EP3853330B1

EP3853330B1 - Detergent composition

Info

Publication number: EP3853330B1
Application number: EP19765252.2A
Authority: EP
Inventors: Dietmar Andreas LANG; Mark Lawrence THOMPSON
Original assignee: Unilever Global IP Ltd; Unilever IP Holdings BV
Current assignee: Unilever Global IP Ltd; Unilever IP Holdings BV
Priority date: 2018-09-17
Filing date: 2019-09-09
Publication date: 2023-06-07
Anticipated expiration: 2039-09-09
Also published as: EP3853330A1; WO2020058024A1; CN112703246A; ZA202101254B; BR112021004507A2; AR116411A1

Description

Field of Invention

The invention concerns a detergent composition, in particular a detergent composition comprising a soil release polymer and a lipase.

Background of the Invention

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, such as described in WO 93/23516 A1 , WO 97/19155 A1 , EP 3 301 162 A1 , WO 2012/010407 A1 and EP 0 839 186 A1 . However, inclusion of lipase enzymes causes degradation of the soil release polymer. So the formulator has to forgo one of these useful ingredients.
A problem with inclusion of lipases is that they cannot be included in a detergent formulation with soil release polymers.
This problem is particularly pronounced in laundry detergent formulations, especially liquid laundry detergent formulations.

Summary of the Invention

We have found that the incorporation of non-fungal lipase enzymes in detergent compositions doesn't cause degradation of the soil release polymer. However, the non-fungal lipases still provide effective cleaning.
In one aspect the present invention provides a detergent composition according to present claim 1, wherein the composition comprises:

(i) 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; and,
(ii) from 0.0005 to 2.5 wt.%, preferably from 0.005 to 2 wt.%, more preferably from 0.01 to 1 wt.% of a non-fungal lipase enzyme,

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.
Preferably 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.
In another aspect the present invention provides a method of treatment of a substrate with a detergent composition according to present claim 8, wherein the detergent composition comprises i) the above-mentioned lipase enzyme; and ii) the above-mentioned 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 above-mentioned composition of the first aspect; and subsequent treatment of a substrate, preferably textiles, with said composition.
In another aspect the present invention provides the use of the above-mentioned bacterial lipase enzyme, according to present claim 9, in a detergent composition comprising a polyethylene and/or polypropylene terephthalate polyester soil release polymer, to provide lipolytic cleaning without degradation of said polyester soil release polymer.

Brief description of the figures

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 Exeter)

Detailed Description of the Invention

The 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.
All % levels of ingredients in compositions (formulations) listed herein are in wt.% based on total formulation unless other stated.
It is understood that any reference to a preferred ingredient of the detergent composition is envisaged to be combinable subject matter with any other preferred ingredient of the detergent composition disclosed herein.
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.

Soil release polymer

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 selected as 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 .

Non-fungal lipases

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. Such 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.
The non-fungal lipase enzyme of the present invention is a bacterial lipase enzyme.
Examples of bacterial lipases, are classified in Arpigny & Jaeger (1999) and Lopez-Lopez et al., 2014).
The bacterial lipases of the present invention are derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingrahamii.
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.
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 soil release polymer due to degradation of the polymer.

Surfactant

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.
Examples of suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher C₈ to C₁₈ alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl C₉ to C₂₀ benzene sulphonates, particularly sodium linear secondary alkyl C₁₀ to C₁₅ benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
The anionic surfactant is preferably selected from: linear alkyl benzene sulphonate; alkyl sulphates; alkyl ether sulphates; soaps; alkyl (preferably methyl) ester sulphonates, and mixtures thereof.
The most preferred anionic surfactants are selected from: linear alkyl benzene sulphonate; alkyl sulphates; alkyl ether sulphates and mixtures thereof. Preferably 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). Preferably the linear alkyl benzene sulphonate is a sodium C₁₁ to C₁₅ alkyl benzene sulphonates. Preferably the alkyl sulphates is a linear or branched sodium C₁₂ to C₁₈ alkyl sulphates. Sodium dodecyl sulphate is particularly preferred, (SDS, also known as primary alkyl sulphate).
In liquid formulations preferably two or more anionic surfactant are present, for example linear alkyl benzene sulphonate together with an alkyl ether sulphate.
In liquid formulations, preferably 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 C₈ to C₁₈ primary or secondary linear or branched alcohols with ethylene oxide.
Most preferably the nonionic detergent compound is the alkyl ethoxylated non-ionic surfactant is a C₈ to C₁₈ primary alcohol with an average ethoxylation of 7EO to 9EO units.
Preferably the 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

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: 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.
Preferably the further enzyme is selected from: proteases, cellulases, and/or alpha-amylases.
Protease enzymes hydrolyse bonds within peptides and proteins, in the laundry context this leads to enhanced removal of protein or peptide containing stains. Examples of suitable proteases families include aspartic proteases; cysteine proteases; glutamic proteases; aspargine peptide lyase; serine proteases and threonine proteases. Such protease families are described in the MEROPS peptidase database (http://merops.sanger.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 subdivisions, i.e. the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
Examples of subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and WO09/021867 , 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 PD138 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 (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 .
Most preferably the protease is a subtilisins (EC 3.4.21.62).
Examples of subtilases are those derived from Bacillus such as Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii described in; US7262042 and WO09/021867 , 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 ). Preferably the subsilisin is derived from Bacillus, preferably Bacillus lentus, B. alkalophilus, B. subtilis, B. amyloliquefaciens, Bacillus pumilus and Bacillus gibsonii as described in US 6,312,936 B1 , US 5,679,630 , US 4,760,025 , US7,262,042 and WO 09/021867 . Most preferably the 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 (alpha and/or beta) 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 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.).
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 Celluzyme^™, Carezyme^™, Celluclean ^™, Endolase^™, Renozyme^™ (Novozymes 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 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 Guardzyme^™ and Novozym^™ 51004 (Novozymes A/S).
Further enzymes suitable for use are discussed in WO 2009/087524 , WO 2009/090576 , WO 2009/107091 , WO 2009/111258 and WO 2009/148983 .
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 1ppm.

Enzyme Stabilizers

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 .

Chelating Agent

Chelating agents may be present or absent from the detergent compositions.
If present, then 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); Aminotris(methylenephosphonic acid) (ATMP); Ethylenediaminetetra(methylenephosphonic acid) (EDTMP); Tetramethylenediaminetetra(methylenephosphonic acid) (TDTMP); and, Phosphonobutanetricarboxylic acid (PBTC).

Further materials

Further optional but preferred materials that may be included in the detergent compositions (preferably laundry detergent compositions) include fluorescent agent, perfume, shading dyes and polymers.

Fluorescent Agent

The composition preferably comprises a fluorescent agent (optical brightener). Fluorescent agents are well known and many such fluorescent agents are available commercially. Usually, 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.
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.
Most preferred 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.

Perfume

The composition preferably comprises a perfume. Many suitable examples of 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.
Preferably 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; geranyl anthranilate; alpha-irone; beta-phenyl ethyl benzoate; alpa-santalol; cedrol; cedryl acetate; cedry formate; cyclohexyl salicyate; gamma-dodecalactone; and, beta phenylethyl phenyl acetate.
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).
It is commonplace for a plurality of perfume components to be present in a formulation. In the 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.
In perfume mixtures preferably 15 to 25 wt% are top notes. Top notes are defined by Poucher (Journal of the Society of Cosmetic Chemists 6(2):80 [1955]). Preferred top-notes are selected from citrus oils, linalool, linalyl acetate, lavender, dihydromyrcenol, rose oxide and cis-3-hexanol.
The International Fragrance Association has published a list of fragrance ingredients (perfumes) in 2011. (http://www.ifraorg.org/en-us/ingredients#.U7Z4hPidWzk)
The Research Institute for Fragrance Materials provides a database of perfumes (fragrances) with safety information.
Perfume top note may be used to cue the whiteness and brightness benefit of the invention.
Some or all of the 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 advantageous to encapsulate perfume components 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, dimethyl benzyl carbinol, dimethyl benzyl carbinol acetate, ethyl acetate, ethyl aceto acetate, ethyl amyl ketone, ethyl benzoate, ethyl butyrate, ethyl hexyl ketone, ethyl phenyl acetate, eucalyptol, eugenol, fenchyl acetate, flor acetate (tricyclo decenyl acetate) , frutene (tricyclco decenyl propionate) , geraniol, hexenol, hexenyl acetate, hexyl acetate, hexyl formate, hydratropic alcohol, hydroxycitronellal, indone, isoamyl alcohol, iso menthone, isopulegyl acetate, isoquinolone, ligustral, linalool, linalool oxide, linalyl formate, menthone, menthyl acetphenone, methyl amyl ketone, methyl anthranilate, methyl benzoate, methyl benyl acetate, methyl eugenol, methyl heptenone, methyl heptine 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 bornate, pulegone, rose oxide, safrole, 4-terpinenol, alphaterpinenol, and /or viridine. It is commonplace for a plurality of perfume components to be present in a formulation. In the 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.
Another group of 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, Lavender, Mace Extract, Neroli, Nutmeg, Spearmint, Sweet Violet Leaf and Valerian.
It is preferred that the laundry treatment composition does not contain a peroxygen bleach, e.g., sodium percarbonate, sodium perborate, and peracid.

Shading Dye

Preferably when the composition is a laundry detergent composition, then it comprises a shading dye. Preferably 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, Zürich, 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 5000 L mol^-1 cm^-1, preferably greater than 10000 L mol^-1 cm^-1. 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.
Shading dyes are discussed 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 ).
Mono-azo dyes preferably contain a heterocyclic ring and are most preferably thiophene dyes. The mono-azo dyes are preferably alkoxylated and are preferably uncharged or anionically charged at pH=7. Alkoxylated thiophene dyes are discussed in WO/2013/142495 and WO/2008/087497 . Preferred examples of thiophene dyes are shown below:

and,
Bis-azo dyes are preferably sulphonated bis-azo dyes. Preferred examples of sulphonated bis-azo compounds are direct violet 7, direct violet 9, direct violet 11, direct violet 26, direct violet 31, direct violet 35, direct violet 40, direct violet 41, direct violet 51, Direct Violet 66, direct violet 99 and alkoxylated versions thereof. Alkoxylated bis-azo dyes are discussed in WO2012/054058 and WO2010/151906 .
An example of an alkoxylated bis-azo dye is :
Thiophene dyes are available from Milliken under the tradenames of Liquitint Violet DD and Liquitint Violet ION.
Azine dye are preferably selected from sulphonated phenazine dyes and cationic phenazine dyes. Preferred examples are acid blue 98, acid violet 50, dye with CAS-No 72749-80-5, acid blue 59, and the phenazine dye selected from:
wherein:

X₃ is selected from: -H; -F; -CH₃; -C₂H₅; -OCH₃; and, -OC₂H₅;
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.

The shading dye is present is present in the composition in range from 0.0001 to 0.5 wt %, preferably 0.001 to 0.1 wt%. Depending upon the nature of the shading dye there are preferred ranges depending upon the efficacy of the shading dye which is dependent on class and particular efficacy within any particular class. As stated above 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. Preferably 80 to 95 mol% of the N-H groups in the polyethylene imine are replaced with iso-propyl alcohol groups by propoxylation. Preferably 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:

Polymers

The 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.

Examples

The invention will be demonstrated by the following non-limiting examples.

Biochemical determination of lipase activity

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

Storage of lipase and SRP in laundry formulation

Into 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 benchmark enzyme Lipex 100L (Novozymes), based on the specific activity as quoted by the commercial supplier of the lipase. This level of addition corresponded to a final lipase addition of 400 Units/mL, which in the case of Lipex 100L is a final lipase concentration of 0.08mg/mL. A control incubation without lipase was also made. Formulations with and without lipases were stored in incubators at either 37°C or 45°C for a minimum of 4 weeks. After different time intervals, 1mL samples were transferred into an Eppendorf tube and stored at -20°C prior to NMR analysis. After 4 weeks incubation, lipase activity was assayed in the remaining storage sample.

¹H-NMR studies of SRP structure

Standard qualitative and quantitative experiments were performed using a Bruker Avance DRX 400 MHz spectrometer. Samples were prepared as polymer solutions in D₂O to track polymer stability as fully formulated laundry liquids after storage. D₂O contained 0.05% 3-(trimethylsilyl)propionic acid, sodium salt (TSP) as the internal standards. Signals are quoted in parts per million (ppm) relative to TSP.

Wash studies in MTP for lipase wash performance

Woven cotton fabric stained with either frying fat (CS46B) or beef fat (CS61) (Centre for Testmaterials - Netherlands) was cut into empty 96-well microtitre plates and pre-wash readings taken for stain intensity. Lipase solutions were prepared in FH32 water, and subsequently transferred (200µL) to the stains using a multi-channel pipette just prior to incubation at 40°C, with shaking at 200rpm for 20min. Following washing, the wash liqueur was immediately removed using a multi-channel pipette, and the stain discs washed 3× with 200µL dH₂O, before leaving overnight in a cupboard to dry. 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. Mathematically, the definition of deltaE is: $deltaE = [(Δ L) 2 + (Δ a) 2 + (Δ b) 2] 1 / 2$
wherein ΔL is a measure of the difference in darkness between the washed and white cloth; Δa and Δb are measures for the difference in redness and yellowness respectively between both cloths. From this equation, it is clear that the lower the value of deltaE, the whiter the cloth will be. With regard to this colour measurement technique, reference is made to Commission International de I'Eclairage (CIE); Recommendation on Uniform Colour Spaces, colour difference equations, psychometric colour terms, supplement no. 2 to CIE Publication, no. 15, Colormetry, Bureau Central de la CIE, Paris 1978.
Herein the cleaning effect is expressed in the form of a stain removal index (SRI): $SRI = 100 - deltaE .$
The higher the SRI the cleaner the cloth, SRI = 100 (white).

Wash studies in mini-bottles for SRP/lipase cleaning benefit

Pre-washing fabrics:

Washed-off knitted polyester fabric was cut into 5×5cm 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.

Application of stain:

One stain used for these experiments was sunflower oil containing 0.2% Macrolex Violet dye. A volume of 100µL 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).

Main wash:

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.

Wash studies in Tergo for SRP/lipase cleaning benefit

Pre-washing fabrics:

Washed-off knitted polyester fabric was cut into 5×5cm squares. Into a 1L Tergo pot, 2.5g of stored formulation containing SRP and lipase was diluted with 1L 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.

Application of stain:

The stain used for these experiments was Dende oil. A volume of 200µL per polyester stain swatch was applied and allowed to dry and age for 3 days at r/t.

Main wash:

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.

Example 1 - Screening of different lipases for formulation storage stability

To compare against the benchmark commercially available lipase Lipex 100L (a fungal lipase) which is known to degrade Texcare UL soil release polymer (SRP), 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 1mL 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 (PinLip) originates from Psychromonas ingrahamii, and was supplied as purified enzyme by the University of Exeter (the enzyme used is identical to that disclosed in WO 2017/036901 ). The 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). Both bacterial lipases were found to be active after the 4 week storage period, with Amano lipase from Burkholderia cepacia maintaining a similar level of activity to the Lipex 100L benchmark. None of the fungal/plant lipases which were purchased from Sigma Aldrich proved to be active after 4-week's storage in the laundry formulation at 37°C.
This experiment shows that the bacterial lipases retain their cleaning efficacy function after storage in a detergent composition containing a soil release polymer.

Example 2 - Comparison of lipase activity towards soil release polymer degradation

Formulation samples from those that retained lipase activity after 4 weeks storage (i.e. Lipex 100L control, PinLip from Psychromonas ingrahamii, and Amano lipase from Burkholderia cepacia) were tested for SRP integrity via NMR.
Figure 1 shows the NMR spectra for SRP-containing formulation which has been incubated for 4 weeks in the absence of lipase. This figure shows that the NMR peak corresponding to SRP retains its shape after storage at both 37°C and 45°C for 4 weeks (i.e. identical spectra to T=0).
In contrast, 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. Interestingly, when incubated with Amano lipase from Burkholderia cepacia, 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. Interestingly, lipase from Psychromonas ingrahamii (PinLip) 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.

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

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

Table 1 shows that within the formulation controls, the presence of SRP results in a large noticeable increase in cleaning (~10 dSRI). In 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

Sample	SRI
Negative Control (formulation - SRP)	85.45 ± 2.42
Positive Control (formulation + SRP)	93.96 ± 0.72
A Formulation + SRP + Lipex 100L	92.03 ± 0.22
1 Formulation + SRP + Amano lipase	95.85 ± 0.45
2 Formulation + SRP + PinLip	95.91 ± 0.77

The formulation without SRP or lipase gave a SRI of ~85. Adding the SRP improved the SRI to ~94. Addition of Lipex 100L, a fungal lipase enzyme, to the positive control, had a negative effect, such that the SRI was even less than the positive control. Addition of either of 2 bacterial enzymes (Amano lipase or PinLip) did not show the negative effect on the SRP and gave a small statistical improvement over the positive control.

Claims

A detergent composition comprising:
(i) 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; and,

(ii) from 0.0005 to 2.5 wt.%, preferably from 0.005 to 2 wt.%, more preferably from 0.01 to 1 wt.% of a non-fungal lipase enzyme,

wherein the soil release polymer is a polyester based soil released polymer,

wherein the polyester soil release polymer is a polyethylene and/or polypropylene terephthalate based soil release polymer; and,

wherein the non-fungal lipase enzyme is a bacterial lipase enzyme derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingrahamii.
A detergent composition according to any preceding claim, wherein the detergent composition comprises from 1 to 60 wt.%, preferably from 2.5 to 50 wt.%, more preferably from 4 to 40 wt.%, most preferably from 8 to 35 wt.% of a surfactant.
A detergent composition according to claim 3, wherein the detergent composition comprises anionic and/or nonionic surfactant, preferably comprising both anionic and nonionic surfactant.
A detergent composition according to any preceding claim, wherein the detergent composition is a laundry detergent composition.
A laundry detergent composition according to claim 4, wherein the laundry detergent composition is a liquid or a powder, preferably a liquid detergent.
A laundry detergent composition according to any one of claims 4 or 5, wherein the laundry 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.%.
A detergent composition according to any preceding claim, additionally comprising a further enzyme selected from the group consisting of: proteases, cellulases, alpha-amylases, peroxidases/oxidases, pectate lyases, and/or mannanases.
A method of treatment of a substrate with a detergent composition comprising i) a lipase enzyme; and ii) 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 any one of claims 1 to 7; and subsequent treatment of a substrate, preferably textiles, with said composition.
Use of a bacterial lipase enzyme derived from Burkholderia cepacia, Pseudomonas fluorescence or Psychromonas ingrahamii, in a detergent composition comprising a polyethylene and/or polypropylene terephthalate polyester soil release polymer, to provide lipolytic cleaning without degradation of said polyester soil release polymer.