BR112021004507A2 - detergent composition, method of treating a substrate with a detergent composition and use of a bacterial lipase enzyme - Google Patents

Abstract

DETERGENT COMPOSITION, METHOD OF TREATMENT OF A SUBSTRATE WITH A DETERGENT COMPOSITION AND USE OF A BACTERIAL LIPASE ENZYME. The present invention provides a detergent composition comprising: (i) from 0.1 to 10% by weight of a soil release polymer, and (ii) from 0.0005 to 2.5% by weight of a bacterial lipase enzyme, wherein the soil release polymer is a polyester based soil release polymer; and a method of treating a substrate with said composition and using a non-fungal lipase enzyme to provide lipolytic cleaning without degradation of said polyester soil release polymer.

Description

Invention Patent Descriptive Report DETERGENT COMPOSITION, METHOD OF TREATMENT OF A

SUBSTRATE WITH A DETERGENT COMPOSITION AND USE OF A

ENZYME LIPASE BACTERIAL Field of Invention

[0001] The present invention relates to a detergent composition, particularly a detergent composition comprising a dirt release polymer.

Background of the Invention

[0002] Dirt release polymers are useful ingredients 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 dirt release polymer. So the formulator has to forego one of these useful ingredients.

[0003] One problem with the inclusion of lipases is that they cannot be included in a detergent formulation with dirt release polymers.

[0004] This problem is particularly pronounced in laundry detergent formulations, especially liquid laundry detergent formulations.

Invention Summary

[0005] It has been found that the incorporation of non-fungal lipase enzymes in detergent compositions does not cause the degradation of the soil release polymer. On the other hand, non-fungal lipases still provide an effective cleanser.

[0006] In one aspect the present invention provides a detergent composition comprising: (i) from 0.1 to 10% by weight, preferably from 0.2 to 9% by weight, more preferably from 0.25 to 8%, further more preferably from 0.5 to 6% by weight, even more preferably from 1 to 5% by weight of a soil release polymer; and, (ii) from 0.0005 to 2.5% by weight, preferably from 0.005 to 2% by weight, more preferably from 0.01 to 1% by weight of a non-fungal lipase enzyme, wherein the release polymer dirt release polymer is a polyester based dirt release polymer.

[0007] Most preferably the polyester soil release polymer is a soil release polymer based on polyethylene and/or polypropylene terephthalate.

[0008] Preferably the non-fungal lipase enzyme is a bacterial lipase enzyme.

[0009] Preferred bacterial lipases are derived from Burkholderia cepacia, Pseudomonas fluorescense or Psychromonas ingrahamii. Most preferred bacterial lipases are derived from Burkholderia cepacia or Psychromonas ingrahamii.

[0010] A preferred detergent composition is a laundry detergent composition. Preferably the laundry detergent composition is a liquid or a powder, more preferably the detergent is a liquid detergent.

[0011] Preferably the laundry detergent composition comprises an anionic and/or nonionic surfactant, more preferably the laundry detergent composition comprises both anionic and nonionic surfactants.

The laundry detergent composition preferably comprises from 0.1 to 8% by weight of an alkoxylated polyamine.

Preferred detergent compositions, particularly laundry detergent compositions further comprise an additional enzyme selected from the group consisting of: proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases.

[0014] In another aspect the present invention provides a method of treating a substrate with a detergent composition comprising i) a lipase enzyme; and ii) a polyester soil release polymer, preferably a polyethylene soil release polymer and/or polypropylene terephthalate; to provide lipolytic cleaning without degradation of said polyester soil release polymer, said method comprising incorporating in a detergent composition a bacterial lipase enzyme in a detergent composition in accordance with the composition of the first aspect; and subsequently treating a substrate, preferably fabrics, with said composition.

[0015] In another aspect the present invention provides the use of a bacterial lipase enzyme, in a detergent composition comprising a polyester soil release polymer, preferably a polyethylene polyester soil release polymer and/or polypropylene terephthalate, to provide lipolytic cleaning without degradation of said polyester dirt release polymer.

Brief Description of Figures

[0016] Figure 1 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL from Clariant). As shown in Figure 1, the incubation control of the lipase-free formulation. The main peak for SRP being highlighted.

[0017] Figure 2 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL from Clariant) and Lipex 100L (a fungal lipase from Novozymes). As shown in figure 2, the formulation plus Lipex 100L (fungal lipase). The main peak for SRP being highlighted.

[0018] Figure 3 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL from Clariant) and Amano lipase from Burkholderia cepacia (a bacterial lipase enzyme supplied by Sigma). As shown in Figure 3, the Amano lipase plus formulation from Burkholderia cepacia. The main peak for SRP being highlighted.

[0019] Figure 4 shows the NMR spectrum of the detergent formulation including the soil release polymer (Texcare UL from Clariant) and PinLip lipase from Psychromonas ingrahamii (a bacterial lipase enzyme supplied as a purified enzyme by the University of Exeter). As shown in Figure 4, the PinLip plus formulation. The main peak for SRP being highlighted.

Detailed Description of the Invention

[0020] The indefinite article "a" or "an" and its corresponding definite article "the" or "the" as used herein means at least one, or one or more, unless otherwise specified.

[0021] All % levels of ingredients in compositions (formulations) listed herein are % by weight based on total formulation unless otherwise indicated.

[0022] It is understood that any reference to a preferred detergent composition ingredient is considered to be combinable matter with any other preferred detergent composition ingredient disclosed herein.

The detergent composition may take any suitable form, for example liquids, solids (including powders) or gels.

[0024] The detergent composition can be applied to any suitable substrate. Particularly preferred substrates are fabrics. Particularly preferred detergent compositions are laundry detergent compositions.

[0025] Laundry detergent compositions may take any suitable form. Preferred forms are liquid or powder, with liquid being most preferred.

dirt release polymer

[0026] The dirt release polymer is present at a level of from 0.1 to 10% by weight.

[0027] Dirt release polymer levels are preferably from 0.2 to 9% by weight, more preferably from 0.25 to 8% by weight, even more preferably from 0.5 to 6% by weight, even more preferably from 1 to 5% by weight.

[0028] Soil release polymer is a polyester based soil release polymer. More preferably the soil release polymer is a soil release polymer based on polyethylene and/or polypropylene terephthalate, more preferably a soil release polymer based on polypropylene terephthalate.

[0029] Polyester-based dirt release polymers are described in WO 2014/029479 and WO 2016/005338.

Non-fungal lipases

[0030] Lipases (E.C. 3.1.1.3) are hydrolytic enzymes that are known to cleave ester bonds in lipids.

The lipase is of other than fungal origin, i.e., it is a non-fungal lipase enzyme. Such non-fungal lipase enzymes can be, for example, of 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.

[0033] Preferably the non-fungal lipase enzyme is a bacterial lipase enzyme.

[0034] Examples of bacterial lipases are classified in Arpigny & Jaeger (1999) and Lopez-Lopez et al. (2014).

Preferred bacterial lipases are derived from Burkholderia cepacia,

Pseudomonas fluorescense or Psychromonas ingrahamii.

Most preferred bacterial lipases are derived from Burkholderia cepacia or Psychromonas ingrahamii.

[0037] A non-fungal lipase is an isolated, synthetic or recombinant polypeptide, not encoding a fungal lipase.

[0038] These 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 dirt release polymer due to polymer degradation.

surfactant

[0039] The detergent composition comprises surfactant (which includes a mixture of two or more surfactants). The composition comprises from 1 to 60% by weight, preferably from 2.5 to 50% by weight, more preferably from 4 to 40% by weight of surfactant. Even more preferred levels of surfactant are from 6 to 40% by weight, more preferably from 8 to 35% by weight.

[0040] The detergent composition (preferably a laundry detergent composition) comprises anionic and/or nonionic surfactant, preferably comprising both anionic and nonionic surfactant.

[0041] Suitable anionic detergent compounds that may be used are generally alkali metal salts of water-soluble organic sulfates and sulfonates 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.

[0042] Examples of suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulfates, especially those obtained by sulfating higher C 8 to C 18 alcohols, produced for example from tallow or coconut oil, C 9 to alkyl sulfonates sodium and potassium C 20 benzene, particularly linear secondary C 10 to C 15 alkyl benzene sulphonates of sodium; and sodium alkyl glyceryl ether sulfates, especially those ethers of higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.

[0043] The anionic surfactant is preferably selected from: linear alkyl benzene sulfonate; alkyl sulfates; alkyl ether sulfates; soaps; alkyl (preferably methyl) ester sulfonates and mixtures thereof.

[0044] The most preferred anionic surfactants are selected from: linear alkyl benzene sulfonate; alkyl sulfate; alkyl ether sulfate and mixtures thereof. Preferably the alkyl ether sulfate is an n-C 12 -C 14 alkyl ether sulfate with an average of 1 to 3 EO (ethoxylate) units.

[0045] Sodium lauryl ether sulfate (SLES) is particularly preferred. Preferably the linear alkyl benzene sulfonate is a sodium C 11 -C 15 alkyl benzene sulfonate. Preferably the alkyl sulfate is a linear or branched sodium C 12 -C 18 alkyl sulfate. Sodium dodecyl sulfate is particularly preferred (SDS, also known as primary alkyl sulfate).

[0046] In liquid formulations preferably two or more surfactants are present, for example linear alkyl benzene sulphonate together with an alkyl ether sulphate.

[0047] In liquid formulations, preferably the laundry composition, in addition to the anionic surfactant, comprises nonionic alkyl ethoxylated surfactant, preferably from 2 to 8% by weight of nonionic alkyl ethoxylated surfactant.

[0048] Suitable nonionic detergent compounds that can 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 C8 to C18 aliphatic alcohols, primary or secondary, linear or branched with ethylene oxide.

[0049] Most preferably, the nonionic detergent compound is the alkyl ethoxylated nonionic surfactant which is a C 8 to C 18 primary alcohol with ethoxylation average of 7 to 9 EO units.

[0050] Preferably, the surfactants used are saturated.

Alkoxylated polyamine

[0051] 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 are in the range from 0.1 to 8% by weight, preferably from 0.2 to 6% by weight, more preferably 0.5 to 5% by weight. Another preferred level is from 1 to 4% by weight.

[0053] The alkoxylated polyamine can be linear or branched. It can be branched to the extent that it is a dendrimer. Alkoxylation can 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.

[0054] A preferred material is alkoxylated polyethyleneimine, more preferably ethoxylated polyethyleneimine, with an average degree of ethoxylation being from 10 to 30, preferably from 15 to 25, where one nitrogen atom is ethoxylated.

additional enzymes

[0055] Additional enzymes other than the specified lipases may be present in the detergent composition. It is preferred that additional enzymes are present in the preferred laundry detergent composition.

[0056] If present, then the level of each enzyme in the laundry composition of the invention is from 0.0001% by weight to 0.1% by weight.

[0057] Levels of enzyme present in the composition preferably refer to the level of enzyme as pure protein.

Additional preferred enzymes include those in the group consisting of: proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases. Said additional preferred enzymes include a mixture of two or more of these enzymes.

Preferably the additional enzyme is selected from: proteases, cellulases and/or alpha-amylases.

[0060] Protease enzymes hydrolyze bonds within peptides and proteins, in the context of laundry, this leads to improved removal of stains containing proteins or peptides. Examples of suitable protease families include aspartic proteases; cysteine proteases; glutamic proteases; asparagine peptide lyase; serine and threonine proteases. Such protease families are described in the MEROPS peptidase database (http://merops.sanger.ac.uk/). Serine proteases are preferred. Subtylase-type serine proteases are more preferred. The term "subtylase" refers to a serine protease subgroup 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 defined by having a serine in the active site, which form a covalent adduct with the substrate. The subtylases can be divided into 6 subdivisions, i.e., the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.

[0061] Examples of subtylases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in US 7262042 and WO 09/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD 138 described in WO 93/18140. Other useful proteases may be those described in WO 92/175177, WO 01/016285, WO 02/026024 and WO 02/016547. Examples of trypsin-like proteases are trypsin (eg of porcine or bovine origin) and the Fusarium protease described in WO 89/06270, WO 94/25583 and WO 05/040372 and Cellumonas derived chymotrypsin proteases described in WO 05/052161 and WO 05/052146.

Most preferably the protease is a subtilisin (EC 3.4.21.62).

[0063] Examples of subtylases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in US 7262042 and WO 09/021867, and subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, Bacillus licheniformis, subtilisin BPN', subtilisin 309, subtilisin 147 and subtilisin 168 described in WO 89/06279 and protease PD 138 described in WO 93/18140. Preferably, the subtilisin is derived from Bacillus, preferably Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii as described in US 6312936 B1, US 5679630, US 4760025, US 7262042 and WO 09/021867 . More preferably the subtilisin is derived from Bacillus gibsonii or Bacillus Lentus.

Suitable commercially available protease enzymes include those sold under the brand names Alcalase®, Blaze®, Duralase®, Duranzym®, Relase®, Relase Ultra®, Savinase®, Savinase Ultra®, Primase®, Polarzyme®, Kannase ®, Liquanase®, Liquanase Ultra®, Ovozyme®, Coronase®, Coronase Ultra®, Neutrase®, Everlase® and Esperase® can all be sold as Ultra® or Evity® (Novozymes A/S).

[0065] The composition can use cutinase, classified to EC 3.1.1.74. The cutinase used according to the invention can be of any origin. Preferably the cutinases are of microbial origin, in particular of bacterial, fungal or yeast origin.

Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin. Chemically modified proteins 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 1296839 or the strain of Bacillus sp. disclosed in WO 95/026397 or WO 00/060060. Commercially available amylases are Duramyl®, Termamyl®, Termamyl Ultra®, Natalase®, Stainzyme®, Amplify®, Fungamyl® and BAN® (Novozymes A/S), Rapidase® and Purastar® (from Genencor

International Inc.).

[0067] Suitable cellulases include those of bacterial or fungal origin. Chemically modified proteins or protein engineered mutants are included. Suitable cellulases include cellulases from the genus Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, eg fungal cellulase produced by Humicola insolens, Thielavia terrestris, Myceliophthora thermophila and Fusarium oxysporum disclosed in US 4435307, US 5647911, US 5648263, US /09259, WO 96/029397 and WO 98/012307. Commercially available cellulases include Celluzyme®, Carezyme®, Celluclean®, Endolase®, Renozyme® (Novozyme A/S), Clazinase® and Puradax HA® (Genencor International Inc.), and KAC-500(B)®, (Kao Corporation ). Celluclean® is preferred.

Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified proteins or protein engineered mutants are included. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus and variants thereof such as those described in WO 93/24618, WO 95/10602 and WO 98/15257. Commercially available peroxidases include Guardzyme® and Novozym® 51004 (Novozymes A/S).

[0069] Additional enzymes suitable for use are discussed in WO 2009/087524, WO 2009/090576, WO 2009/107091, WO 2009/111258 and WO 2009/148983.

[0070] 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 of 0.01 to 10 ppm, preferably 0.05 to 1 ppm.

Enzyme Stabilizers

[0071] Any enzyme present in the composition can be stabilized using conventional stabilizing agents, eg a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid or boric acid derivative, eg 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 eg WO 92/19709 and WO 92/19708.

chelating agent

[0072] Chelating agents may be present or absent in detergent compositions.

[0073] If present, then the chelating agent is present at a level of from 0.01 to 5% by weight.

[0074] Examples of phosphonic acid chelating agents (or salt thereof) are: 1-hydroxyethylidene-1,1-diphosphonic acid (HEDP); diethylenetriaminepenta(methylenephosphonic acid) (DTPMP); hexamethylenediaminetetra(methylenephosphonic) acid (HDTMP); aminotris(methylenephosphonic acid) (ATMP); ethylenediaminetetra(methylenephosphonic) acid (EDTMP); tetramethylenediaminetetra(methylenephosphonic) acid (TDTMP); and phosphonobutanetricarboxylic acid (PBTC).

Additional materials

Additional optional but preferred materials that may be included in detergent compositions (preferably laundry detergent compositions) include fluorescent agent, perfume, colorant and polymers.

Fluorescent agent

[0076] The composition preferably comprises a fluorescent agent (optical lightener). Fluorescent agents are well known and many such fluorescent agents are commercially available. Generally, these fluorescent agents are supplied and used in the form of their alkali metal salts, for example, sodium salts.

[0077] The total amount of fluorescent agent or agents used in the composition is generally 0.0001 to 0.5% by weight, preferably 0.005 to 2% by weight, more preferably 0.01 to 0.1% by weight.

Preferred classes of fluorescent agent are: biphenyl distyryl compounds, Tinopal®, CBS-X, diaminostilbene disulfonic acid compounds, e.g. Tinopal DMS pure Xtra and Blankophor® HRH, and pyrazoline compounds, e.g. Blankophor SN.

Preferred fluorescent agents are fluorescent agents with CAS #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.

[0080] Most preferred fluorescent agents are: 2-(4-styryl-3-sulfophenyl)-2H-naphthol[1,2-d]triazole sodium, 4,4'-bis{[(4-anilino-6- (N-methyl-N-2-hydroxyethyl)amino 1,3,5-triazin-2-yl)]amino}stilbene-2-2'-disodium disulfonate, 4,4'-bis{[(4-anilino Disodium -6-morpholino-1,3,5-triazin-2-yl)]amino}stilbene-2,2'-disulfonate and disodium 4,4'-bis(2-sulfostyryl)biphenyl.

[0081] The aqueous solution used in the method has a fluorescent agent present. The fluorescent agent is present in the aqueous solution used in the method preferably in the range of 0.0001 g/L to 0.1 g/L, more preferably 0.001 to 0.02 g/L.

perfume

[0082] The composition preferably comprises a perfume. Many suitable perfume examples are provided in the CTFA International Buyers Guide (Association of Cosmetics, Toiletries and Fragrances) 1992, published by CFTA Publications and the 80th annual edition of the 1993 OPD Chemical Buyers Directory, published by Schnell Publishing Co.

[0083] Preferably the perfume comprises at least one note

(compound) of: 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; verdil acetate; dodecanal; hexyl cinnamic aldehyde; cyclopentadecanolide; benzeneacetic acid, 2-phenylethyl ester; amyl salicylate; beta-caryophyllene; ethyl undecylenate; geranyl anthranilate; alpha-irone; beta-phenyl ethyl benzoate; alpha-santalol; cedrol; cedryl acetate; cedrilla shape; cyclohexyl salicylate; gamma-dodecalactone; and beta-phenylethyl phenyl acetate.

[0084] Useful components of perfume include materials with both natural and synthetic origin. They include compounds alone or mixtures. Specific examples of such components can be found in current literature, e.g. Fenaroli Flavor Ingredients Guide, 1975, CRC Press; Synthetic Food Adjuncts, 1947 by M.B. Jacobs, edited by Van Nostrand; or Perfume and Aroma Chemicals by S. Arctander 1969, Montclair, N.J. (USA).

[0085] It is common practice for a plurality of perfume components to be present in a formulation. In the compositions of the present invention it is envisaged that there are four or more, preferably five or more, more preferably six or more or even more preferably seven or more different perfume components.

[0086] In perfume blends preferably 15 to 25% by weight are top notes. Top notes are set by Poucher (Journal of the Society of Cosmetic Chemists 6(2):80 [1955]). Preferred top notes are selected from oils of citrus, linalool, linalyl acetate, lavender, dihydromyrcenol, rose oxide and cis-3-hexanol.

[0087] The International Fragrance Association published a list of fragrance ingredients (perfumes) in 2011 (http://ifraorg.org/en-us/ingredients#.U7Z4hPldWzk).

[0088] The Fragrance Materials Research Institute provides a database of perfumes (fragrances) with reliable information.

[0089] Perfume top notes can be used to suggest the whiteness and shine benefit of the invention.

[0090] Some or all of the perfumes may be encapsulated, typical perfume components where 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°C. It is also advantageous to encapsulate perfume components that have a low CLog P (i.e., those that have a greater tendency to partition in water), preferably with a CLog P of less than 3.0. These relatively low boiling and relatively low CLog P materials have been called "prolonged bloom" 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 isovalerate, benzyl propionate, beta gamma hexenol, camphor gum, laevo-carvone, d-carvone, cinnamic alcohol, cinnamyl formate, cis -jasmone, cis-3-hexenyl acetate, cumin alcohol, cyclal C, dimethyl benzyl carbinol, dimethyl benzyl carbinol acetate, ethyl acetate, ethyl acetate, ethyl amyl ketone, ethyl benzoate, ethyl butyrate, ethyl hexyl ketone , ethyl phenyl acetate, eucalyptol, eugenol, fenchyl acetate, flower acetate (decenyl tricycle acetate), fructone (decenyl tricycle propionate), geraniol, hexenol, hexenyl acetate, hexyl acetate, hexyl formate, alcohol ol hydrate, hydroxycitronellal, indone, isoamyl alcohol, isomentone, isopulegyl acetate, isoquinolone, ligustral, linalool, linalool oxide, linalyl formate, menthone, mentyl acetophenone, methyl amyl ketone, methyl methyl acetate, benzoate benyl, methyl eugenol, methyl heptenone, methyl heptin carbonate, methyl heptyl ketone, methyl hexyl ketone, methyl phenyl carbinyl acetate, methyl salicylate, methyl-n-methyl anthranilate, nerol, octalactone, octyl alcohol, p-cresol , p-cresol methyl ether, p-methoxy acetophenone, p-methyl acetophenone, phenoxy ethanol, phenyl acetaldehyde, phenyl ethyl acetate, phenyl ethyl alcohol, phenyl ethyl dimethyl carbinol, prenyl acetate, propyl borne, pulegone, rose oxide , safrol, 4-terpinelol, alpha-terpinelol and/or viridine. It is common practice for a plurality of perfume components to be present in a formulation. In the compositions of the present invention it is envisaged that there are four or more, preferably five or more, more preferably six or more or even more preferably seven or more perfume components different from the list given above of extended flowering perfumes present in the perfume.

[0091] Another group of perfumes with which the present invention can be applied are the so-called 'aromatherapy' materials. These include various components also used in perfumery, including essential oil components such as clary sage, eucalyptus, geranium, lavender, apple extract, neroli, nutmeg, peppermint, violet anise and valerian.

It is preferred that the laundry treatment composition does not contain a peroxygen bleach, e.g. sodium percarbonate, sodium perborate and peracid.

coloring dye

[0093] Preferably when the composition is a laundry detergent composition then it comprises a colorant. Preferably, the colorant is present at 0.0001 to 0.1% by weight of the composition.

[0094] Dyes are described in Color Chemistry Synthesis, Properties and Applications of Organic Dyes and Pigments (H. Zollinger, Wiley VCH, Zürich, 2003) and, Industrial Dye Chemistry, Properties and Applications (K Hunger (ed), Wiley-VCH Weinheim 2003).

[0095] Color dyes for use in laundry compositions preferably have an extinction coefficient at maximum absorption in the visible range (400 to 700nm) of more than 5000 L mol-1cm-1, preferably more than 10000 L mol-1cm-1 . Dyes are blue or violet in color.

Preferred colorant chromophores are azo, azine, anthraquinone and triphenylmethane.

[0097] Azo, anthraquinone, phthalocyanine and triphenylmethane dyes preferably carry a net anionic charge or are uncharged. Azine preferably carries a net anionic or cationic charge. Blue or violet shade dyes deposit on the fabric during the wash or rinse step of the wash process providing a visible shade to the fabric. In this context, the dye gives a blue or violet color to a white fabric having a hue angle of 240 to 345, more preferably 250 to 320, more preferably 250 to 280. The white fabric used in this test was a non-woven cotton sheet. bleached mercerized.

Coloring dyes are described in WO 2005/003274, WO 2006/032327 (Unilever), WO 2006/032397 (Unilever), WO 2006/045275 (Unilever), WO 2006/027086 (Unilever), WO 2008/017570 ( Unilever), WO 2008/141880 (Unilever), WO 2009/132870 (Unilever), WO 2009/141173 (Unilever), WO 2010/099997 (Unilever), WO 2010/102861 (Unilever), WO 2010/148624 (Unilever) , WO 2008/087497 (P&G), WO 2011/011799 (P&G), WO 2012/054820 (P&G), WO 2013/142495 (P&G) and WO 2013/151970 (P&G).

[0099] Monoazo dyes preferably contain a heterocyclic ring and are more preferably thiophene dyes. Monoazo dyes are preferably alkoxylated and are preferably uncharged or anionically charged at pH=7. Alkoxylated thiophene dyes are described in WO 2013/142495 and WO 2008/087497. Preferred examples of thiophene dyes are shown below: (I);

(II); and, (III).

[0100] Bis-azo dyes are preferably sulfonated bis-azo dyes. Preferred examples of sulfonated bis-azo dyes are direct violet 7, direct violet 9, direct violet 11, direct violet 26, direct violet 31, direct violet 35, direct violet 40, direct violet 41, direct violet 51, direct violet 66, violet direct 99 and alkoxylated versions thereof. Bis-azo alkoxylated dyes are described in WO 2012/054058 and WO 2010/151906.

[0101] An example of an alkoxylated bis-azo dye is: (IV).

[0102] Thiophene dyes are available from Milliken under the brand names of Liquitint Violet DD and Liquitint Violet ION.

[0103] Azine dyes are preferably selected from sulphonated phenazine dyes and cationic phenazine dyes. Preferred examples are acid blue 98, acid violet 50, dye with CAS #72749-80-5, acid blue 59 and phenazine dye selected from: (V), where: X3 is selected from: -H; -F; -CH3; -C 2H5; -OCH3; and -OC 2H5; X4 is selected from: -H; -CH3; -C2H5; -OCH3; and -OC2H5; Y2 is selected from: -OH; -OCH2CH2OH; -CH(OH)CH2OH; -OC(O)CH3; and C(O)OCH3.

[0104] The colorant dye is present in the composition in the range of 0.0001 to 0.5% by weight, preferably 0.001 to 0.1% by weight. Depending on the nature of the dye dye, there are preferred ranges depending on the efficacy of the dye dye which is dependent on the particular class and efficacy within any particular class. As mentioned above, the dye dye is a blue or violet dye dye.

[0105] A mixture of coloring dyes can be used.

[0106] The shade dye is even more preferably a blue reactive anthraquinone dye covalently bonded to an alkoxylated polyethyleneimine. Alkoxylation is preferably selected from ethoxylation and propoxylation, more preferably propoxylation. Preferably 80 to 95 mol% of the N-H groups in the polyethyleneimine are replaced with isopropyl alcohol groups by propoxylation. Preferably the polyethyleneimine prior to reaction with dye and propoxylation has a molecular weight of 600 to 1800.

[0107] An example of a structure of a reactive anthraquinone covalently linked to a propoxylated polyethyleneimine is:

(VI) Polymers

[0108] The composition may comprise one or more additional polymers. Examples are carboxymethylcellulose, poly(ethylene glycol), poly(vinyl alcohol), polycarboxylates like polyacrylates, maleic/acrylic acid copolymers and lauryl methacrylate/acrylic acid copolymers.

Examples

[0109] The invention will be demonstrated by the following non-limiting examples. Biochemical determination of lipase activity

[0110] Lipase activity was determined by a colorimetric method using 4-nitrophenyl-valerate (C5) and 4-nitrophenyl-dodecanoate (C12) as substrates. 4-nitrophenyl-dodecanoate (25 mg) or 4-nitrophenyl-valerate (18 mg) were dissolved in 10 mL of solvent (methanol) to prepare stock solutions of

8mm. Before performing the assay, 1 mL of stock solution was added to 7 mL of acidified water (pH 4.5) to give a final concentration of 1 mM. In 96-well microtiter plates, 60 µl dH2O, 115 µl Tris-HCl buffer (pH 8.5, 50 mM), 5 µl diluted enzyme solution and 20 µl substrate (multi-channel at the end) were added . For blanks, the enzyme solution was replaced with dH2O. Following addition of reagents, product release (4-nitrophenol) was monitored at 405nm for 15 min at room temperature in a Varioskan plate reader. Storage of lipase and SRP in laundry formulation

[0111] In a laundry formulation containing 2% w/w Texcare UL soil release polymer, different lipases were added to give the same unit/ml activity as a 0.4% w/v addition of the Lipex 100L reference enzyme (Novozymes), based on specific activity as cited by the commercial lipase supplier. This level corresponded to a final lipase addition of 400 units/ml, which in the case of Lipex 100L is a final lipase concentration of 0.08 mg/ml. A control incubation without lipase was also performed. Formulations with and without lipases were stored in incubators at 37 °C or 45 °C for a minimum of 4 weeks. After different time intervals, 1 mL samples were transferred into an Eppendorf tube and stored at -20 °C before analysis by NMR. After 4 weeks of incubation, lipase activity was assessed in the remaining storage samples. 1H-NMR studies of the SRP structure

[0112] Standard qualitative and quantitative experiments were performed using a Bruker Avance DRX 400 MHz spectrometer. Samples were prepared as polymeric solutions in D 2 O to monitor polymer stability as fully formulated laundry liquids after storage. D 2O containing 0.05% 3-(trimethylsilyl)propionic acid, sodium salt (TSP) as internal standards. Signals are indicated in parts per million (ppm) relative to TSP.

MTP wash studies for lipase wash performance

[0113] Woven cotton fabric stained with either frying fat (CS46B) or meat fat (CS61) (Test Materials Center - Netherlands) was cut into empty 96-well microtiter plates and prewash readings were collected for the intensity of the stain. Lipase solutions were prepared in FH32 water, and subsequently transferred (200µL) to the spots using a multi-channel pipette just before incubation at 40°C, with shaking at 200 rpm for 20 min. After washing, the washing liquid was immediately removed using a multi-channel pipette, and the stain discs were washed 3x with 200 µl of dH2O, before leaving overnight in a cabinet to dry. After drying, the stain plates were digitally scanned and their deltaE was measured. This value is used to express cleaning effect and is defined as the color difference between a white garment and that of stained garment after washing. Mathematically, the definition of deltaE is: deltaE = [(ΔL) 2 + (Δa) 2 + (Δb) 2] 1/2 (1) where ΔL is measured by the difference in darkness between washed and white tissue; Δa and Δb are measured by the difference in redness and yellowness respectively between both tissues. From this equation, it is clear that the smaller the deltaE value, the whiter the tissue will be. In connection with this color measurement technique, reference is made to the International Commission on l'Eclairage (CIE); Recommendation on Uniform Color Spaces, Color Difference Equations, Psychometric Color Terms, Supplement No. 2 to CIE Publication No. 15, Colorimetry, CIE Head Office, Paris, 1978.

[0114] Here the cleaning effect is expressed in the form of stain removal index (SRI): SRI = 100 – deltaE (2)

[0115] The higher the SRI, the cleaner the fabric, SRI = 100 (white).

Mini-vial wash studies for SRP/lipase cleaning benefit Pre-wash fabrics:

[0116] Washed woven polyester fabric was cut into 5x5cm squares. In a 250ml glass vial, 0.5g of stored formulation containing SRP and lipase was diluted with 200ml of Prenton water and the polyester tissue was added before incubation at 30°C for 30 min. This gave a final SRP concentration of 50 ppm (in the wash). The fabric was rinsed twice in Prenton water and allowed 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. Stain application:

[0117] A stain used for these experiments was sunflower oil containing 0.2% Macrolex violet dye. A volume of 100 µL per stain sample was applied and allowed to dry and age for 5 days at room temperature, before taking a 'prewash' reading on stain intensity (DE* value). Main wash:

[0118] The main wash to clean the macrolex sunflower oil/dye stain was a repetition of the prewash conditions, however, using 3 squares of stained fabric plus 2 squares of ballast cotton fabric; 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 the SRI as a measure of cleanliness. Wash studies in Tergo for SRP/lipase cleaning benefit Pre-wash fabrics:

[0119] Washed woven polyester fabric was cut into 5x5cm squares. In a Tergo vessel, 2.5 g of stored formulation containing SRP and lipase was diluted with 1 L of FH26 water and the polyester tissue was added before incubation at 30 °C for 30 min. Ballast cotton fabric was added to ensure a net:fabric ratio of 20:1 was maintained. This gave a final SRP concentration of 50 ppm (in the wash). The fabric was rinsed twice in FH26 water and left to dry, before repeating the wash again using the same formulation and conditions. Control used was formulation containing SRP but no lipase. Stain application:

[0120] The stain used for these experiments was palm oil. A volume of 200 µL per polyester stain sample was applied and allowed to dry and age for 3 days at room temperature. Main wash:

[0121] The main wash to clean the palm oil stain was a repetition of the pre-wash conditions, however, using 4 squares of palm oil stained fabric plus 3 lard stained cotton swatches (for the measure of cleaning the palm oil lipase). Ballast cotton fabric has been added to ensure a net:fabric ratio of 20:1. Following the wash, the fabric was rinsed twice in FH26 water and allowed to dry before taking a 'post wash' stain intensity reading and calculating the SRI as a measure of cleanliness.

Example 1 - Classification of different lipases for formulation storage stability

[0122] To compare against the commercially available reference lipase Lipex 100L (a fungal lipase) which is known to degrade the soil release polymer (SRP) Texcare UL, three different commercially available fungal lipases, plus two lipases of bacterial origin and one of plant were incubated in a laundry formulation containing SRP for a period of 4 weeks, from which 1 mL samples were extracted to test lipase activity and for SRP integrity. SRP was a polyester-based dirt release polymer based on a polypropylene terephthalate polymer.

[0123] 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 (PinLip) originates from Psychromonas ingrahamii, and was supplied as a purified enzyme by the University of Exeter (the enzyme used is identical to that disclosed in WO 2017/036901). Wheat germ lipase (purchased from Sigma Aldrich – cat. no: L3001) was also tested in these studies. Based on the activity of the specific lipase as cited by the commercial supplier or determined in a previous work, lipases were incorporated into storage samples to give the same unit/mL activity as a 0.4% w/v addition of the reference enzyme Lipex 100L - corresponding to a final lipase addition of 400 units/ml. Of the six lipases tested against Lipex, only two of these were shown to retain lipase activity after 4 weeks of storage in a laundry laundry formulation (containing the SRP). Both bacterial lipases were found to be active after the 4 week storage period. With the Amano lipase from Burkholderia cepacia maintaining a similar level of activity as the reference Lipex 100L. None of the fungal/plant lipases that were purchased from Sigma Aldrich proved to be active after 4 weeks storage in the laundry formulation at 37°C.

[0124] This experiment shows that bacterial lipases retain their cleaning effectiveness function after storage in a detergent composition containing a soil release polymer.

Example 2 - Comparison of lipase activity versus dirt release polymer degradation

[0125] Formulation samples from those that maintained lipase activity after 4 weeks of storage (i.e., control Lipex 100L, PinLip de

Psychromonas ingrahamii, and Amano lipase from Burkholderia cepacia) were tested for SRP integrity via NMR.

[0126] Figure 1 shows the NMR spectrum for the formulation containing SRP that was incubated for 4 weeks in the absence of lipase. This figure shows that the NMR peak corresponding to the SRP maintains its shape after storage at both 37°C and 45°C for 4 weeks (i.e., spectrum identical to t=0).

[0127] In contrast, Figure 2 shows how peak integrity is lost when Lipex 100L is included in the SRP laundry laundry formulation. This leads to a reduction in the polymer peak as well as an increase in peak intensity corresponding to peaks related to the monomer unit (terephthalic acid) and oligomer. Interestingly, when incubated with Amano lipase from Burkholderia cepacia, NMR clearly shows the SRP maintaining structural integrity despite the 4-week incubation period at both 37°C and 45°C (figure 3). The measurements of lipase activity taken from this same sample were previously described in example 1. Interestingly, lipase from Psychromonas ingrahamii (PinLip) also showed no hydrolytic activity relative to SRP Texcare, with the period of the NMR samples in Figure 4 showing preservation of the SRP NMR peak throughout the storage period at 45 °C.

[0128] This result shows that lipases of bacterial origin are preferable for compatibility with SRP, since fungal Lipex 100L is particularly aggressive towards hydrolysis of SRP, even after only 1 week of incubation.

Example 3 - Measurement of the cleaning benefit of residual SRP after storage of lipases in the formulation containing SRP - Lipex 100L vs. pinlip

[0129] With NMR analysis of stored formulations previously showing the preservation of SRP structural integrity (example 2), and biochemical assays showing lipase activity remaining (example 1), the following results provide a measure of the cleaning benefit that arise due to the presence of SRP and lipase.

[0130] Table 1 shows that within the formulation controls, the presence of SRP results in a noticeably large increase in cleanliness (~10 dSRI). In the SRP formulation containing Lipex 100L the cleaning level is reduced compared to the SRP formulation itself. This shows that the cleaning benefit due to SRP is greater than that of Lipex 100L, and underscores the importance of preserving the SRP under storage. Cleaning benefits due to a structurally intact dirt release polymer and an active bacterial lipase (Amano or PinLip) are also shown in the table. The additional cleaning benefit of having the lipase present with the SRP is seen in these cases. Table 1: Showing the positive effect of bacterial lipases with SRP Sample SRI Negative Control 85.45 ± 2.42 (formulation – SRP) Positive Control 93.96 ± 0.72 (formulation + SRP) A 92.03 ± 0. 22 Formulation + SRP + Lipex 100L 1 95.85 ± 0.45 Formulation + SRP + Amano lipase 2 95.91 ± 0.77 Formulation + SRP + PinLip

[0131] The formulation without SRP or lipase resulted in an SRI of ~85. Adding SRP has improved SRI to ~94. Addition of Lipex 100L, a fungal lipase enzyme, to the positive control had a negative effect, so the SRI was even lower than the positive control. Addition of either of the 2 bacterial enzymes (Lipase Amano or PinLip) showed no negative effect on SRP and resulted in a small statistical improvement over the positive control.

Claims (9)

Claims 1. Detergent composition characterized in that it comprises: (i) from 0.1% to 10% by weight, preferably from 0.2% to 9% by weight, more preferably from 0.25% to 8%, even more preferably from 0 .5 to 6% by weight, even more preferably from 1% to 5% by weight of a soil release polymer; and, (ii) from 0.0005% to 2.5% by weight, preferably from 0.005 to 2% by weight, more preferably from 0.01 to 1% by weight of a non-fungal lipase enzyme, wherein the polymer of soil release is a polyester based soil release polymer, where the soil release polymer is a soil release polymer based on polyethylene terephthalate and/or propylene terephthalate; and, wherein the non-fungal lipase enzyme is a bacterial lipase enzyme derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingranhamii. 2. Detergent composition according to claim 1, characterized in that the detergent composition comprises from 1 to 60% by weight, preferably from 2.5 to 50% by weight, more preferably from 4 to 40% by weight, even more preferably from 8 to 35% by weight of a surfactant. 3. Detergent composition, according to claim 2, characterized in that the detergent composition comprises an anionic and/or non-ionic surfactant, preferably comprising both anionic and non-ionic surfactants. 4. Detergent composition according to any one of the preceding claims, characterized in that the detergent composition is a laundry detergent composition. 5. Detergent composition according to claim 4, characterized in that it is for laundry and the laundry detergent composition is a liquid or a powder, preferably a liquid detergent. 6. Detergent composition according to claims 4 or 5, characterized in that it is for laundry and in that the detergent composition comprises an alkoxylated polyamine, preferably at a level of from 0.1% to 8% by weight, more preferably 0. 2% to 6% by weight, even more preferably from 0.5% to 5% by weight. 7. Detergent composition according to any one of the preceding claims, characterized in that it additionally comprises an additional enzyme selected from the group consisting of: proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases and/or mannanases. 8. Method of treating a substrate with a detergent composition characterized by comprising i) a lipase enzyme; and ii) a soil release polymer, preferably a polyester soil release polymer based on polyethylene terephthalate and/or polypropylene terephthalate; to provide lipolytic cleaning without degradation of said polyester soil release polymer, said method comprising incorporating in a detergent composition a bacterial lipase enzyme in a detergent composition as defined in any one of claims 1 to 7; and subsequently treating a substrate, preferably fabrics, with said composition. 9. Use of a bacterial lipase enzyme derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingrahamii characterized by being in a detergent composition, comprising a polyester soil release polymer, preferably a polyethylene terephthalate and/or soil release polymer polypropylene terephthalate, to provide lipolytic cleaning without degradation of said polyester dirt release polymer.