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EP3884024A1 - Reinigungsmittelzusammensetzung - Google Patents

Reinigungsmittelzusammensetzung

Info

Publication number
EP3884024A1
EP3884024A1 EP19795212.0A EP19795212A EP3884024A1 EP 3884024 A1 EP3884024 A1 EP 3884024A1 EP 19795212 A EP19795212 A EP 19795212A EP 3884024 A1 EP3884024 A1 EP 3884024A1
Authority
EP
European Patent Office
Prior art keywords
detergent composition
enzyme
seq
sterol esterase
composition according
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
EP19795212.0A
Other languages
English (en)
French (fr)
Other versions
EP3884024B1 (de
Inventor
Jens Carlo BENNINGHOFF
Simone Antonio DE ROSE
Michail ISUPOV
Dietmar Andreas LANG
Jennifer Ann LITTLECHILD-BOND
Sarah Rebecca SMITH
Mark Lawrence THOMPSON
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Unilever Global IP Ltd
Unilever IP Holdings BV
Original Assignee
Unilever Global IP Ltd
Unilever IP Holdings BV
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
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Publication of EP3884024A1 publication Critical patent/EP3884024A1/de
Application granted granted Critical
Publication of EP3884024B1 publication Critical patent/EP3884024B1/de
Active legal-status Critical Current
Anticipated expiration legal-status Critical

Links

Classifications

    • 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
    • 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
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • the invention concerns a detergent composition, more specifically a laundry detergent composition, said composition comprising a novel sterol esterase enzyme.
  • Sebum is an oily soil which has remained a difficult stain to remove from worn garments.
  • Sebum consists of a 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.
  • the present invention provides a liquid detergent composition comprising:
  • the sterol esterase enzyme has at least 60%, preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, sequence identity to any one of SEQ ID NO: 1 or 2.
  • the sterol esterase enzyme has 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 one of SEQ ID NO: 1 or 2.
  • the sterol esterase enzyme has 100% sequence identity to any one of SEQ ID NO: 1 or 2.
  • 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 released polymer.
  • the polyester soil release polymer is a polyethylene and/or polypropylene terephthalate based soil release polymer, preferably a polypropylene terephthalate based soil release polymer.
  • the detergent composition comprises an 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.%.
  • the detergent composition is a laundry detergent composition.
  • the surfactant in the detergent composition comprises anionic and/or nonionic surfactant, in one case comprising both anionic and nonionic surfactant.
  • Preferred detergent compositions particularly laundry detergent compositions additionally comprise a further enzyme selected from the group consisting of: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
  • a further enzyme selected from the group consisting of: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
  • Preferred detergent compositions particularly laundry detergent compositions additionally comprise a further ingredient selected from fluorescent agent, perfume, shading dyes and polymers, and mixtures thereof.
  • the present invention provides a method of treatment of a fabric substrate with a sebum stain, said method comprising incorporation of a sterol esterase enzyme 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%, most preferably 100%, sequence identity to any one of SEQ ID NO: 1 or 2 into a detergent composition comprising from 1 to 60 wt.% of a surfactant; and subsequent treatment of a fabric substrate with a sebum stain, with said composition.
  • the present invention provides the use of a sterol esterase enzyme to improve cleaning of sebum stains on fabric, wherein the sterol esterase enzyme has 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 any one of SEQ ID NO: 1 or 2.
  • indefinite article“a” or“an” and its corresponding definite article“the” as used herein means at least one, or one or more, unless specified otherwise.
  • the detergent composition is a liquid.
  • the detergent composition can be applied to any suitable substrate.
  • Particularly preferred substrates are textiles.
  • Particularly preferred detergent compositions are laundry detergent compositions.
  • sequences disclosed herein are SEQ ID NO. 1 or 2.
  • SEQ ID 1 is a truncated sequence derived from SEQ ID NO. 2 from Corynebacterium The sequence is:
  • SEQ ID 2 is from Corynebacterium
  • the sterol esterase enzyme has at least 60% sequence identity to any one of SEQ ID NO: 1 or 2.
  • the sterol esterase enzyme 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 one of SEQ ID NO: 1 or 2.
  • the sterol esterase enzyme has 100% sequence identity to any one of SEQ ID NO: 1 or 2.
  • the sterol esterase can be described as being of enzyme class EC 3.1.1.13.
  • Preferred sterol esterases are from Corynebacterium
  • the detergent composition comprises surfactant (which may include 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.% of surfactant.
  • the detergent composition (preferably a laundry detergent composition) comprises anionic and/or nonionic surfactant, preferably comprising both anionic and nonionic surfactant.
  • Suitable anionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher alkyl radicals.
  • suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher Cs to Cie alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl Cg to C20 benzene sulphonates, particularly sodium linear secondary alkyl C10 to C15 benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
  • the anionic surfactant is preferably selected from: linear alkyl benzene sulphonate; alkyl sulphates; alkyl ether sulphates; soaps; alkyl (preferably methyl) ester sulphonates, and mixtures thereof.
  • the most preferred anionic surfactants are selected from: linear alkyl benzene sulphonate; alkyl sulphates; alkyl ether sulphates and mixtures thereof.
  • the alkyl ether sulphate is a C12-C14 n-alkyl ether sulphate with an average of 1 to 3EO (ethoxylate) units.
  • Sodium lauryl ether sulphate is particularly preferred (SLES).
  • the linear alkyl benzene sulphonate is a sodium Cn to C15 alkyl benzene sulphonates.
  • the alkyl sulphates is a linear or branched sodium C12 to Cie alkyl sulphates.
  • Sodium dodecyl sulphate is particularly preferred, (SDS, also known as primary alkyl sulphate).
  • liquid formulations preferably two or more anionic surfactant are present, for example linear alkyl benzene sulphonate together with an alkyl ether sulphate.
  • the laundry composition in addition to the anionic surfactant comprises alkyl exthoylated non-ionic surfactant, preferably from 2 to 8 wt.% of alkyl ethoxylated non-ionic 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, aliphatic alcohols, acids or amides, especially ethylene oxide either alone or with propylene oxide.
  • Preferred nonionic detergent compounds are the condensation products of aliphatic Cs to Cis primary or secondary linear or branched alcohols with ethylene oxide.
  • nonionic detergent compound is the alkyl ethoxylated non-ionic surfactant is a Cs to Cie primary alcohol with an average ethoxylation of 7EO to 9EO units.
  • surfactants used are saturated.
  • the soil release polymer is preferably present at a level of from 0.1 to 10 wt.%. Preferred levels of inclusion 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.%.
  • the soil release polymer is a polyester based soil released polymer. More preferably the polyester soil release polymer is a polyethylene and/or polypropylene terephthalate based soil release polymer, most preferably a polypropylene terephthalate based soil release polymer.
  • Suitable polyester based soil release polymers are described in WO 2014/029479 and WO 2016/005338.
  • the detergent composition preferably comprises an alkoxylated polyamine. Especially when the detergent composition is in the form of a laundry composition, it is preferred that an alkoxylated polyamine is included. Preferred levels of alkoxylated polyamine range from 0.1 to 8 wt.%, preferably from 0.2 to 6 wt.%, more preferably from 0.5 to 5 wt.%. Another preferred level is from 1 to 4 wt.%.
  • the alkoxylated polyamine may be linear or branched. It may be branched to the extent that it is a dendrimer.
  • the alkoxylation may typically be ethoxylation or propoxylation, or a mixture of both. Where a nitrogen atom is alkoxylated, a preferred average degree of alkoxylation is from 10 to 30, preferably from 15 to 25.
  • a preferred material is alkoxylated polyethylenimine, most preferably ethoxylated
  • polyethyleneimine with an average degree of ethoxylation being from 10 to 30 preferably from 15 to 25, where a nitrogen atom is ethoxylated.
  • Additional enzymes other than the specified lipase may be present in the detergent composition. It is preferred that additional enzymes are present in the preferred laundry detergent composition.
  • the level of each enzyme in the laundry composition of the invention is from 0.0001 wt.% to 0.1 wt.%.
  • Levels of enzyme present in the composition preferably relate to the level of enzyme as pure protein.
  • Preferred further enzymes include those in the group consisting of: lipases, proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
  • Said preferred additional enzymes include a mixture of two or more of these enzymes.
  • the further 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 lipases from Humicola (synonym Thermomyces), e.g. 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, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes (EP 218 272), P. cepacia (EP 331 376), P. stutzeri (GB 1 ,372,034), P.
  • lipase variants such as those described in WO 92/05249,
  • LipolaseTM and Lipolase UltraTM LipexTM and LipocleanTM (Novozymes A/S).
  • the method of the invention may be carried out in the presence of phospholipase classified as EC 3.1.1.4 and/or EC 3.1.1.32.
  • phospholipase is an enzyme which has activity towards phospholipids.
  • Phospholipids such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1 ) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol.
  • Phospholipases are enzymes which participate in the hydrolysis of phospholipids.
  • phospholipases Ai and A2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
  • lysophospholipase or phospholipase B
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • proteases hydrolyse bonds within peptides and proteins, in the laundry context this leads to enhanced removal of protein or peptide containing stains.
  • suitable proteases families include aspartic proteases; cysteine proteases; glutamic proteases; aspargine peptide lyase; serine proteases and threonine proteases.
  • Such protease families are described in the MEROPS peptidase database (http://merops.sanqer.ac.uk/) ⁇ Serine proteases are preferred.
  • Subtilase type serine proteases are more preferred.
  • subtilases refers to a sub-group of serine protease 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 subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
  • the subtilases may be divided into 6 sub divisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • subtilases are those derived from Bacillus such as Bacillus lentus, B.
  • trypsin-like proteases examples include trypsin (e.g. of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 05/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 05/052161 and WO 05/052146.
  • protease is a subtilisins (EC 3.4.21.62).
  • subtilases are those derived from Bacillus such as Bacillus lentus, B.
  • subtilis alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and W009/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO89/06279 and protease PD138 described in (WO93/18140).
  • the subsilisin is derived from Bacillus, preferably Bacillus lentus, B. alkalophilus, B. subtilis,
  • subtilisin is derived from Bacillus gibsonii or Bacillus Lentus.
  • Suitable commercially available protease enzymes include those sold under the trade names names Alcalase®, Blaze®; DuralaseTm, DurazymTm, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Primase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Neutrase®, Everlase® and Esperase® all could be sold as Ultra® or Evity® (Novozymes A/S).
  • the composition may use cutinase, classified in EC 3.1.1.74.
  • the cutinase used according to the invention may be of any origin.
  • cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
  • Suitable amylases 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 special strain of B. licheniformis, described in more detail in GB 1 ,296,839, or the Bacillus sp. strains disclosed in WO 95/026397 or WO
  • amylases are DuramylTM, TermamylTM, Termamyl UltraTM, NatalaseTM, StainzymeTM, AmplifyTM, FungamylTM and BANTM (Novozymes A/S), RapidaseTM and 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 the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced 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, CellucleanTM, EndolaseTM,
  • RenozymeTM Novozymes A/S
  • ClazinaseTM and Puradax HATM
  • KAC-500(B)TM Kao Corporation
  • CellucleanTM 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 Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, and WO 98/15257. Commercially available peroxidases include GuardzymeTM and NovozymTM 51004 (Novozymes A/S).
  • the aqueous solution used in the method preferably has an enzyme present.
  • the enzyme is preferably present in the aqueous solution used in the method at a concentration in the range from 0.01 to 10ppm, preferably 0.05 to 1 ppm.
  • Any enzyme present in the composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in e.g. WO 92/19709 and WO 92/19708.
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid
  • detergent compositions preferably laundry detergent compositions
  • the composition preferably comprises a fluorescent agent (optical brightener).
  • fluorescent agents are well known and many such fluorescent agents are available commercially.
  • these fluorescent agents are supplied and used in the form of their alkali metal salts, for example, the sodium salts.
  • the total amount of the fluorescent agent or agents used in the composition is generally from 0.0001 to 0.5 wt.%, preferably 0.005 to 2 wt.%, more preferably 0.01 to 0.1 wt.%.
  • Preferred classes of fluorescer are: Di-styryl biphenyl compounds, e.g. Tinopal (Trade Mark) CBS-X, Di-amine stilbene di-sulphonic acid compounds, e.g. Tinopal DMS pure Xtra and Blankophor (Trade Mark) HRH, and Pyrazoline compounds, e.g. Blankophor SN.
  • Di-styryl biphenyl compounds e.g. Tinopal (Trade Mark) CBS-X
  • Di-amine stilbene di-sulphonic acid compounds e.g. Tinopal DMS pure Xtra and Blankophor (Trade Mark) HRH
  • Pyrazoline compounds e.g. Blankophor SN.
  • Preferred fluorescers are fluorescers with 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; CAS-No 27344-41-8.
  • fluorescers are: sodium 2 (4-styryl-3-sulfophenyl)-2H-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-sulphostyryl)biphenyl.
  • the aqueous solution used in the method has a fluorescer present.
  • the fluorescer is present in the aqueous solution used in the method preferably in the range from 0.0001 g/l to 0.1 g/l, more preferably 0.001 to 0.02 g/l.
  • the composition preferably comprises a perfume.
  • perfumes are provided in the CTFA (Cosmetic, Toiletry and Fragrance Association) 1992 International Buyers Guide, published by CFTA Publications and OPD 1993 Chemicals Buyers Directory 80th Annual Edition, published by Schnell Publishing Co.
  • the perfume comprises at least one note (compound) from: alpha-isomethyl ionone, benzyl salicylate; citronellol; coumarin; hexyl cinnamal; linalool; pentanoic acid, 2- methyl-, ethyl ester; octanal; benzyl acetate; 1 ,6-octadien-3-ol, 3,7-dimethyl-, 3-acetate; cyclohexanol, 2-(1 ,1-dimethylethyl)-, 1-acetate; delta-damascone; beta-ionone; verdyl acetate; dodecanal; hexyl cinnamic aldehyde; cyclopentadecanolide; benzeneacetic acid, 2- phenylethyl ester; amyl salicylate; beta-caryophyllene; ethyl undecylenate
  • Useful components of the perfume include materials of both natural and synthetic origin. They include single compounds and mixtures. Specific examples of such components may be found in the current literature, e.g., in Fenaroli's Handbook of Flavour Ingredients, 1975, CRC Press; Synthetic Food Adjuncts, 1947 by M. B. Jacobs, edited by Van Nostrand; or Perfume and Flavour Chemicals by S. Arctander 1969, Montclair, N.J. (USA).
  • 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.
  • top notes are 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. The International Fragrance Association has published a list of fragrance ingredients (perfumes) in 2011. (http://www.ifraorq.Org/en-us/inqredients#.U7Z4hPldWzk)
  • Perfume top note may be used to cue the whiteness and brightness benefit of the invention.
  • perfume may be encapsulated, typical perfume components which it is advantageous to encapsulate, include those with a relatively low boiling point, preferably those with a boiling point of less than 300, preferably 100-250 Celsius. It is also
  • perfume ingredients which have a low CLog P (ie. those which will have a greater tendency to be partitioned into water), preferably with a CLog P of less than 3.0.
  • These materials, of relatively low boiling point and relatively low CLog P have been called the "delayed blooming" perfume ingredients and include one or more of the following materials: allyl caproate, amyl acetate, amyl propionate, anisic aldehyde, anisole, benzaldehyde, benzyl acetate, benzyl acetone, benzyl alcohol, benzyl formate, benzyl iso valerate, benzyl propionate, beta gamma hexenol, camphor gum, laevo-carvone, d- carvone, cinnamic alcohol, cinamyl formate, cis-jasmone, cis-3-hexenyl acetate,
  • 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 from the list given of delayed blooming perfumes given above present in the perfume.
  • perfumes with which the present invention can be applied are the so-called aromatherapy' materials. These include many components also used in perfumery, including components of essential oils such as Clary Sage, Eucalyptus, Geranium,
  • the laundry treatment composition does not contain a peroxygen bleach, e.g., sodium percarbonate, sodium perborate, and peracid.
  • a peroxygen bleach e.g., sodium percarbonate, sodium perborate, and peracid.
  • the composition is a laundry detergent composition
  • it comprises a shading dye.
  • the shading dye is present at from 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, Zurich, 2003) and, Industrial Dyes Chemistry, Properties Applications. (K Hunger (ed), Wiley-VCH Weinheim 2003).
  • Shading Dyes for use in laundry compositions preferably have an extinction coefficient at the maximum absorption in the visible range (400 to 700nm) of greater than
  • the dyes are blue or violet in colour.
  • Preferred shading dye chromophores are azo, azine, anthraquinone, and triphenylmethane.
  • Azo, anthraquinone, phthalocyanine and triphenylmethane dyes preferably carry a net anionic charged or are uncharged.
  • Azine preferably carry a net anionic or cationic charge.
  • Blue or violet shading dyes deposit to fabric during the wash or rinse step of the washing process providing a visible hue to the fabric.
  • the dye gives a blue or violet colour to a 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 is bleached non-mercerised woven cotton sheeting. Shading dyes are discussed in WO 2005/003274, WO 2006/032327(Unilever),
  • Mono-azo dyes preferably contain a heterocyclic ring and are most preferably thiophene dyes.
  • Bis-azo dyes are preferably sulphonated bis-azo dyes.
  • Preferred examples of sulphonated bis-azo 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 versions thereof. Alkoxylated bis-azo dyes are discussed in WO2012/054058 and W02010/151906.
  • alkoxylated bis-azo dye is :
  • Thiophene dyes are available from Milliken under the tradenames of Liquitint Violet DD and Liquitint Violet ION.
  • Azine dye are preferably selected from sulphonated phenazine dyes and cationic phenazine dyes. Preferred examples are acid blue 98, acid violet 50, dye with CAS-No 72749-80-5, acid blue 59, and the phenazine dye selected from:
  • X3 is selected from: -H; -F; -CH3; -C2H5; -OCH3; and, -OC2H5;
  • X4 is selected from: -H; -CH3; -C2H5; -OCH3; and, -OC2H5;
  • Y 2 is selected from: -OH; -OCH 2 CH 2 OH; -CH(OH)CH 2 OH; -OC(0)CH 3 ; and, C(0)OCH 3.
  • the shading dye is present is present in the composition in range from 0.0001 to
  • the shading dye is a blue or violet shading dye.
  • a mixture of shading dyes may be used.
  • the shading dye is most preferably a reactive blue anthraquinone dye covalently linked to an alkoxylated polyethyleneimine.
  • the alkoxylation is preferably selected from ethoxylation and propoxylation, most preferably propoxylation.
  • the polyethylene imine before reaction with the dye and the propoxylation has a molecular weight of 600 to 1800.
  • An example structure of a preferred reactive anthraquinone covalently attached to a propoxylated polyethylene imine is:
  • composition may comprise one or more further polymers. Examples are:
  • carboxymethylcellulose poly (ethylene glycol), poly(vinyl alcohol), polycarboxylates such as polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid
  • Chelating agents may be present or absent from the detergent compositions.
  • the chelating agent is present at a level of from 0.01 to 5 wt.%.
  • Example phosphonic acid (or salt thereof) chelating agents are: 1-Hydroxyethylidene-1 ,1- diphosphonic acid (HEDP); Diethylenetriaminepenta(methylenephosphonic acid) (DTPMP); Hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP);
  • HEDP 1-Hydroxyethylidene-1 ,1- diphosphonic acid
  • DTPMP Diethylenetriaminepenta(methylenephosphonic acid)
  • HDTMP Hexamethylenediaminetetra(methylenephosphonic acid)
  • AMP Aminotris(methylenephosphonic acid)
  • ETMP Ethylenediaminetetra(methylenephosphonic acid)
  • TTMP Tetramethylenediaminetetra(methylenephosphonic acid)
  • PBTC Phosphonobutanetricarboxylic acid
  • the DNA sequence encoding a protein with putative cholesterol esterase activity was identified in the NCBI database and synthesized with codon optimization for Escherichia coli. Cloning was performed using the aLICator LIC Cloning and Expression Kit for an C-terminal His 6 -tag (pLATE31 ) In the cloning process the N-terminal site of the protein containing transmembrane helices was as truncated for better protein solubility. E. coli XL2 blue was used as cloning strain and transformed using the heat-shock method. After plasmid isolation the plasmid was sequenced and the cloning success confirmed. £. coli BL21 (DE3) harbouring the plasmid pKJE7 for co-expression of chaperons was transformed (heat-shock) and used as an expression strain for protein production.
  • Protein production was performed in 2L Erlenmeyer flasks with 1 L LB-medium and the appropriate antibiotic for plasmid selection (Ampicillin, 100 pg/mL, Chloramphenicol 35 pg/mL).
  • the expression of the chaperons was induced by 20mg/mL L-arabinoase and the culture was cultivated for 30 min at 20°C.
  • the gene expression was induced by addition of IPTG to final 1 mM and carried out for 3h at 20 ° C and 180rpm.
  • Cells were harvested by centrifugation (4750 x g, 20 min, 4 ° C) and stored at - 80 ° C.
  • Cell lysis was performed by resuspension of the cell paste in equilibration buffer (25 mM Tris-HCI, pH 8.0. , 500 mM NaCI, 20 mM Imidazole, 10mL buffer for 1g cell wet weight) and sonication on ice to break the cells.
  • the protein purification was performed using a 1 mL HisTrap FF column using the AKTA purifier system for affinity chromatography via the poly Histidine-tag.
  • Elution of the protein was performed via a linear gradient for 30 min using buffer with increased imidazole concentration (25 mM Tris-HCI, pH 8.O., 500 mM NaCI, 500 mM Imidazole). Elution fractions were identified via absorbance (280nm) and applied to an SDS-PAGE. Fractions containing the protein of interest were pooled and dialysed overnight against 5 L of buffer without imidazole (25 mM Tris-HCI, pH 8.0, 500 mM NaCI). The dialysed protein was supplemented with 0.005% (v/v) sodium azide and 10% (v/v) glycerol for freezing and storage at -80 ° C.
  • the total amount of protein of enzyme samples was estimated by using Sigma-Aldrich (bicinchoninic acid) BCA assay kit.
  • the BCA reagent was prepared by mixing solution A [1 % ( w/v ) bicinchoninic acid in sodium salt form, 2% ( w/v ) sodium carbonate, 0.16% ( w/v ) sodium tartrate, 0.4% (w/v) sodium hydroxide, 0.95% (w/v) sodium hydrogen carbonate, pH 1 1.5] with solution B [4% (w/v) copper sulphate] at 50:1 (v/v) ratio.
  • a serial dilution of bovine serum albumin (2mg/ml_) was carried out in deionised water to create 7 points of a standard curve.
  • BCA reagent 200mI_ was added into the wells of 96-well plate, followed by sample protein dilutions (20mI_).
  • sample protein dilutions (20mI_).
  • MTP microtitre plates
  • Enzyme-containing samples (20mI_) were prepared with SDS-PAGE loading buffer and heated at 70°C for 10min before running on 4-12% NuPage Bis-Tris gels with MOPS buffer at 170V. PageRulerPlus molecular weight marker were run alongside samples for the determination of the molecular mass. Each gel was then stained using GelCode Blue Safe protein stain.
  • Sterol esterase activity was determined by a colorimetric method using 4-nitrophenyl- valerate (C5) and 4-nitrophenyl-dodecanoate (C12) as substrates.
  • 4-nitrophenyl- dodecanoate (25mg) or 4-nitrophenyl-valerate (18mg) were dissolved in 10ml_ solvent (methanol) to prepare 8mM stock solutions.
  • 10ml_ solvent methanol
  • 1 ml. of stock solution was added in 7ml_ of acidified water (pH 4.5), to give a final concentration of 1 mM.
  • Table 1 A shows the composition of human-like sebum to be used in the wash studies, and which is comparable to human sebum analysed in the literature (table 1 B).
  • Macrolex violet dye (0.4% w/w) was added to the model sebum, and then 100mI_ applied to a 10x10cm swatch of polycotton which was pre-heated to 60°C. Wicking of the stain was facilitated by leaving the stain to dry o/n at 60°C. Uniformity of staining was confirmed by colourimetric determination of SRI values across the swatch which was subsequently cut into smaller 30 mm diameter circles, enabling a fit in 6-well microtitre plates for subsequent wash trials.
  • Table 1 (A) Composition of the human-like sebum tested. Shown in comparison (B) is the composition of human sebum as proposed by Nikkari 1974, In Ro 2005, Stefaniak 2010. Model human-like sebum was designed to mimic the literature description.
  • wash studies in a 5ml_ wash volume identified that the sterol esterase shows improved performance towards removal of the human-like sebum than formulation control.
  • the SRI increase for the experimental enzyme sterol esterase show improved performance towards removal of the human-like sebum than the control samples with includes the laundry esterase benchmark (Cutinase) and the laundry lipase benchmark (Lipase Evity).
  • the 4-6 units SRI increase for the experimental enzymes shown is a clearly visualised cleaning improvement above that of the control enzyme (Cutinase) and the laundry lipase benchmark (Lipase Evity). Test was carried out in triplicate at 40°C for 1 h. Formulation applied contains 7.5% total surfactant.
  • the >4 units SRI increase for the sterol esterase enzyme of the invention is a clearly visualised cleaning improvement compared to Cutinase and Lipex Evity (table 2).
  • Table 2 Cleaning performance of sterol esterase enzymes of SEQ ID 1 (towards model human-like sebum) shown in comparison to controls of washes in either: water, or formulation plus benchmark commercial esterase (Cutinase) or formulation plus benchmark commercial laundry lipase (Lipex Evity)
  • the stain removal index (SRI) indicating wash performance was measured.
  • the ⁇ statistics relates to 95% confidence level. The test shows that the sterol esterase of SEQ ID 1 had much better performance against sebum than the commercial enzymes esterase (Cutinase) and lipase (Lipex Evity).
  • Table 3 Cleaning performance of sterol esterase enzyme of SEQ ID 1 (towards model human-like sebum) shown in comparison to controls of washes in either: water, or formulation plus benchmark commercial esterase (Cutinase) or formulation plus benchmark commercial laundry lipase (Lipex Evity)

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Wood Science & Technology (AREA)
  • Organic Chemistry (AREA)
  • Detergent Compositions (AREA)
EP19795212.0A 2018-11-20 2019-10-30 Reinigungsmittelzusammensetzung Active EP3884024B1 (de)

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PCT/EP2019/079657 WO2020104158A1 (en) 2018-11-20 2019-10-30 Detergent composition

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