WO2020058024A1 - Composition détergente - Google Patents

Composition détergente Download PDF

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Publication number
WO2020058024A1
WO2020058024A1 PCT/EP2019/074006 EP2019074006W WO2020058024A1 WO 2020058024 A1 WO2020058024 A1 WO 2020058024A1 EP 2019074006 W EP2019074006 W EP 2019074006W WO 2020058024 A1 WO2020058024 A1 WO 2020058024A1
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WO
WIPO (PCT)
Prior art keywords
detergent composition
soil release
release polymer
lipase
composition according
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP2019/074006
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English (en)
Inventor
Dietmar Andreas LANG
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 BR112021004507-4A priority Critical patent/BR112021004507A2/pt
Priority to EP19765252.2A priority patent/EP3853330B1/fr
Priority to CN201980060687.9A priority patent/CN112703246A/zh
Publication of WO2020058024A1 publication Critical patent/WO2020058024A1/fr
Priority to ZA2021/01254A priority patent/ZA202101254B/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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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
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/0005—Other compounding ingredients characterised by their effect
    • C11D3/0036—Soil deposition preventing compositions; Antiredeposition agents
    • 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
    • C11D3/37—Polymers
    • C11D3/3703—Macromolecular compounds obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds
    • C11D3/3715—Polyesters or polycarbonates

Definitions

  • the invention concerns a detergent composition, in particular a detergent composition comprising a soil release polymer
  • Soil release polymers are a useful ingredient for detergent formulations, particularly for laundry detergents. Another ingredient that is useful is the incorporation of enzymes, particularly lipase enzymes. However, inclusion of lipase enzymes causes degradation of the soil release polymer. So the formulator has to forgo one of these useful ingredients.
  • lipases A problem with inclusion of lipases is that they cannot be included in a detergent formulation with soil release polymers.
  • compositions doesn’t cause degradation of the soil release polymer.
  • the non- fungal lipases still provide effective cleaning.
  • the present invention provides a detergent composition comprising:
  • 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, preferably a polypropylene terephthalate based soil release polymer.
  • non-fungal lipase enzyme is a bacterial lipase enzyme.
  • Preferred bacterial lipases are derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingrahamii. Most preferred bacterial lipases are derived from Burkholderia cepacia, or Psychromonas ingrahamii.
  • a preferred detergent composition is a laundry detergent composition.
  • the laundry detergent composition is a liquid or a powder, more preferably the detergent is a liquid detergent.
  • the laundry detergent composition comprises anionic and/or nonionic surfactant, more preferably the laundry detergent composition comprises both anionic and nonionic surfactant.
  • the laundry detergent preferably comprises from 0.1 to 8 wt.% of an alkoxylated polyamine.
  • 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.
  • the present invention provides a method of treatment of a substrate with a detergent composition comprising i) a lipase enzyme; and ii) a polyester soil release polymer, preferably a polyethylene and/or polypropylene terephthalate polyester soil release polymer; to provide lipolytic cleaning without degradation of said polyester soil release polymer, said method comprising incorporation in a detergent composition of a bacterial lipase enzyme into a detergent composition according to the composition of the first aspect; and subsequent treatment of a substrate, preferably textiles, with said composition.
  • the present invention provides the use of a bacterial lipase enzyme, in a detergent composition comprising a polyester soil release polymer, preferably a polyethylene and/or polypropylene terephthalate polyester soil release polymer, to provide lipolytic cleaning without degradation of said polyester soil release polymer.
  • Figure 1 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL ex. Clariant)
  • Figure 2 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL ex. Clariant) and Lipex 100L (a fungal lipase ex. Novozymes)
  • Figure 3 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL ex. Clariant) and Amano lipase from Burkholderia cepacia (a bacterial lipase enzyme supplied by Sigma)
  • Figure 4 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL ex. Clariant) and PinLip lipase from Psychromonas ingrahamii, (a bacterial lipase enzyme supplied as purified enzyme by the University of Singer)
  • 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.
  • the soil release polymer is present at a level of from 0.1 to 10 wt.%.
  • the levels of 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.
  • Lipases (E.C. 3.1.1.3) are hydrolytic enzymes that are known to cleave ester bonds in lipids.
  • the lipase is of origin other than fungal, i.e. it is a non-fungal lipase enzyme.
  • non-fungal lipase enzymes can be for example mammalian, plant or bacterial origin.
  • Non-fungal lipases have been identified, but not limited to, from plants, e.g. Arabidopsis thaliana, from mammals, e.g. pancreas, hepatic, lipoprotein, from bacterial microorganism, e.g. Psychromonas, Pseudomonas, Vibrio, Burkholderia, Chromobacterium.
  • non-fungal lipase enzyme is a bacterial lipase enzyme.
  • bacterial lipases are classified in Arpigny & Jaeger (1999) and Lopez-Lopez et al consult 2014).
  • Preferred bacterial lipases are derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingrahamii.
  • Most preferred bacterial lipases are derived from Burkholderia cepacia, or Psychromonas ingrahamii.
  • a non-fungal lipase is an isolated, synthetic, or recombinant polypeptide, not encoding for a fungal lipase.
  • non-fungal, preferably bacterial lipase enzymes provide effective cleaning, the purpose of inclusion in these detergent compositions, as well as overcoming the problem of incompatibility with the soil release polymer due to degradation of the polymer.
  • the detergent composition comprises surfactant (which includes a mixture of two or more surfactants).
  • the composition comprises from 1 to 60 wt.%, preferably from 2.5 to 50 wt.%, more preferably from 4 to 40 wt.% of surfactant. Even more preferred levels of surfactant are from 6 to 40 wt.%, more preferably from 8 to 35 wt.%.
  • 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 C 20 benzene sulphonates, particularly sodium linear secondary alkyl C 10 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.
  • alkoxylated polyamine 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;
  • proteases aspargine peptide lyase; serine proteases and threonine proteases.
  • protease families are described in the MEROPS peptidase database (htp://merops.sanqer.ac.uk/). Serine proteases are preferred. Subtilase type serine proteases are more preferred.
  • the term "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
  • 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
  • Chelating agents may be present or absent from the detergent compositions.
  • the chelating agent is present at a level of from 0.01 to 5 wt.%.
  • Example phosphonic acid (or salt thereof) chelating agents are: 1-Hydroxyethylidene-1 ,1- diphosphonic acid (HEDP); Diethylenetriaminepenta(methylenephosphonic acid) (DTPMP); Hexamethylenediaminetetra(methylenephosphonic acid) (HDTMP);
  • HEDP 1-Hydroxyethylidene-1 ,1- diphosphonic acid
  • DTPMP Diethylenetriaminepenta(methylenephosphonic acid)
  • HDTMP Hexamethylenediaminetetra(methylenephosphonic acid)
  • AMP Aminotris(methylenephosphonic acid)
  • ETMP Ethylenediaminetetra(methylenephosphonic acid)
  • TTMP Tetramethylenediaminetetra(methylenephosphonic acid)
  • PBTC Phosphonobutanetricarboxylic acid
  • detergent compositions preferably laundry detergent compositions
  • materials that may be included in the detergent compositions include fluorescent agent, perfume, shading dyes and polymers.
  • 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. 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:
  • X3 is selected from: -H; -F; -CH3; -C2H5; -OCH3; and, -OC2H5;
  • X 4 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
  • Lipase activity was determined by a colorimetric method using 4-nitrophenyl-valerate (C5) and 4-nitrophenyl-dodecanoate (C12) as a 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.
  • Washed-off knitted polyester fabric was cut into 5x5cm squares.
  • Into a 250ml_ glass bottle 0.5g of stored formulation containing SRP and lipase was diluted with 200ml_ of Prenton water and the polyester fabric added before incubating at 30°C for 30min. This gave a final SRP concentration of 50ppm (in wash). The fabric was rinsed twice in Prenton water and allow to dry, before repeating the wash again using the same formulation and conditions. Controls used were formulation without SRP and also a control plus SRP without lipase.
  • One stain used for these experiments was sunflower oil containing 0.2% Macrolex Violet dye. A volume of 100mI_ per stain swatch was applied and allowed to dry and age for 5 days at r/t, before taking a‘pre-wash’ reading of stain intensity (DE * value).
  • the main wash for cleaning of the sunflower oil/macrolex dye stain was a repeat of the pre- wash conditions though using 3 squares of stained fabric plus 2 squares of woven cotton ballast. Following the wash, the fabric was rinsed twice in Prenton water and allowed to dry before taking a‘post-wash’ reading of stain intensity and calculating SRI as a measure of cleaning.
  • Washed-off knitted polyester fabric was cut into 5x5cm squares.
  • 2.5g of stored formulation containing SRP and lipase was diluted with 1 L of FH26 water and the polyester fabric added before incubating at 30°C for 30min.
  • Ballast cotton fabric was added to ensure a liquid:cloth ratio of 20:1 was maintained. This gave a final SRP concentration of 50ppm (in wash).
  • the fabric was rinsed twice in FH26 water and allow to dry, before repeating the wash again using the same formulation and conditions. Control used was formulation containing SRP but without lipase.
  • the stain used for these experiments was Dende oil. A volume of 200mI_ per polyester stain swatch was applied and allowed to dry and age for 3 days at r/t.
  • the main wash for cleaning of the Dende oil stain was a repeat of the pre-wash conditions though using 4 squares of Dende oil-stained fabric plus 3 swatches of lard stained cotton (for measure of lipase cleaning). Ballast cotton fabric was added to ensure a liquid:cloth ratio of 20:1. Following the wash, the fabric was rinsed twice in FH26 water and allowed to dry before taking a‘post-wash’ reading of stain intensity and calculating SRI as a measure of cleaning.
  • Lipex 100L a fungal lipase
  • SRP degrade Texcare UL soil release polymer
  • three different commercially available fungal lipases, plus two lipases of bacterial origin and one from plant were incubated in SRP containing laundry formulation for a period of 4 weeks, from which 1 ml. samples were extracted for testing of lipase activity and for SRP integrity.
  • the SRP was a polyester based soil release polymer, based on a polypropylene terephthalate polymer.
  • the three fungal lipases purchased from Sigma Aldrich originate from different organisms: Rhizomucor miehei (cat. no: L4277), Thermomyces lanuginosus (cat. no: L0777), Candida rugosa (cat. no: L1754).
  • Bacterial Amano lipase from Burkholderia cepacia was also purchased from Sigma (cat. no: 534641 ).
  • a second bacterial lipase used in these studies originates from Psychromonas ingrahamii, and was supplied as purified enzyme by the University of Starbucks (the enzyme used is identical to that disclosed in WO 2017/036901 ).
  • lipase from wheat germ (Purchased from Sigma Aldrich - cat. no: L3001 ) was also tested in these studies. Based on specific lipase activity as quoted by the commercial supplier or determined from prior work, lipases were incorporated into storage samples to give the same Unit/mL activity as a 0.4% w/v addition of the benchmark enzyme Lipex 100L - corresponding to a final lipase addition of 400 Units/mL. Of the six lipases tested in comparison to Lipex, only two of these were shown to retain lipase activity after 4 weeks storage in laundry formulation (containing the SRP).
  • Formulation samples from those that retained lipase activity after 4 weeks storage were tested for SRP integrity via NMR.
  • figure 2 shows how the peak intergrity is lost when Lipex 100L is included in the SRP laundry formulation. This is translated into a reduction of the polymer peak, as well as increase in peak intensity corresponding to the monomer (terephthalic acid) unit and oligomer related peaks.
  • NMR clearly shows the SRP to retain structural integrity despite a 4 week incubation period at both 37°C and 45°C (figure 3). The lipase activity measurements taken from this same sample were previously described in example 1.
  • lipase from Psychromonas ingrahamii also showed no hydrolytic activity towards the Texcare SRP, with the timecourse of NMR samples in figure 4 showing preservation of the SRP NMR peak throughout the storage period at 45°C.
  • This result shows that lipases of bacterial origin are preferable for compatibility with SRP, since the fungal Lipex 100L is particularly aggressive towards the hydrolysis of SRP, even after just 1 week incubation.
  • Table 1 shows that within the formulation controls, the presence of SRP results in a large noticeable increase in cleaning (-10 dSRI).
  • SRP formulation containing Lipex 100L the level of cleaning is reduced when compared to SRP formulation on its own. This shows that the cleaning benefit due to SRP is greater than that of Lipex 100L, and underlines the importance for preservation of the SRP within storage.
  • Cleaning benefits due to a structurally intact soil release polymer and an active bacterial lipase (Amano or PinLip) are also shown in table. The additional cleaning benefit from having the lipase present with the SRP is observed in these cases.
  • Table 1 Showing the positive effect of the bacterial lipases with the SRP
  • the formulation without SRP or lipase gave a SRI of ⁇ 85. Adding the SRP improved the SRI to ⁇ 94.
  • Addition of either of 2 bacterial enzymes did not show the negative effect on the SRP and gave a small statistical improvement over the positive control.

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  • Engineering & Computer Science (AREA)
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Abstract

La présente invention concerne une composition détergente comprenant : (i) 0,1 à 10 % en poids d'un polymère antisalissure ; et (ii) 0,0005 à 2,5 % en poids d'une enzyme lipase bactérienne, le polymère antisalissure étant un polymère antisalissure à base de polyester ; et un procédé de traitement d'un substrat par ladite composition en tant qu'utilisation d'une enzyme lipase non fongique pour obtenir un nettoyage lipolytique sans dégradation dudit polymère antisalissure à base de polyester.
PCT/EP2019/074006 2018-09-17 2019-09-09 Composition détergente Ceased WO2020058024A1 (fr)

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BR112021004507-4A BR112021004507A2 (pt) 2018-09-17 2019-09-09 composição detergente, método de tratamento de um substrato com uma composição detergente e uso de uma enzima lipase bacteriana
EP19765252.2A EP3853330B1 (fr) 2018-09-17 2019-09-09 Composition de détergent
CN201980060687.9A CN112703246A (zh) 2018-09-17 2019-09-09 洗涤剂组合物
ZA2021/01254A ZA202101254B (en) 2018-09-17 2021-02-24 Detergent composition

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ZA202101254B (en) 2022-09-28
EP3853330A1 (fr) 2021-07-28
EP3853330B1 (fr) 2023-06-07
CN112703246A (zh) 2021-04-23
BR112021004507A2 (pt) 2021-06-08

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