGGKPTLPIFTEIPMEQPLKGLKIGIFKDWINDCIEDIKEQTYKCIDILREQGAEIVEIEIPNLLVSRISQLVLILSEMKTSMKRFKNHNNEFQLDSRISLAIAGMFTAEDYIQSNRIRTYCIEELKKIFTNVDAIVTPTNGVVAPEIEKGVPQLGEVNIRAVGDLMKFVFLGNISGIPGISIPIGVTKQNNLPIGFQIMGKWWEEDLLFYISFVLERNIKFNGKPQYFNSPLKVSIENNNSNSNNNNNESTNENNKENNTNIPTNNNEENKSDK
fatty acid amide hydrolase
The fatty acid amide hydrolase preferably has at least 60% sequence identity with SEQ ID NO 1.
Preferably, the fatty acid amide hydrolase 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 SEQ ID No. 1.
Most preferably, the fatty acid amide hydrolase has 1100% sequence identity to SEQ ID NO.
Fatty acid amide hydrolases may be described as belonging to the enzyme class EC 3.5. More specifically, it can be described as belonging to enzyme class EC 3.5.1.99. .
Preferred fatty acid amide hydrolases are those from Dictyostelium purpureum.
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 2to 50 wt%, more preferably from 3 to 45 wt%, even more preferably from 5 to 40 wt%, most preferably from 6 to 40 wt% of a 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 sulphuric and sulphonic acids having an alkyl group 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 higher C by reaction, for example from tallow or coconut oil8To C18Those obtained by sulfation of alcohols, alkyl radicals C9To C20Sodium and potassium benzene-sulphonates, especially linear secondary alkyl C10To C15Sodium benzenesulfonate; and sodium alkyl glyceryl ether sulfates, 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 alkyl benzene sulfonate; an alkyl sulfate; alkyl ether sulfates; soap; alkyl (preferably methyl) ester sulfonates and mixtures thereof.
Most preferred anionic surfactants are selected from: linear alkyl benzene sulfonate; an alkyl sulfate; alkyl ether sulfates and mixtures thereof. Preferably, the alkyl ether sulphate is C with an average of 1 to 3 EO (ethoxylate) units12-C14N-alkyl ether sulfates.
Sodium Lauryl Ether Sulfate (SLES) is particularly preferred. Preferably, the linear alkylbenzene sulfonate is C11To C15Sodium alkyl benzene sulfonate. Preferably, the alkyl sulfates are linear or branched C12To C18Sodium alkyl sulfate.Sodium dodecyl sulfate is particularly preferred (SDS, also known as primary alkyl sulfate).
In liquid formulations, preferably two or more anionic surfactants are present, such as linear alkyl benzene sulphonate together with alkyl ether sulphate.
In liquid formulations, preferably, the laundry composition comprises, in addition to the anionic surfactant, an alkyl ethoxylated nonionic surfactant, preferably from 2to 8 wt% of alkyl ethoxylated nonionic surfactant.
Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having an aliphatic hydrophobic group and a reactive hydrogen atom (for example, fatty alcohols, acids or amides) with, inter alia, ethylene oxide (alone or together with propylene oxide). Preferred nonionic detergent compounds are aliphatic C8To C18Condensation 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 a C having an average ethoxylation of from 7EO to 9EO units8To C18A primary alcohol.
Preferably, the surfactant used is saturated.
Soil release polymers
The soil release polymer is preferably present at a level of from 0.1 to 10 wt%. Preferred inclusion levels of the soil release polymer are preferably 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 alkoxylated polyamines. Especially when the detergent composition is in the form of a laundry composition, it preferably comprises alkoxylated polyamines.
The preferred content of alkoxylated polyamine is 0.1 to 8 wt.%, preferably 0.2 to 6 wt.%, more preferably 0.5 to 5 wt.%. Another preferred content is1 to 4% by weight.
The alkoxylated polyamines may be linear or branched. It may be branched to the extent that it is a dendrimer. The alkoxylation can 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 polyethyleneimines, most preferably ethoxylated polyethyleneimines, having an average degree of ethoxylation of from 10 to 30, preferably from 15 to 25, in which the nitrogen atoms are ethoxylated.
Additional enzymes
In addition to the specified lipase, additional enzymes may be present in the detergent composition. It is preferred that the additional enzyme is present in the preferred laundry detergent composition.
Each enzyme, if present, is present in the laundry composition of the present invention at a level 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: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases. The preferred additional enzyme comprises a mixture 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: humicola (Humicola) (synonym thermophilic fungi (Thermomyces)), for example from h.lanuginosa (t.lanuginosus) as described in EP 258068 and EP 305216 or from h.insolens as described in WO 96/13580; pseudomonas lipases, for example from pseudomonas alcaligenes (p. alcaligenes) or pseudomonas pseudoalcaligenes (p. pseudoalcaligenes) (EP 218272), pseudomonas cepacia (p.cepacia) (EP 331376), pseudomonas stutzeri (GB 1,372,034), pseudomonas fluorescens (p. fluoroscens), pseudomonas strains SD 705(WO 95/06720 and WO 96/27002), p.wisconsinensis (WO 96/12012); bacillus lipases, for example from Bacillus subtilis (B.subtilis) (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).
Further examples are lipase variants, such as those described in WO 92/05249, WO 94/01541, EP 407225, EP 260105, 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 LipolaseTMAnd Lipolase UltraTM、LipexTMAnd LipocleanTM(Novozymes A/S)。
The process of the invention may be carried out in the presence of a phospholipase classified under EC 3.1.1.4 and/or EC 3.1.1.32. As used herein, the term phospholipase is an enzyme that is active on phospholipids.
Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified at the outer (sn-1) and middle (sn-2) positions with two fatty acids and phosphorylated at the third position; phosphoric acid, in turn, can be esterified to an amino alcohol. Phospholipases are enzymes involved in phospholipid hydrolysis. Can distinguish between various types of phospholipase activity, including phospholipase A1And A2Which hydrolyses one fatty acyl group (at the sn-1 and sn-2 positions, respectively) to form lysophospholipids; and lysophospholipase (or phospholipase B), which can hydrolyze the remaining fatty acyl groups in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterases) release diacyl glycerol or phosphatidic acid, respectively.
Proteases hydrolyze the peptides and bonds within the protein, which results in enhanced removal of protein or peptide containing stains in a laundry environment. Examples of suitable protease families include aspartic proteases; a cysteine protease; a protease of glutamate; asparagine (aspargegine) peptide lyase; serine proteases and threonine proteases. Such protease families are in the MEROPS peptidase database: (http://merops.sanger.ac.uk/) As described in (1). Serine proteases are preferred. A subtilase (subtilase) type serine protease is more preferred. The term "subtilase" refers to a subgroup of serine proteases according to Siezen et al, Protein Engng.4(1991)719-737 and Siezen et al, Protein Science 6(1997) 501-523. Serine proteases are a subset of proteases characterized by a serine at the active site that forms a covalent adduct with a substrate. Subtilases can be divided into 6 sub-classes, namely the Subtilisin (Subtilisin) family, the thermolysin (thermolase) family, the proteinase 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 Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in US7262042 and WO09/021867, as well as subtilisin (subtilisin lentitus), subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279, and the protease 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 as described in WO89/06270, WO94/25583 and WO05/040372, and chymotrypsin derived from Cellulomonas (Cellumonas) as 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 Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in US7262042 and WO09/021867, as well as subtilisin tarda, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279, and protease 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 U.S. Pat. No. 6,312,936B 1, U.S. Pat. No. 5,679,630, U.S. Pat. No. 4,760,025, U.S. Pat. No. 3,7,262,042 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
Figure BDA0003075810250000091
DuralaseTm、DurazymTm、
Figure BDA0003075810250000092
Ultra、
Figure BDA0003075810250000093
Ultra、
Figure BDA0003075810250000094
Ultra、
Figure BDA0003075810250000095
Ultra、
Figure BDA0003075810250000096
And
Figure BDA0003075810250000097
saleAll of them can be regarded as
Figure BDA0003075810250000098
Or
Figure BDA0003075810250000099
(Novozymes A/S).
The composition may use cutinases (cutinases) classified in EC 3.1.1.74. The cutinase to be used according to the invention may be of any origin. Preferably, the cutinase is of microbial origin, in particular of bacterial, fungal or yeast origin.
Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a particular strain of 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 DuramylTM、TermamylTM、Termamyl UltraTM、NatalaseTM、StainzymeTM、AmplifyTM、FungamylTMand BANTM(Novozymes A/S)、RapidaseTMAnd PurastarTM(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: fungal cellulases produced by bacillus, pseudomonas, humicola, fusarium, thielavia, acremonium, e.g. from humicola insolens, thielavia terrestris, myceliophthora thermophila and fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691,178, US 5,776,757, WO 89/09259, WO 96/029397 and WO 98/012307. Commercially available cellulases include CelluzymeTM、CarezymeTM、Celluclean TM、EndolaseTM、RenozymeTM(Novozymes A/S)、ClazinaseTMand Puradax HATM(Genencor International Inc.) and KAC-500(B)TM(Kao Corporation)。CellucleanTMIs 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 Coprinus, e.g., Coprinus cinereus, and variants thereof, such as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include GuardzymeTMAnd NovozymTM51004(Novozymes A/S)。
Further suitable enzymes are discussed in WO2009/087524, WO2009/090576, WO2009/107091, WO2009/111258 and WO 2009/148983.
The aqueous solution used in the process preferably has the enzyme present. The enzyme is preferably present in the aqueous solution used in the process at 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 stabilized using conventional stabilizers, for example polyols such as propylene glycol or glycerol; a sugar or sugar alcohol; lactic acid; boric acid or a boric acid derivative, for example an aromatic borate ester, or a phenyl boronic acid derivative, for example 4-formylphenyl boronic 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, shading dyes, polymers and chelants.
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 fluorescent agent or 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: distyrylbiphenyl compounds, such as Tinopal (trade mark) CBS-X, diamine distyrylbisonic 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 245765-13-7; 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.
The 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 ' -disulfonate, disodium 4,4' -bis { [ (4-anilino-6-morpholinyl-1, 3, 5-triazin-2-yl) ] amino } stilbene-2-2 ' -disulfonate, 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 the range of 0.0001 to 0.1g/L, more preferably 0.001 to 0.02 g/L.
Perfume
The composition preferably comprises a perfume. Many suitable examples of fragrances are provided in CTFA (Cosmetic, Toiletry and Fragrance Association)1992International layers Guide, published by CFTA Publications, and OPD 1993Chemicals layers Directory 80th annular Edition, published by Schnell Publishing Co.
Preferably, the fragrance comprises at least one of the following notes (compounds): alpha-isomethyl ionone, benzyl salicylate; citronellol; coumarin; hexyl cinnamic aldehyde; linalool; 2-methyl pentanoic acid ethyl ester; 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 cinnnamic aldehyde); cyclopentadecanolide; 2-phenylethyl phenylacetate; amyl salicylate; beta-caryophyllene; ethyl undecylenate; geranyl anthranilate; α -irone; beta-phenylethyl benzoate; α -santalol; cedrol; cedryl acetate; cedryl formate (cedry format); cyclohexyl salicylate; gamma-dodecalactone, and beta-phenylethylphenyl acetate.
Useful components of perfumes include both materials of natural and synthetic origin. They include single compounds and mixtures. Specific examples of such components can be found in the literature, for example, in the Feraroli's Handbook of flavour Ingredients,1975, CRC Press; jacobs, Synthetic Food adjuns, 1947, edited by Van nonstrand; or s.arctander, Perfume and flavour Chemicals,1969, Montclair, n.j. (USA).
It is common for multiple perfume components to be present in a formulation. In the compositions of the present invention, it is envisaged that four or more, preferably five or more, more preferably six or more, or even seven or more different perfume components will be present.
In the perfume mixture, preferably 15 to 25% by weight is top notes. Top notes are defined by Poucher (Journal of the Society of Cosmetic Chemists 6(2):80[1955 ]). Preferred top notes are selected from citrus oil, linalool, linalyl acetate, lavender, dihydromyrcenol, rose oxide and cis-3-hexanol.
The international daily-use perfumery association has issued a list of fragrance ingredients (fragrances) in 2011. (http:// www.ifraorg.org/en-us/ingredients#.U7Z4hPldWzk)
The international daily fragrance institute provides a database of fragrances (fragrances) with safety information.
Perfume top notes can be used to suggest the 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 a boiling point of less than 300 ℃, preferably 100 ℃ and 250 ℃. It is also advantageous to encapsulate perfume components having a low Clog P (i.e. those that will have a higher tendency to partition into water), preferably having a Clog P of less than 3.0. Materials having relatively low boiling points and relatively low CLog P have been referred to as perfume ingredients of "delayed blooming" and comprise one or more of the following materials: allyl hexanoate, amyl acetate, amyl propionate, anisaldehyde, anisole, benzaldehyde, benzyl acetate, benzyl acetone, benzyl alcohol, benzyl formate, benzyl isovalerate, benzyl propionate, β - γ hexenol, camphor gum, l-carvone, d-carvone, cinnamyl alcohol, cinnamyl formate (cinamyl form), cis-jasmone, cis-3-hexenyl acetate, cuminol, cyclal c, dimethyl benzyl methanol acetate, ethyl acetoacetate, ethyl ethylacetoacetate, ethylamyl ketone, ethyl benzoate, ethyl butyrate, ethylhexyl ketone, ethylphenyl acetate, eucalyptol, eugenol, fenchyl acetate (fenchyl acetate), flor acetate (tricyclodecenyl acetate), tricyclodecene propionate, geraniol, hexenol, hexenyl acetate, hexyl acetate, Hexyl formate, solanol (hydroacetylalcohol), hydroxycitrocitronellal, indanone, isoamyl alcohol, isomenthone, isopulegyl acetate, isoquinolinone, ligustral, linalool oxide, linalyl formate, menthone, menthylacetone, methyl amyl ketone, methyl anthranilate, methyl benzoate, methyl benzyl acetate, methyl eugenol, methyl heptenone, methyl heptyne carbonate, methyl heptyne ketone, methyl hexyl ketone, methyl phenyl methyl acetate, methyl salicylate, methyl-n-methyl anthranilate, nerol, octolactone, octanol, p-cresol methyl ether, p-methoxyacetophenone, p-methylacetone, phenyl acetaldehyde, phenyl ethyl acetate, phenyl ethyl alcohol, Phenylethyldimethylcarbinol, prenyl acetate, propyl borate, pulegone, rose oxide, safrole, 4-terpinenol (4-terpinenol), alpha-terpinenol and/or phenylacetaldehyde dimethanol acetal (viridine). It is common for multiple perfume components to be present in a 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 employed with the present invention are the 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, dried nutmeg skin (Mace) extract, neroli, nutmeg, spearmint, sweet violet leaves and valerian.
It is preferred that the laundry treatment composition is devoid of peroxygen bleach, such as sodium percarbonate, sodium perborate and peracids.
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 wt% of the composition.
Dyes are described in Color Chemistry Synthesis, Properties and Applications of Organic Dyes and Pigments, (H Zollinger, Wiley VCH, Surich, 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 (400-700nm) of greater than 5000L mol-1cm-1Preferably greater than 10000L mol-1cm-1The extinction coefficient of (a). The color of the dye is blue or violet.
Preferred shading dye chromophores are azo, azine, anthraquinone and triphenylmethane.
Azo, anthraquinone, phthalocyanine and triphenylmethane dyes preferably carry a net anionic charge or no charge. Azines preferably carry a net anionic or cationic charge. During the washing or rinsing step of the washing process, a blue or violet shading dye is deposited onto the fabric, providing a visible shade 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 a 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 dyes preferably contain a heterocyclic ring, and are most preferably thiophene dyes. The monoazo dyes are preferably alkoxylated and are 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:
Figure BDA0003075810250000141
Figure BDA0003075810250000151
the disazo dye is preferably a sulfonated disazo dye. Preferred examples of sulfonated 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 disazo dyes are discussed in WO2012/054058 and WO 2010/151906.
Examples of alkoxylated disazo dyes are:
Figure BDA0003075810250000152
thiophene dyes are available from Milliken under the trade names Liquitin Violet DD and Liquitin 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 having CAS number 72749-80-5, acid blue 59, and phenazine dyes selected from the group consisting of:
Figure BDA0003075810250000153
wherein:
X3selected from: -H; -F; -CH3；-C2H5；-OCH3(ii) a and-OC2H5；
X4Selected from: -H; -CH3；-C2H5；-OCH3(ii) a and-OC2H5；
Y2Selected from: -OH; -OCH2CH2OH；-CH(OH)CH2OH；-OC(O)CH3(ii) a And C (O) OCH3。
The 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 potency of the hueing dye, which depends on the class and the specific potency within any particular class. As mentioned above, the hueing dye is a blue or violet hueing dye.
Mixtures of hueing dyes may be used.
Most preferably, the hueing dye is a reactive blue anthraquinone dye covalently linked to an alkoxylated polyethyleneimine. The alkoxylation is preferably selected from 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 polyethyleneimine is:
Figure BDA0003075810250000161
(Structure I).
Polymer and method of making same
The composition may comprise one or more additional polymers. Examples are carboxymethylcellulose, poly (ethylene glycol), poly (vinyl alcohol), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.
Chelating agents
The chelant may or may not be present in the detergent composition. If present, the chelating agent is present in an amount of 0.01 to 5 wt%.
Examples of phosphonic acid (or salts thereof) chelating agents are: 1-hydroxyethylidene-1, 1-diphosphonic acid (HEDP); diethylenetriamine penta (methylene phosphonic acid) (DTPMP); hexamethylenediamine tetra (methylene phosphonic acid) (HDTMP); aminotris (methylenephosphonic Acid) (ATMP); ethylenediaminetetra (methylenephosphonic acid) (EDTMP); tetramethylenediaminetetra (methylenephosphonic acid) (TDTMP); and phosphinobutane tricarboxylic acid (PBTC).
Examples
The invention will be illustrated by the following non-limiting examples.
Examples
Cloning including sequence information&Expression ofThe DNA sequence encoding the fatty acid amide hydrolase was synthesized by codon optimization for E.coli. The DNA sequence was amplified using primers with restriction sites for EcoRI and HindIII. The resulting PCR product was digested with EcoRI and HindIII, purified, and ligated into the protein expression vector pMal2cx digested with the same restriction enzymes to obtain a plasmid for expressing the C-terminal MBP-tagged FAAH protein. Coli XL2 blue was used as a cloning strain and transformed using the heat shock method. After plasmid isolation, the plasmid was sequenced and the cloning was confirmed to be successful. Coli BL21(DE3) was transformed (heat shock) and used as expression strain for protein production.
(SEQ ID 1):
MSLSSSTTNSNSKNKKGNHKSDKVYDLTPYDAPRLQGFLLKSTVFLCESHYLKNSFLSTLYVKNKVPVITQFNTDNMPTFYPIVEKQPEGDFKFKKYFAEDIFLDQNLIDICQSSSQNESSSSSSSSNINIPENNSIFIYNKLYKSNKASPNDILNNFIEVKNHSDEQSPPLAAFIKVLESDIKEQANQSSERWKNKEPLSILDGVPISIKDELDQIGYHTTCGTTFLSKCYPNVKEEDSFVAKKLRERGAILVGKNNMHEIGISTLGYNTHFGFTRNPYNINHYPGGSSSGSAASVSSGLNPISIGCDGGGSIRVPASLCGVVGIKPTFARVSHGGVFELCYSVGHIGPIGSCVVDTAVGYACIAGADPKDPQSVTAEQLGGKPTLPIFTEIPMEQPLKGLKIGIFKDWINDCIEDIKEQTYKCIDILREQGAEIVEIEIPNLLVSRISQLVLILSEMKTSMKRFKNHNNEFQLDSRISLAIAGMFTAEDYIQSNRIRTYCIEELKKIFTNVDAIVTPTNGVVAPEIEKGVPQLGEVNIRAVGDLMKFVFLGNISGIPGISIPIGVTKQNNLPIGFQIMGKWWEEDLLFYISFVLERNIKFNGKPQYFNSPLKVSIENNNSNSNNNNNESTNENNKENNTNIPTNNNEENKSDK
fermentation (harvesting) and purification
Protein production was performed in 2L Erlenmeyer flasks with 1L LB medium and the appropriate antibiotic for plasmid selection (ampicillin, 100. mu.g/mL). LB-medium was inoculated with 1-3% (v/v) of the preculture and incubated at 37 ℃ and 180rpm until OD was reached6000.6. Gene expression was induced by adding IPTG to a final concentration of 1mM and was carried out at 20 ℃ and 180rpm for 3 h. 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 (20mM Tris-HCl, pH 7.4, 200mM NaCl, 1mM EDTA, 10mL buffer for 1g of cell wet weight) and sonicating the cells on ice. Protein purification was performed using a 1mL MBPTrap HP column and AKTA purification system for affinity chromatography by MBP-tag. Protein elution was performed via a linear gradient for 30 min using buffers with increasing maltose concentration (20mM Tris-HCl, pH 7.4, 200mM NaCl, 1mM EDTA, 10mM maltose). The eluted fractions were identified by absorbance (280nm) and applied to SDS-PAGE. Fractions containing the protein of interest were pooled and dialyzed overnight against 5L of buffer (25mM Tris-HCl, pH 8.0, 500mM NaCl). The dialyzed protein was supplemented with 0.005% (v/v) sodium azide and 10% (v/v) glycerol for freezing and stored at-80 ℃.
Biological analysis
Of protein concentrationMeasurement of
The total amount of protein of the enzyme sample was estimated by using Sigma-Aldrich (bicinchoninic acid) BCA assay kit, and working reagents were prepared as indicated in the user manual. The BCA reagent was prepared by mixing solution A [ 1% (w/v) sodium salt form of dioctanoclonic 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 (2mg/mL) were made in deionized water to generate a 7-point standard curve. To perform this protein assay, BCA reagent (200 μ L) was added to wells of a 96-well plate, followed by sample protein dilution (20 μ L). Microtiter plates (MTP) were sealed and incubated at 37 ℃ for 30 minutes. After incubation, the absorbance at 540nm was measured on a spectrophotometer.
Determination of enzyme puritySamples of esterase-containing protein (20. mu.L) were prepared in SDS-PAGE loading buffer and heated at 70 ℃ for 10 min, then run on 4-12% NuPage Bis-Tris gels in MOPS buffer at 170V. The PageRulerPlus molecular weight markers were run on gel with the samples to determine molecular mass. Each gel was stained using GelCode Blue Safe Protein Stain according to the manufacturer's protocol.
Application test
Composition and application of model human sebum to fabricTable 1A shows the composition of human 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 model sebum and then 100. mu.L was applied to a 10X 10cm sample of polycotton preheated to 60 ℃. Wicking of the stain was promoted by allowing the stain to dry overnight at 60 ℃, uniformity of staining was confirmed by colorimetric determination of SRI values across the sample, which was subsequently cut into smaller 30mm diameter circles enabling assembly in 6-well microtiter plates for subsequent wash tests.
TABLE 1 (A) composition of the human sebum tested. The composition of human sebum proposed by Nikkari1974, In Ro2005, Stefaniak 2010 is shown In comparison (B). A model human sebum-like model was designed to mimic the literature description.
Figure BDA0003075810250000191
Figure BDA0003075810250000201
Figure BDA0003075810250000211
Wash study for enzymatic cleaning Performance on human sebum-like
A pre-wash reading was taken on a 30mm diameter sebum stain to measure stain strength. Wash studies were performed in 5mL volumes (1 hour at 100rpm in 6-well plates at 40 ℃) or 100mL (1 hour at 100rpm in a glass vial at 40 ℃). The enzyme was present at 25mg/L in a 7.5% surfactant formulation at 2 g/L. The stain was then rinsed three times after washing to completely remove the wash liquor and any remaining enzyme. After drying, the stained plates were digitally scanned and their Δ Ε was measured. This value is used to indicate the cleaning effect and is defined as the color difference between white cloth and soiled cloth after washing.
Mathematically, Δ E is defined as:
ΔE＝[(ΔL)2+(Δa)2+(Δb)2]1/2
wherein Δ L is a measure of the difference in darkness between the wash cloth and the white cloth; Δ a and Δ b are measures of the difference in red and yellow, respectively, between the two cloths. It is evident from this equation that the lower the Δ Ε value, the whiter the fabric. For this color measurement technique, reference is made to Commission International de l' eclairage (cie); recommendation on Uniform color Spaces, color difference equations, psychometric color fields, supplement No.2to CIE Publication, No.15, Colormetric, Bureau Central de Ia CIE, Paris 1978.
Herein, the cleaning effect is expressed in the form of the Stain Release Index (SRI):
SRI＝100-ΔE
the higher the SRI, the cleaner the cloth, the SRI is 100 (white).
Enzymatic cleaning performance against human sebum
A wash study at a wash volume of 5mL determined that the Fatty Acid Amidohydrolase (FAAH) showed improved performance for removal of human sebum compared to control samples comprising a laundry esterase benchmark (Cutinase) and a laundry Lipase benchmark (Lipase event). The increase in SRI for the indicated experimental enzymes was a significant improvement over the control enzyme (Cutinase) and laundry Lipase benchmark (Lipase event). The tests were performed in triplicate at 40 ℃ for 1 hour. The formulation used contained 7.5% total surfactant.
An increase in SRI is a clear visible cleaning improvement for the fatty acid amide hydrolase of the invention compared to Cutinase and particularly Lipex event (table 2).
Figure BDA0003075810250000221
Table 2: the cleaning performance of the fatty acid amide hydrolase of SEQ ID1 (against model human sebum) shown in water or formulation + benchmark commercial esterase (Cutinase) or formulation + benchmark commercial laundry lipase (Lipex event) compared to the wash control.
Stain Release Index (SRI) indicating wash performance was measured. The ± statistics relate to 95% confidence levels. This experiment shows that the fatty acid amide hydrolase of SEQ ID1 has better anti-sebum properties than the commercial esterase (Cutinase) and especially the lipase (Lipex event).
Enzymatic cleaning performance against human sebum
A washing study at a volume of 100ml confirmed that the fatty acid amide hydrolase of SEQ ID1 showed improved performance for removal of human sebum compared to a control sample comprising the current commercial lipase (Lipex event). It was also found to be roughly equivalent to esterase (Cutinase) (table 3). The test was performed in triplicate at 40 ℃ for 1 hour. The formulation used contained 7.5% total surfactant.
Figure BDA0003075810250000231
Table 3: the cleaning performance of the fatty acid amide hydrolase of SEQ ID1 (against model human sebum) shown in water or formulation + benchmark commercial esterase (Cutinase) or formulation + benchmark commercial laundry lipase (Lipex event) compared to the wash control.
Figure IDA0003075810310000011
Figure IDA0003075810310000021
Figure IDA0003075810310000031

Claims (12)

1. A detergent composition comprising:
(i)1 to 60 wt%, preferably 2to 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 wt.%, preferably from 0.005 to 2.5 wt.%, more preferably from 0.01 to 1 wt.% of a fatty acid amide hydrolase;
wherein the fatty acid amide hydrolase has at least 70% sequence identity to SEQ ID NO 1.
2. The detergent composition according to claim 1, wherein the fatty acid amide hydrolase has 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 SEQ ID No. 1.
3. The detergent composition of claim 1 or claim 2, wherein the fatty acid amide hydrolase has 1100% sequence identity to SEQ ID NO.
4. The detergent composition according to any preceding claims comprising 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% of a soil release polymer, more preferably a polyester based soil release polymer.
5. The detergent composition according to claim 4, wherein 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.
6. The detergent composition according to any preceding claims, wherein the detergent composition comprises alkoxylated polyamine, preferably at a level of from 0.1 to 8 wt%, more preferably from 0.2 to 6 wt%, most preferably from 0.5 to 5 wt%.
7. The detergent composition according to any preceding claims, wherein the detergent composition is a laundry detergent composition, preferably the laundry detergent composition is a liquid or powder, most preferably a liquid detergent.
8. A laundry detergent composition according to claim 7, wherein the surfactant comprises an anionic surfactant and/or a nonionic surfactant, preferably both an anionic surfactant and a nonionic surfactant.
9. A detergent composition, preferably a laundry detergent composition, according to any preceding claims, further comprising an additional enzyme selected from the group consisting of: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases.
10. A detergent composition, preferably a laundry detergent composition, according to any preceding claims, further comprising an additional ingredient selected from the group consisting of: fluorescers, perfumes, shading dyes and polymers, and mixtures thereof.
11. A method of treating a fabric substrate having sebum stains, the method comprising adding a fatty acid amide hydrolase having sequence identity to SEQ ID NO 1 of 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% to a detergent composition comprising from 1 to 60% by weight of a surfactant; and subsequently treating the fabric substrate having the sebum stain with the composition added to a detergent composition comprising 1 to 60 wt% of a surfactant; and subsequently treating the fabric substrate with the sebum stain with the composition.
12. Use of a fatty acid amide hydrolase having a sequence identity to SEQ ID NO 1 of 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% to improve the cleaning of sebum stains on fabrics.
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