WO2020104155A1 - Composition détergente - Google Patents

Composition détergente

Info

Publication number
WO2020104155A1
WO2020104155A1 PCT/EP2019/079654 EP2019079654W WO2020104155A1 WO 2020104155 A1 WO2020104155 A1 WO 2020104155A1 EP 2019079654 W EP2019079654 W EP 2019079654W WO 2020104155 A1 WO2020104155 A1 WO 2020104155A1
Authority
WO
WIPO (PCT)
Prior art keywords
detergent composition
enzyme
composition according
sebum
seq
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.)
Ceased
Application number
PCT/EP2019/079654
Other languages
English (en)
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 NV
Conopco Inc
Original Assignee
Unilever NV
Conopco Inc
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
Application filed by Unilever NV, Conopco Inc filed Critical Unilever NV
Priority to CN201980076344.1A priority Critical patent/CN113056549B/zh
Priority to EP19795210.4A priority patent/EP3884022B1/fr
Priority to BR112021009807-0A priority patent/BR112021009807A2/pt
Publication of WO2020104155A1 publication Critical patent/WO2020104155A1/fr
Priority to ZA2021/02581A priority patent/ZA202102581B/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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 isomerase 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.
  • compositions improve the sebum removal from fabrics.
  • the present invention provides a detergent composition comprising:
  • the 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% sequence identity to any one of SEQ ID NO: 1 or 2.
  • the isomerase 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 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: 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 an isomerase enzyme, wherein the isomerase enzyme is a squalene hopene cyclase enzyme, 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 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.
  • the present invention provides the use of an isomerase enzyme, wherein the isomerase enzyme is a squalene hopene cyclase enzyme, to improve cleaning of sebum stains on fabric.
  • the 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 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.
  • sequences disclosed herein are SEQ ID NO 1 or 2.
  • SEQ ID 1 is a truncated sequence derived from SEQ ID 2 and is from Methanosarcina thermophila
  • SEQ ID 2 is from Methanosarcina thermophila
  • the isomerase enzyme can be described as being of enzyme class EC 5.
  • the isomerase enzyme is a squalene hopene cyclase, which can be described as being of enzyme class EC 5.4.99.17.
  • the enzyme has at least 60% sequence identity to any one of SEQ ID NO: 1 or 2.
  • the 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 enzyme has 100% sequence identity to any one of SEQ ID NO: 1 or 2.
  • Preferred isomerases are from Methanosarcina thermophila.
  • 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 Cm to C 15 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 Cis 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 Cis primary alcohol with an average ethoxylation of 7EO to 9EO units.
  • surfactants used are saturated. Soil release polymer
  • 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. If present, then 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).
  • 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 (httpi//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.
  • 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, Fusahum, Thielavia, Acremonium, e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora
  • thermophila and Fusahum 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.
  • 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.
  • 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, cuminic alcohol, cyclal c,
  • 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.
  • Shading 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 1 1 , 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: wherein:
  • 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; -0C(0)CH 3 ; and, C(0)0CH 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.
  • 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
  • the DNA sequence encoding a protein with putative hydrolytic 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 C-terminal site of the protein harbouring
  • transmembrane helices was truncated to increase the solubility of the protein.
  • 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 (GE Healthcare) column and AKTA purifier system (GE Healthcare) 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 200pL was added into the wells of 96-well plate, followed by sample protein dilutions (20pL).
  • sample protein dilutions (20pL).
  • 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.
  • 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.
  • 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.
  • SHC Squalene Hopene Cyclase
  • the SRI increase for the experimental enzyme SHC 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 3-6 units SRI increase for the experimental enzyme 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 >3 units SRI increase for the isomerase enzyme of the invention is a clearly visualised cleaning improvement compared to Cutinase and Lipex Evity (table 2).
  • Table 2 Cleaning performance of isomerase 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)
  • the stain removal index (SRI) indicating wash performance was measured.
  • the ⁇ statistics relates to 95% confidence level.
  • the test shows that the isomerase of SEQ ID 1 had much better performance against sebum than the commercial enzymes esterase (Cutinase) and lipase (Lipex Evity). Enzymatic cleaning performance against human-like sebum
  • Table 3 Cleaning performance of isomerase 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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Abstract

L'invention concerne une composition détergente comprenant: (I) de 1 à 60 % en poids d'un tensioactif; et, (ii) de 0,0005 à 5 % en poids d'une enzyme isomérase, l'enzyme isomérase étant une enzyme squalène-hopène cyclase; un procédé utilisant l'enzyme et l'utilisation de l'enzyme pour améliorer le nettoyage des taches de sébum sur le tissu.
PCT/EP2019/079654 2018-11-20 2019-10-30 Composition détergente Ceased WO2020104155A1 (fr)

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CN201980076344.1A CN113056549B (zh) 2018-11-20 2019-10-30 洗涤剂组合物
EP19795210.4A EP3884022B1 (fr) 2018-11-20 2019-10-30 Composition de détergent
BR112021009807-0A BR112021009807A2 (pt) 2018-11-20 2019-10-30 composição detergente, método de tratamento de um substrato de tecido e uso de uma enzima isomerase
ZA2021/02581A ZA202102581B (en) 2018-11-20 2021-04-19 Detergent composition

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Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP4692293A1 (fr) * 2024-08-06 2026-02-11 Unilever IP Holdings B.V. Composition
WO2026032715A1 (fr) * 2024-08-06 2026-02-12 Unilever Ip Holdings B.V. Composition
WO2026032722A1 (fr) * 2024-08-06 2026-02-12 Unilever Ip Holdings B.V. Composition

Citations (81)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1296839A (fr) 1969-05-29 1972-11-22
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
US4435307A (en) 1980-04-30 1984-03-06 Novo Industri A/S Detergent cellulase
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
EP0260105A2 (fr) 1986-09-09 1988-03-16 Genencor, Inc. Préparation d'enzymes à activité modifiée
US4760025A (en) 1984-05-29 1988-07-26 Genencor, Inc. Modified enzymes and methods for making same
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
WO1989006270A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Detergent enzymatique
WO1989006279A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Genes de subtilisine mutes
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
WO1989009259A1 (fr) 1988-03-24 1989-10-05 Novo-Nordisk A/S Preparation de cellulase
EP0407225A1 (fr) 1989-07-07 1991-01-09 Unilever Plc Enzymes et compositions détergentes enzymatiques
WO1991016422A1 (fr) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Lipases bacillaires alcalines, sequences d'adn de codage pour celles-ci et bacilles produisant ces lipases
WO1992005249A1 (fr) 1990-09-13 1992-04-02 Novo Nordisk A/S Variantes lipasiques
WO1992017517A1 (fr) 1991-04-02 1992-10-15 Minnesota Mining And Manufacturing Company Condensats d'uree-aldehyde et derives de melamine comprenant des oligomeres fluorochimiques
WO1992019709A1 (fr) 1991-04-30 1992-11-12 The Procter & Gamble Company Detergents liquides contenant un adjuvant et un complexe polyol acide borique qui sert a inhiber l'enzyme proteolytique
WO1992019708A1 (fr) 1991-04-30 1992-11-12 The Procter & Gamble Company Detergents liquides comprenant un ester de borate aromatique servant a inhiber l'enzyme proteolytique
WO1993018140A1 (fr) 1992-03-04 1993-09-16 Novo Nordisk A/S Nouvelles proteases
WO1993024618A1 (fr) 1992-06-01 1993-12-09 Novo Nordisk A/S Variante de peroxydase avec stabilite amelioree vis-a-vis du peroxyde d'hydrogene
WO1994001541A1 (fr) 1992-07-06 1994-01-20 Novo Nordisk A/S Lipase de c. antarctica et variantes lipasiques
WO1994025583A1 (fr) 1993-05-05 1994-11-10 Novo Nordisk A/S Protease recombinee de type trypsine
WO1994025578A1 (fr) 1993-04-27 1994-11-10 Gist-Brocades N.V. Nouveaux variants de lipase utilises dans des detergents
WO1995006720A1 (fr) 1993-08-30 1995-03-09 Showa Denko K.K. Nouvelle lipase, micro-organisme la produisant, procede de production de cette lipase, et utilisation de ladite lipase
WO1995010602A1 (fr) 1993-10-13 1995-04-20 Novo Nordisk A/S Variants de peroxydase stables par rapport a h2o¿2?
WO1995014783A1 (fr) 1993-11-24 1995-06-01 Showa Denko K.K. Gene de lipase et lipase variante
WO1995022615A1 (fr) 1994-02-22 1995-08-24 Novo Nordisk A/S Procede pour preparer un variant d'une enzyme lipolytique
WO1995026397A1 (fr) 1994-03-29 1995-10-05 Novo Nordisk A/S Amylase alcaline issue d'un bacille
WO1995030744A2 (fr) 1994-05-04 1995-11-16 Genencor International Inc. Lipases a resistance aux tensioactifs amelioree
WO1995035381A1 (fr) 1994-06-20 1995-12-28 Unilever N.V. Lipases modifiees provenant de pseudomonas et leur utilisation
WO1996000292A1 (fr) 1994-06-23 1996-01-04 Unilever N.V. Pseudomonas lipases modifiees et leur utilisation
WO1996012012A1 (fr) 1994-10-14 1996-04-25 Solvay S.A. Lipase, micro-organisme la produisant, procede de preparation de cette lipase et utilisation de celle-ci
WO1996013580A1 (fr) 1994-10-26 1996-05-09 Novo Nordisk A/S Enzyme a activite lipolytique
WO1996027002A1 (fr) 1995-02-27 1996-09-06 Novo Nordisk A/S Nouveau gene de lipase et procede de production de lipase a l'aide de celui-ci
WO1996029397A1 (fr) 1995-03-17 1996-09-26 Novo Nordisk A/S Nouvelles endoglucanases
WO1997004079A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Enzyme modifiee a activite lipolytique
WO1997007202A1 (fr) 1995-08-11 1997-02-27 Novo Nordisk A/S Nouvelles enzymes lipolytiques
US5648263A (en) 1988-03-24 1997-07-15 Novo Nordisk A/S Methods for reducing the harshness of a cotton-containing fabric
US5679630A (en) 1993-10-14 1997-10-21 The Procter & Gamble Company Protease-containing cleaning compositions
WO1998012307A1 (fr) 1996-09-17 1998-03-26 Novo Nordisk A/S Variants de cellulase
WO1998015257A1 (fr) 1996-10-08 1998-04-16 Novo Nordisk A/S Derives de l'acide diaminobenzoique en tant que precurseurs de matieres tinctoriales
WO2000060060A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides presentant une activite alcaline alpha-amylase et acides nucleiques les codant
WO2000060063A1 (fr) 1999-03-31 2000-10-12 Novozymes A/S Variante genetique de lipase
WO2001016285A2 (fr) 1999-08-31 2001-03-08 Novozymes A/S Nouvelles proteases et leurs variants
US6265371B1 (en) * 1997-07-18 2001-07-24 Kao Corporation Powdery detergent composition containing a partially neutralized chelant
US6312936B1 (en) 1997-10-23 2001-11-06 Genencor International, Inc. Multiply-substituted protease variants
WO2002016547A2 (fr) 2000-08-21 2002-02-28 Novozymes A/S Enzymes subtilases
WO2002026024A1 (fr) 2000-08-05 2002-04-04 Haiquan Li Appareil utilisant des ressources recyclables
WO2005003274A1 (fr) 2003-06-18 2005-01-13 Unilever Plc Compositions pour le traitement du linge
WO2005040372A1 (fr) 2003-10-23 2005-05-06 Novozymes A/S Protease a stabilite amelioree dans les detergents
WO2005052146A2 (fr) 2003-11-19 2005-06-09 Genencor International, Inc. Serine proteases, acides nucleiques codants pour les enzymes a serine et vecteurs et cellules hotes les contenant
WO2006027086A1 (fr) 2004-09-11 2006-03-16 Unilever Plc Compositions de traitement de linge
WO2006032397A1 (fr) 2004-09-23 2006-03-30 Unilever Plc Compositions detergentes
WO2006032327A1 (fr) 2004-09-23 2006-03-30 Unilever Plc Compositions de traitement pour la blanchisserie
WO2006045275A2 (fr) 2004-10-25 2006-05-04 Müller Weingarten AG Systeme d'entrainement d'une presse de formage
US7262042B2 (en) 2001-12-20 2007-08-28 Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) Alkaline protease from Bacillus gibsonii (DSM 14393) and washing and cleaning products comprising said alkaline protease
WO2008017570A1 (fr) 2006-08-10 2008-02-14 Unilever Plc Composition de coloration légère
WO2008087497A1 (fr) 2007-01-19 2008-07-24 The Procter & Gamble Company Composition de lessive munis d'un agent de blanchiment pour substrats cellulosiques
WO2008141880A1 (fr) 2007-05-18 2008-11-27 Unilever Plc Colorants à la triphénodioxazine
WO2009021867A2 (fr) 2007-08-10 2009-02-19 Henkel Ag & Co. Kgaa Agents contenant des protéases
WO2009087524A1 (fr) 2008-01-04 2009-07-16 The Procter & Gamble Company Compositions contenant une enzyme et un agent de nuançage des tissus
WO2009090576A2 (fr) 2008-01-11 2009-07-23 Procter & Gamble International Operations Sa Compositions de nettoyage et/ou de traitement
WO2009107091A2 (fr) 2008-02-29 2009-09-03 The Procter & Gamble Company Composition de détergent contenant une lipase
WO2009111258A2 (fr) 2008-02-29 2009-09-11 The Procter & Gamble Company Composition détergente comprenant une lipase
WO2009132870A1 (fr) 2008-05-02 2009-11-05 Unilever Plc Granulés à tachage réduit
WO2009141173A1 (fr) 2008-05-20 2009-11-26 Unilever Plc Composition de nuançage
WO2009148983A1 (fr) 2008-06-06 2009-12-10 The Procter & Gamble Company Composition détergente comprenant un variant de xyloglucanase de la famille 44
WO2010099997A1 (fr) 2009-03-05 2010-09-10 Unilever Plc Initiateurs radicalaires colorants
WO2010102861A1 (fr) 2009-03-12 2010-09-16 Unilever Plc Formulations de polymères colorants
WO2010151906A2 (fr) 2010-10-22 2010-12-29 Milliken & Company Colorants diazo utilisés comme produits d’azurage
WO2010148624A1 (fr) 2009-06-26 2010-12-29 Unilever Plc Polymères colorants
WO2011011799A2 (fr) 2010-11-12 2011-01-27 The Procter & Gamble Company Colorants azoïques thiophéniques et compositions de lessive les contenant
WO2012054820A1 (fr) 2010-10-22 2012-04-26 The Procter & Gamble Company Composition de détergent contenant un agent azurant et un agent de blanchiment fluorescent rapidement hydrosoluble
WO2012054058A1 (fr) 2010-10-22 2012-04-26 The Procter & Gamble Company Colorants bis-azoïques destinés à être utilisés à titre d'agents de bleuissement
WO2013142495A1 (fr) 2012-03-19 2013-09-26 Milliken & Company Colorants carboxilate
WO2013151970A1 (fr) 2012-04-03 2013-10-10 The Procter & Gamble Company Composition détergente pour la lessive comprenant un composé de phtalocyanine soluble dans l'eau
WO2014029479A1 (fr) 2012-08-18 2014-02-27 Clariant International Ltd Utilisation de polyesters dans des produits de lavage et de nettoyage
WO2014090940A1 (fr) * 2012-12-14 2014-06-19 Novozymes A/S Élimination de souillures issues de la peau
WO2016005338A1 (fr) 2014-07-09 2016-01-14 Clariant International Ltd Compositions stables au stockage contenant des polymères détachants
EP3243897A1 (fr) * 2016-05-09 2017-11-15 The Procter & Gamble Company Composition de détergent comprenant une enzyme qui transforme les acides gras

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB201507207D0 (en) * 2015-04-24 2015-06-10 Givaudan Sa Enzymes and applications thereof

Patent Citations (84)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1296839A (fr) 1969-05-29 1972-11-22
GB1372034A (en) 1970-12-31 1974-10-30 Unilever Ltd Detergent compositions
US4435307A (en) 1980-04-30 1984-03-06 Novo Industri A/S Detergent cellulase
US4760025A (en) 1984-05-29 1988-07-26 Genencor, Inc. Modified enzymes and methods for making same
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
EP0260105A2 (fr) 1986-09-09 1988-03-16 Genencor, Inc. Préparation d'enzymes à activité modifiée
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
JPS6474992A (en) 1987-09-16 1989-03-20 Fuji Oil Co Ltd Dna sequence, plasmid and production of lipase
WO1989006279A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Genes de subtilisine mutes
WO1989006270A1 (fr) 1988-01-07 1989-07-13 Novo-Nordisk A/S Detergent enzymatique
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
US5691178A (en) 1988-03-22 1997-11-25 Novo Nordisk A/S Fungal cellulase composition containing alkaline CMC-endoglucanase and essentially no cellobiohydrolase
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
WO1989009259A1 (fr) 1988-03-24 1989-10-05 Novo-Nordisk A/S Preparation de cellulase
US5648263A (en) 1988-03-24 1997-07-15 Novo Nordisk A/S Methods for reducing the harshness of a cotton-containing fabric
EP0407225A1 (fr) 1989-07-07 1991-01-09 Unilever Plc Enzymes et compositions détergentes enzymatiques
WO1991016422A1 (fr) 1990-04-14 1991-10-31 Kali-Chemie Aktiengesellschaft Lipases bacillaires alcalines, sequences d'adn de codage pour celles-ci et bacilles produisant ces lipases
WO1992005249A1 (fr) 1990-09-13 1992-04-02 Novo Nordisk A/S Variantes lipasiques
WO1992017517A1 (fr) 1991-04-02 1992-10-15 Minnesota Mining And Manufacturing Company Condensats d'uree-aldehyde et derives de melamine comprenant des oligomeres fluorochimiques
WO1992019708A1 (fr) 1991-04-30 1992-11-12 The Procter & Gamble Company Detergents liquides comprenant un ester de borate aromatique servant a inhiber l'enzyme proteolytique
WO1992019709A1 (fr) 1991-04-30 1992-11-12 The Procter & Gamble Company Detergents liquides contenant un adjuvant et un complexe polyol acide borique qui sert a inhiber l'enzyme proteolytique
WO1993018140A1 (fr) 1992-03-04 1993-09-16 Novo Nordisk A/S Nouvelles proteases
WO1993024618A1 (fr) 1992-06-01 1993-12-09 Novo Nordisk A/S Variante de peroxydase avec stabilite amelioree vis-a-vis du peroxyde d'hydrogene
WO1994001541A1 (fr) 1992-07-06 1994-01-20 Novo Nordisk A/S Lipase de c. antarctica et variantes lipasiques
WO1994025578A1 (fr) 1993-04-27 1994-11-10 Gist-Brocades N.V. Nouveaux variants de lipase utilises dans des detergents
WO1994025583A1 (fr) 1993-05-05 1994-11-10 Novo Nordisk A/S Protease recombinee de type trypsine
WO1995006720A1 (fr) 1993-08-30 1995-03-09 Showa Denko K.K. Nouvelle lipase, micro-organisme la produisant, procede de production de cette lipase, et utilisation de ladite lipase
WO1995010602A1 (fr) 1993-10-13 1995-04-20 Novo Nordisk A/S Variants de peroxydase stables par rapport a h2o¿2?
US5679630A (en) 1993-10-14 1997-10-21 The Procter & Gamble Company Protease-containing cleaning compositions
WO1995014783A1 (fr) 1993-11-24 1995-06-01 Showa Denko K.K. Gene de lipase et lipase variante
WO1995022615A1 (fr) 1994-02-22 1995-08-24 Novo Nordisk A/S Procede pour preparer un variant d'une enzyme lipolytique
WO1995026397A1 (fr) 1994-03-29 1995-10-05 Novo Nordisk A/S Amylase alcaline issue d'un bacille
WO1995030744A2 (fr) 1994-05-04 1995-11-16 Genencor International Inc. Lipases a resistance aux tensioactifs amelioree
WO1995035381A1 (fr) 1994-06-20 1995-12-28 Unilever N.V. Lipases modifiees provenant de pseudomonas et leur utilisation
WO1996000292A1 (fr) 1994-06-23 1996-01-04 Unilever N.V. Pseudomonas lipases modifiees et leur utilisation
WO1996012012A1 (fr) 1994-10-14 1996-04-25 Solvay S.A. Lipase, micro-organisme la produisant, procede de preparation de cette lipase et utilisation de celle-ci
WO1996013580A1 (fr) 1994-10-26 1996-05-09 Novo Nordisk A/S Enzyme a activite lipolytique
WO1996027002A1 (fr) 1995-02-27 1996-09-06 Novo Nordisk A/S Nouveau gene de lipase et procede de production de lipase a l'aide de celui-ci
WO1996029397A1 (fr) 1995-03-17 1996-09-26 Novo Nordisk A/S Nouvelles endoglucanases
WO1997004079A1 (fr) 1995-07-14 1997-02-06 Novo Nordisk A/S Enzyme modifiee a activite lipolytique
WO1997007202A1 (fr) 1995-08-11 1997-02-27 Novo Nordisk A/S Nouvelles enzymes lipolytiques
WO1998012307A1 (fr) 1996-09-17 1998-03-26 Novo Nordisk A/S Variants de cellulase
WO1998015257A1 (fr) 1996-10-08 1998-04-16 Novo Nordisk A/S Derives de l'acide diaminobenzoique en tant que precurseurs de matieres tinctoriales
US6265371B1 (en) * 1997-07-18 2001-07-24 Kao Corporation Powdery detergent composition containing a partially neutralized chelant
US6312936B1 (en) 1997-10-23 2001-11-06 Genencor International, Inc. Multiply-substituted protease variants
WO2000060060A2 (fr) 1999-03-31 2000-10-12 Novozymes A/S Polypeptides presentant une activite alcaline alpha-amylase et acides nucleiques les codant
WO2000060063A1 (fr) 1999-03-31 2000-10-12 Novozymes A/S Variante genetique de lipase
WO2001016285A2 (fr) 1999-08-31 2001-03-08 Novozymes A/S Nouvelles proteases et leurs variants
WO2002026024A1 (fr) 2000-08-05 2002-04-04 Haiquan Li Appareil utilisant des ressources recyclables
WO2002016547A2 (fr) 2000-08-21 2002-02-28 Novozymes A/S Enzymes subtilases
US7262042B2 (en) 2001-12-20 2007-08-28 Henkel Kommanditgesellschaft Auf Aktien (Henkel Kgaa) Alkaline protease from Bacillus gibsonii (DSM 14393) and washing and cleaning products comprising said alkaline protease
WO2005003274A1 (fr) 2003-06-18 2005-01-13 Unilever Plc Compositions pour le traitement du linge
WO2005040372A1 (fr) 2003-10-23 2005-05-06 Novozymes A/S Protease a stabilite amelioree dans les detergents
WO2005052146A2 (fr) 2003-11-19 2005-06-09 Genencor International, Inc. Serine proteases, acides nucleiques codants pour les enzymes a serine et vecteurs et cellules hotes les contenant
WO2005052161A2 (fr) 2003-11-19 2005-06-09 Genencor International, Inc. Serine proteases, acides nucleiques codant des enzymes de serine et vecteurs et cellules hotes les integrant
WO2006027086A1 (fr) 2004-09-11 2006-03-16 Unilever Plc Compositions de traitement de linge
WO2006032397A1 (fr) 2004-09-23 2006-03-30 Unilever Plc Compositions detergentes
WO2006032327A1 (fr) 2004-09-23 2006-03-30 Unilever Plc Compositions de traitement pour la blanchisserie
WO2006045275A2 (fr) 2004-10-25 2006-05-04 Müller Weingarten AG Systeme d'entrainement d'une presse de formage
WO2008017570A1 (fr) 2006-08-10 2008-02-14 Unilever Plc Composition de coloration légère
WO2008087497A1 (fr) 2007-01-19 2008-07-24 The Procter & Gamble Company Composition de lessive munis d'un agent de blanchiment pour substrats cellulosiques
WO2008141880A1 (fr) 2007-05-18 2008-11-27 Unilever Plc Colorants à la triphénodioxazine
WO2009021867A2 (fr) 2007-08-10 2009-02-19 Henkel Ag & Co. Kgaa Agents contenant des protéases
WO2009087524A1 (fr) 2008-01-04 2009-07-16 The Procter & Gamble Company Compositions contenant une enzyme et un agent de nuançage des tissus
WO2009090576A2 (fr) 2008-01-11 2009-07-23 Procter & Gamble International Operations Sa Compositions de nettoyage et/ou de traitement
WO2009107091A2 (fr) 2008-02-29 2009-09-03 The Procter & Gamble Company Composition de détergent contenant une lipase
WO2009111258A2 (fr) 2008-02-29 2009-09-11 The Procter & Gamble Company Composition détergente comprenant une lipase
WO2009132870A1 (fr) 2008-05-02 2009-11-05 Unilever Plc Granulés à tachage réduit
WO2009141173A1 (fr) 2008-05-20 2009-11-26 Unilever Plc Composition de nuançage
WO2009148983A1 (fr) 2008-06-06 2009-12-10 The Procter & Gamble Company Composition détergente comprenant un variant de xyloglucanase de la famille 44
WO2010099997A1 (fr) 2009-03-05 2010-09-10 Unilever Plc Initiateurs radicalaires colorants
WO2010102861A1 (fr) 2009-03-12 2010-09-16 Unilever Plc Formulations de polymères colorants
WO2010148624A1 (fr) 2009-06-26 2010-12-29 Unilever Plc Polymères colorants
WO2010151906A2 (fr) 2010-10-22 2010-12-29 Milliken & Company Colorants diazo utilisés comme produits d’azurage
WO2012054820A1 (fr) 2010-10-22 2012-04-26 The Procter & Gamble Company Composition de détergent contenant un agent azurant et un agent de blanchiment fluorescent rapidement hydrosoluble
WO2012054058A1 (fr) 2010-10-22 2012-04-26 The Procter & Gamble Company Colorants bis-azoïques destinés à être utilisés à titre d'agents de bleuissement
WO2011011799A2 (fr) 2010-11-12 2011-01-27 The Procter & Gamble Company Colorants azoïques thiophéniques et compositions de lessive les contenant
WO2013142495A1 (fr) 2012-03-19 2013-09-26 Milliken & Company Colorants carboxilate
WO2013151970A1 (fr) 2012-04-03 2013-10-10 The Procter & Gamble Company Composition détergente pour la lessive comprenant un composé de phtalocyanine soluble dans l'eau
WO2014029479A1 (fr) 2012-08-18 2014-02-27 Clariant International Ltd Utilisation de polyesters dans des produits de lavage et de nettoyage
WO2014090940A1 (fr) * 2012-12-14 2014-06-19 Novozymes A/S Élimination de souillures issues de la peau
WO2016005338A1 (fr) 2014-07-09 2016-01-14 Clariant International Ltd Compositions stables au stockage contenant des polymères détachants
EP3243897A1 (fr) * 2016-05-09 2017-11-15 The Procter & Gamble Company Composition de détergent comprenant une enzyme qui transforme les acides gras

Non-Patent Citations (13)

* Cited by examiner, † Cited by third party
Title
"Chemicals Buyers Directory", 1993, SCHNELL PUBLISHING CO
"Fenaroli's Handbook of Flavour Ingredients", 1975, CRC PRESS
"International Buyers Guide", 1992, CFTA PUBLICATIONS
ANONYMOUS: "Hit details for UNIPARC:UPI000615F68D", 9 April 2015 (2015-04-09), XP055579824, Retrieved from the Internet <URL:http://ibis.internal.epo.org/exam/hitDetails.jsp?id=213316935> [retrieved on 20190410] *
ANONYMOUS: "Hit details for UNIPARC:UPI000615F68D", 9 April 2015 (2015-04-09), XP055579888, Retrieved from the Internet <URL:http://ibis.internal.epo.org/exam/hitDetails.jsp?id=213324935> [retrieved on 20190410] *
CHEMICAL ABSTRACTS, Columbus, Ohio, US; abstract no. 72749-80-5
DARTOIS ET AL., BIOCHEMICA ET BIOPHYSICA ACTA, vol. 1131, 1993, pages 253 - 360
H ZOLLINGER: "Color Chemistry Synthesis, Properties and Applications of Organic Dyes and Pigments", 2003, WILEY-VCH
M. B. JACOBS: "Synthetic Food Adjuncts", 1947
POUCHER, JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS, vol. 6, no. 2, 1955, pages 80
S. ARCTANDER, PERFUME AND FLAVOUR CHEMICALS, 1969
SIEZEN ET AL., PROTEIN ENGNG., vol. 4, 1991, pages 719 - 737
SIEZEN ET AL., PROTEIN SCIENCE, vol. 6, 1997, pages 501 - 523

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP4692293A1 (fr) * 2024-08-06 2026-02-11 Unilever IP Holdings B.V. Composition
WO2026032715A1 (fr) * 2024-08-06 2026-02-12 Unilever Ip Holdings B.V. Composition
WO2026032722A1 (fr) * 2024-08-06 2026-02-12 Unilever Ip Holdings B.V. Composition

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