EP3884026A1 - Reinigungsmittelzusammensetzung - Google Patents

Reinigungsmittelzusammensetzung

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Publication number
EP3884026A1
EP3884026A1 EP19798035.2A EP19798035A EP3884026A1 EP 3884026 A1 EP3884026 A1 EP 3884026A1 EP 19798035 A EP19798035 A EP 19798035A EP 3884026 A1 EP3884026 A1 EP 3884026A1
Authority
EP
European Patent Office
Prior art keywords
detergent composition
composition according
enzyme
seq
sequence identity
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
EP19798035.2A
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English (en)
French (fr)
Other versions
EP3884026B1 (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
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Unilever Global IP Ltd
Unilever IP Holdings BV
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Publication of EP3884026A1 publication Critical patent/EP3884026A1/de
Application granted granted Critical
Publication of EP3884026B1 publication Critical patent/EP3884026B1/de
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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
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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 lipase 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 detergent composition comprising:
  • the lipase 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 SEQ ID NO: 1.
  • the lipase enzyme has 100% sequence identity to SEQ ID NO: 1.
  • 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 laundry detergent composition is a liquid or a powder, most preferably a liquid detergent.
  • 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: proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
  • a further enzyme selected from the group consisting of: 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 lipase 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% sequence identity, most preferably 100%, sequence identity to SEQ ID NO: 1 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.
  • a lipase 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% sequence identity, most preferably 100%
  • the present invention provides the use of an 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% sequence identity, most preferably 100%, sequence identity to SEQ ID NO: 1 to improve cleaning of sebum stains on fabric.
  • 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 may take any suitable form, for example liquids, solids (including powders) or gels.
  • the detergent composition can be applied to any suitable substrate.
  • Particularly preferred substrates are textiles.
  • Particularly preferred detergent compositions are laundry detergent compositions.
  • Laundry detergent compositions may take any suitable form. Preferred forms are liquid or powder, with liquid being most preferred. Sequence Information
  • sequences disclosed herein is SEQ ID NO 1.
  • SEQ ID 1 is from Vulcanisaeta moutnovskia
  • the lipase enzyme has at least 60% sequence identity to SEQ ID NO: 1.
  • the lipase 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 SEQ ID NO: 1.
  • the lipase enzyme has 100% sequence identity to SEQ ID NO: 1.
  • the lipase can be described as being of enzyme class EC 3.1.1.3, known as triacyl glycerol lipase.
  • Preferred lipases are from Vulcanisaeta moutnovskia.
  • 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: 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: proteases, cellulases, and/or alpha- amylases.
  • 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 (htp://merops.sanger.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.
  • Preferably 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 (Genencor International Inc.), and 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. Further materials
  • 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.
  • 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. In this regard 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.
  • 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.
  • An example of an 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 copolymers.
  • Chelating agents may be present or absent from the detergent compositions.
  • Example phosphonic acid (or salt thereof) chelating agents are: 1-Hydroxyethylidene-1 ,1- diphosphonic acid (HEDP); Diethylenetriaminepenta(methylenephosphonic acid) (DTPMP); Hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP);
  • AMP Aminotris(methylenephosphonic acid)
  • ETMP Ethylenediaminetetra(methylenephosphonic acid)
  • TTMP Tetramethylenediaminetetra(methylenephosphonic acid)
  • PBTC Phosphonobutanetricarboxylic acid
  • Lipase - type hydrolase (Vulcanisaeta moutnovskia)
  • the DNA sequence encoding a protein with putative hydrolytic activity was identified in the genome of Vulcanisaeta moutnovskia genome synthesized by GeneArt with codon optimization for Escherichia coli. Cloning was performed using the aLICator LIC Cloning and Expression Kit for an N-terminal His 6 -tag (pLATE51 ). 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. E. coli BL21 (DE3) was transformed (heat-shock) and used as an expression strain for protein production. alpha/beta hydrolase [Vulcanisaeta moutnovskia]
  • Protein production was performed in 2L Erlenmeyer flasks with 1 L LB-medium and the appropriate antibiotic for plasmid selection (Ampicillin, 100 pg/mL).
  • the gene expression was induced by addition of IPTG to final 1 mM and carried out for 3h at 37 ° 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. , 250 mM NaCI, 20 mM Imidazole, 0.1 % Triton X-100, 5% Glycerol, 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 an 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 8.0.
  • 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
  • Lipase-containing protein samples (20pL) 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 Scientific) following the manufacturers protocol.
  • Lipase 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.
  • 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 100pL 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.
  • Pre-wash readings were taken for the 30 mm diameter sebum stains to measure stain intensity. Wash studies were conducted either in a 5 mL volume (within a 6 well plate, at 40 °C for 1 hour at 100 rpm) or in 10OmL (within glass bottles, at 40 °C for 1 hour at 100 rpm). Enzymes were present at 25 mg/L within 2 g/L of a 7.5% surfactancy formulation. The stains were then rinsed three times post wash to completely remove the wash liquor and any residual enzyme. After drying, the stain plates were digitally scanned and their deltaE measured. This value is used to express cleaning effect and is defined as the colour difference between a white cloth and that of the stained cloth after being washed.
  • the >5 units SRI increase for the lipase enzyme of the invention is a clearly visualised cleaning improvement compared to Lipex Evity (table 2).
  • Table 2 Cleaning performance of lipase 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 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 lipase of SEQ ID 1 had much better performance against sebum than the commercial enzyme (Lipex Evity).
  • Lipex Evity has approx. 21% sequence identity with SEQ ID NO:1.
  • Table 3 Cleaning performance of lipase 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 laundry lipase (Lipex Evity)

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  • Engineering & Computer Science (AREA)
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  • Detergent Compositions (AREA)
EP19798035.2A 2018-11-20 2019-10-30 Reinigungsmittelzusammensetzung Active EP3884026B1 (de)

Applications Claiming Priority (2)

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EP18207278 2018-11-20
PCT/EP2019/079658 WO2020104159A1 (en) 2018-11-20 2019-10-30 Detergent composition

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Family Cites Families (56)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1296839A (de) 1969-05-29 1972-11-22
DK187280A (da) 1980-04-30 1981-10-31 Novo Industri As Ruhedsreducerende middel til et fuldvaskemiddel fuldvaskemiddel og fuldvaskemetode
US4760025A (en) 1984-05-29 1988-07-26 Genencor, Inc. Modified enzymes and methods for making same
DK6488D0 (da) 1988-01-07 1988-01-07 Novo Industri As Enzymer
EP0471265B1 (de) 1988-01-07 1995-10-25 Novo Nordisk A/S Spezifische Protease
DE68911131T2 (de) 1988-03-24 1994-03-31 Novonordisk As Cellulosezubereitung.
US5776757A (en) 1988-03-24 1998-07-07 Novo Nordisk A/S Fungal cellulase composition containing alkaline CMC-endoglucanase and essentially no cellobiohydrolase and method of making thereof
EP0550631B1 (de) 1990-09-25 1997-01-02 Rhone-Poulenc Rorer International (Holdings) Inc. Verbindungen welche antihypertensive und antiischemische eigenschaften besitzen
EP0583420B1 (de) 1991-04-30 1996-03-27 The Procter & Gamble Company Gerüstsubstanzhaltige flüssigwaschmittel mit borsäure-polyolkomplex zur ptoteolytischen enzyminhibierung
EP0511456A1 (de) 1991-04-30 1992-11-04 The Procter & Gamble Company Flüssiges Reinigungsmittel mit einem aromatischen Boratester zur Inhibierung des proteolytischen Enzyms
DK28792D0 (da) 1992-03-04 1992-03-04 Novo Nordisk As Nyt enzym
DK72992D0 (da) 1992-06-01 1992-06-01 Novo Nordisk As Enzym
DK52393D0 (de) 1993-05-05 1993-05-05 Novo Nordisk As
CN1133062A (zh) 1993-10-13 1996-10-09 诺沃挪第克公司 对过氧化氢稳定的过氧化物酶变体
CA2173105C (en) 1993-10-14 2003-05-27 Andre Baeck Protease-containing cleaning compositions
BR9507229A (pt) 1994-03-29 1997-09-16 Novo Nordisk As Amilase composição detergente aditivo detergente uso de um detergente e de uma amilase construç~o de dna vetor de expressão recombinante célula e processo para produzir amilase
JPH08176590A (ja) * 1994-12-22 1996-07-09 Kao Corp 粉末洗浄剤組成物
CN101173263A (zh) 1995-03-17 2008-05-07 诺沃奇梅兹有限公司 新的内切葡聚糖酶
EP1726644A1 (de) 1996-09-17 2006-11-29 Novozymes A/S Zellulase Varianten
CA2265734A1 (en) 1996-10-08 1998-04-16 Novo Nordisk A/S Diaminobenzoic acid derivatives as dye precursors
AR015977A1 (es) 1997-10-23 2001-05-30 Genencor Int Variantes de proteasa multiplemente substituida con carga neta alterada para su empleo en detergentes
EP2889375B1 (de) 1999-03-31 2019-03-20 Novozymes A/S Polypeptide mit alkalischer Alpha-Amylase-Aktivität und Nukleinsäuren zur Codierung davon
EP1214426A2 (de) 1999-08-31 2002-06-19 Novozymes A/S Neue proteasen und deren varianten
CN1337553A (zh) 2000-08-05 2002-02-27 李海泉 地下观光游乐园
AR030462A1 (es) 2000-08-21 2003-08-20 Novozymes As Novedosas enzimas subtilasas que tienen una reducida tendencia hacia su inhibicion por las sustancias presentes en los huevos
DE10162728A1 (de) 2001-12-20 2003-07-10 Henkel Kgaa Neue Alkalische Protease aus Bacillus gibsonii (DSM 14393) und Wasch-und Reinigungsmittel enthaltend diese neue Alkalische Protease
GB0314210D0 (en) 2003-06-18 2003-07-23 Unilever Plc Laundry treatment compositions
EP1678296B1 (de) 2003-10-23 2011-07-13 Novozymes A/S Protease mit verbesserter stabilität in detergentien
BRPI0416797A (pt) 2003-11-19 2007-04-17 Genencor Int serina proteases, ácidos nucléicos codificando enzimas de serina e vetores e células hospedeiras incorporando as mesmas
GB0420203D0 (en) 2004-09-11 2004-10-13 Unilever Plc Laundry treatment compositions
GB0421145D0 (en) 2004-09-23 2004-10-27 Unilever Plc Laundry treatment compositions
WO2006032397A1 (en) 2004-09-23 2006-03-30 Unilever Plc Laundry treatment compositions
DE102004052007B4 (de) 2004-10-25 2007-12-06 Müller Weingarten AG Antriebssystem einer Umformpresse
BRPI0706277B1 (pt) 2006-08-10 2016-11-01 Unilever Nv composição de tratamento para lavagem de roupa, e, método doméstico de tratamento de produto têxtil
EP2104729B1 (de) 2007-01-19 2010-11-03 The Procter & Gamble Company Wäschepflegemittel mit weisstöner für cellulosehaltige substrate
MY149525A (en) 2007-05-18 2013-09-13 Unilever Plc Triphenodioxazine dyes
DE102007038031A1 (de) 2007-08-10 2009-06-04 Henkel Ag & Co. Kgaa Mittel enthaltend Proteasen
CA2709609C (en) 2008-01-04 2013-05-28 The Procter & Gamble Company Glycosyl hydrolase enzyme and fabric hueing agent containing compositions
EP2085070A1 (de) 2008-01-11 2009-08-05 Procter & Gamble International Operations SA. Reinigungs- und/oder Behandlungszusammensetzungen
WO2009111258A2 (en) 2008-02-29 2009-09-11 The Procter & Gamble Company Detergent composition comprising lipase
US20090217463A1 (en) 2008-02-29 2009-09-03 Philip Frank Souter Detergent composition comprising lipase
WO2009132870A1 (en) 2008-05-02 2009-11-05 Unilever Plc Reduced spotting granules
WO2009141172A1 (en) 2008-05-20 2009-11-26 Unilever Plc Shading composition
CN102057030B (zh) 2008-06-06 2016-05-11 宝洁公司 包含家族44木葡聚糖酶变体的洗涤剂组合物
WO2010099997A1 (en) 2009-03-05 2010-09-10 Unilever Plc Dye radical initiators
BRPI1013881B1 (pt) 2009-03-12 2023-10-17 Unilever Ip Holdings B.V. Composição detergente, e, método doméstico de tratamento de tecido
WO2010148624A1 (en) 2009-06-26 2010-12-29 Unilever Plc Dye polymers
US20120101018A1 (en) 2010-10-22 2012-04-26 Gregory Scot Miracle Bis-azo colorants for use as bluing agents
WO2012054058A1 (en) 2010-10-22 2012-04-26 The Procter & Gamble Company Bis-azo colorants for use as bluing agents
CN103270118B (zh) 2010-10-22 2015-05-13 美利肯公司 用作上蓝剂的二偶氮着色剂
CA2817718C (en) 2010-11-12 2016-02-09 The Procter & Gamble Company Laundry care compositions comprising charged thiophene azo dyes
BR112014023153B1 (pt) 2012-03-19 2021-02-23 Milliken & Company corantes de carboxilato
WO2013151970A1 (en) 2012-04-03 2013-10-10 The Procter & Gamble Company Laundry detergent composition comprising water-soluble phthalocyanine compound
DE102012016462A1 (de) 2012-08-18 2014-02-20 Clariant International Ltd. Verwendung von Polyestern in Wasch- und Reinigungsmitteln
EP2966160A1 (de) 2014-07-09 2016-01-13 Clariant International Ltd. Lagerstabile Zusammensetzungen mit schmutzablösenden Polymeren
DE102016218443A1 (de) * 2016-09-26 2018-03-29 Henkel Ag & Co. Kgaa Neue Lipase

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ZA202102550B (en) 2023-01-25
EP3884026B1 (de) 2024-06-26
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WO2020104159A1 (en) 2020-05-28
CN113015781A (zh) 2021-06-22

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