Classifications

• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/14—Hydrolases (3)
  • C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
  • C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
  • C12N9/2405—Glucanases
  • C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
  • C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
• • C—CHEMISTRY; METALLURGY
  • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
  • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
  • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
  • C11D3/16—Organic compounds
  • C11D3/38—Products with no well-defined composition, e.g. natural products
  • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
  • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
  • C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
  • C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase
• • D—TEXTILES; PAPER
  • D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
  • D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
  • D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
  • D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms

Definitions

• the present invention relates to laundry detergent and/or fabric care compositions comprising a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) having a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4 l/gcellulose.
• CBD Cellulose Binding Domain
• Detergent compositions include nowadays a complex combination of active ingredients and in particular, detergent enzymes such as cellulases.
• cellulase is one in which cellulosic fibres or substrates are attacked by the cellulase and is depending on the particular function of the cellulase, which can be endo- or exo- cellulase and on the respective hemicellulases.
• the cellulose structures are depolymerized or cleaved into smaller and thereby more soluble or dispersible fractions. This activity in particular on fabrics provides cleaning, rejuvenation, softening and generally improved handfeel characteristics to the fabric structure.
• tensile strength loss of fabric is also an unavoidable result of mechanical action due to use/wearing and may further result from damage by a bleaching component in the laundry process, especially if the fabric is contaminated with metal compounds.
• the object of the present invention is to provide laundry detergent and/or fabric care compositions which achieve excellent fabric care, including anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide static control, fabric softness, colour appearance and fabric anti-wear properties and benefits, and which achieve excellent fabric cleaning while preventing tensile strength loss.
• laundry detergent and/or fabric care compositions comprising a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) having a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 41/gcellulose.
• CBD Cellulose Binding Domain
• WO91/10732 discloses an enzyme which exhibits cellulase activity, producible by a strain of Bacillus spp., NICMB 40250, especially an 75, 56 or 45 kD Molecular weight endoglucanase or characterised by a high specific activity for e.g. detergency application, providing softening, soil removal and colour clarification.
• Novel derivatives of cellulase enzymes combining a core region derived from said endoglucanase with a CBD derived from another cellulase enzyme or a combining a core region derived from another cellulase enzyme with a CBD derived from said endoglucanase, are therein contemplated to construct cellulase enzymes with improved binding properties.
• WO94/07998 describes cellulase variants of a cellulase classified in family 45, comprising a CBD, a Catalytically Active Domain (CAD) and a region linking the CBD to the CAD, wherein one or more amino acid residues have been added, deleted or substituted and/or another CBD is added at the opposite end of the CAD.
• CAD Catalytically Active Domain
• These enzymes have improved properties such as alkaline activity, harshness reduction, compatibility with detergent ingredients, particulate soil removal, colour clarification, defuzzing, depilling, harshness reduction and sensitivity to anionic surfactants and peroxidase bleaching systems and are useful in detergent compositions.
• WO95/16782 relates to the cloning and high level expression of novel truncated cellulase proteins or derivatives thereof in Trichoderma longibrachiatum. Combinations of different core regions with several CBDs are described in the fibre/fabric context.
• a cellulolytic enzyme preparation comprising a cellulase with reduced mobility, e.g. by increasing the molecular weight or apparent size of the cellulase protein molecule or by insolubilising or immobilising the cellulase, has been disclosed in WO97/01629.
• the mobility of the cellulase component may be reduced by adsorption to an insoluble or soluble carrier e.g. via the existing or newly introduced CBD.
• a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain having a Kr-a of a definite value, thereby defining a cellulase especially adapted to selectively bind and hydrolyse amorphous cellulose of cotton containing fabrics for a laundry and/or fabric care application.
• the present invention relates a modified cellulolytic enzyme demonstrating selective binding and hydrolysis of amorphous cellulose in cotton containing fabrics.
• the present invention further relates to a laundry detergent and/or fabric care composition comprising said modified enzyme. Said compositions achieve excellent fabric care and fabric cleaning while preventing tensile strength loss.
• This modified enzyme comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) having a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 41/gcellulose.
• CBD Cellulose Binding Domain
• the present invention relates to a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain further characterised by having a relative binding constant for bacterial microcrystalline cellulose (Kr-c) lower than 11/gcellulose, preferably lower than 0.51/gcellulose.
• Kr-c bacterial microcrystalline cellulose
• the modified enzyme of the present invention comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain further characterised by having a relative binding constant (Kr-a) for binding to amorphous cellulose to a relative binding constant for bacterial microcrystalline cellulose (Kr-c) ratio above 3.
• Kr-a relative binding constant for binding to amorphous cellulose
• Kr-c relative binding constant for bacterial microcrystalline cellulose
• the present invention further relates to laundry detergent and/or fabric care compositions comprising said modified enzyme and which preferably further comprise a detergent ingredient selected from cationic surfactants, dye transfer inhibiting polymer, builders, - in particular zeolite A and sodium tripolyphosphate - and/or clays .
• a detergent ingredient selected from cationic surfactants, dye transfer inhibiting polymer, builders, - in particular zeolite A and sodium tripolyphosphate - and/or clays .
• the present invention relates to a modified enzyme which comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a cellulose binding domain having a relative binding constant for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4 l/gcellulose.
• a modified enzyme for use in accordance with the present invention comprises a catalytically active (enzymatically active) amino acid sequence (in general a polypeptide amino acid sequence) of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain having a high affinity for binding to amorphous cellulose.
• the catalytically active amino acid sequence in question may comprise or consist of the whole of - or substantially the whole of - the full amino acid sequence of the mature enzyme in question, or it may consist of a portion of the full sequence which retains substantially the same catalytic (enzymatic) properties as the full sequence.
• enzymes hybrid is described in WO 91/10732 wherein novel derivatives of cellulase enzymes combining a core region derived from a Bacillus NICB 40250 endoglucanase with a CBD derived from another cellulase enzyme or a combining a core region derived from another cellulase enzyme with a CBD derived from a Bacillus NICB 40250 endoglucanase, are constructed.
• WO 95/16782 describes the combinations of different core regions with several CBD and the cloning and high level expression of these novel truncated cellulase proteins or derivatives thereof, in Trichoderma longibrachiatum.
• fusion protein a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain ligated, with or without a linker, to a DNA sequence encoding the enzyme of interest, and growing the transformed host cell to express the fused gene.
• a DNA construct comprising at least a fragment of DNA encoding the cellulose-binding domain ligated, with or without a linker, to a DNA sequence encoding the enzyme of interest, and growing the transformed host cell to express the fused gene.
• CBD is an amino acid sequence comprising at least the cellulose-binding domain (CBD) perse.
• MR (the middle region; a linking region) may be a bond, or a linking group comprising from 1 to about 100 amino acid residues, in particular of from 2 to 40 amino acid residues, e.g. from 2 to 15 amino acid residues.
• MR may, in principle, alternatively be a non-amino-acid linker (See below).
• X is an amino acid sequence comprising the above-mentioned, catalytically
• moieties A and B are independently optional. When present, a moiety A or
• B constitutes a terminal extension of a CBD or X moiety, and normally comprises one or more amino acid residues.
• a CBD in an enzyme hybrid of the type in question may be positioned C-terminally, N-terminally or internally in the enzyme hybrid.
• an X moiety in an enzyme hybrid of the type in question may be positioned N-terminally, C-terminally, or internally in the enzyme hybrid.
• Enzyme hybrids of interest in the context of the invention include enzyme hybrids which comprise more than one CBD, e.g. such that two or more CBDs are linked directly to each other, or are separated from one another by means of spacer or linker sequences (consisting typically of a sequence of amino acid residues of appropriate length).
• Two CBDs in an enzyme hybrid of the type in question may, for example, also be separated from one another by means of an -MR-X- moiety as defined above.
• One or more cellulose binding domain can be linked to the N-terminal and/or C-terminal parts of the cellulase core region. Any part of a CBD can be selected, modified, truncated etc.
• Two- and multi- domain proteins are particularly susceptible towards proteolytic cleavage of linker regions connecting the domains.
• Proteases causing such cleavage may, for example, be subtilisins, which are known to often exhibit broad substrate specificities [see, e.g. : Gr ⁇ n et al., Biochemistry 3_1 (1992), pp. 6011-6018; Teplyakov et al., Protein Engineering 5 (1992), pp. 413-420].
• Glycosylation of linker residues in eukaryotes is one Nature's ways of preventing proteolytic degradation.
• the length of the linker also plays a role in relation to accessibility by proteases. Which "solution” is optimal depends on the environment in which the enzyme hybrid is to function. When constructing new enzyme hybrid molecules, preferably attention will be paid to the linker stability.
• the expression cassette may be included within a replication system for episomal maintenance in an appropriate cellular host or may be provided without a replication system, where it may become integrated into the host genome.
• the DNA may be introduced into the host in accordance with known techniques such as transformation, microinjection or the like.
• the host may be grown to express the fused gene. Normally it is desirable additionally to add a signal sequence which provides for secretion of the fused gene.
• useful genes are :
• the recombinant product may be glycosylated or non- glycosylated.
• Cellulolytic enzymes Any enzyme which exhibits a cellulase activity is suitable for the purpose of the present invention and includes cellulases without naturally occurring CBD, cellulase to which a CBD of Kr-a for binding to amorphous cellulose higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4 l/gcellulose, is added and/or cellulases having a CBD presenting a lower Kr value, to which a CBD of Kr-a higher than 2.41/gcellulose, preferably higher than 3.51/gcellulose, more preferably higher than 4 l/gcellulose, is then substituted or added.
• the catalytically active amino acid sequence of a cellulolytic enzyme can be derived from any cellulase.
• the cellulases usable in the present invention include both bacterial or fungal cellulases. Preferably, they will have a pH optimum of between 5 and 12 and a specific activity above 50 CEVU/mg (Cellulose Viscosity Unit).
• Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and WO96/02653 which discloses fungal cellulase produced respectively from Humicola insolens, Trichoderma, Thielavia and Sporotrichum.
• EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable cellulases are also disclosed in GB-A- 2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and WO95/26398.
• cellulases examples include cellulases produced by a strain of Humicola insolens (Humicola grisea var. thermoidea), particularly the Humicola strain DSM 1800.
• Other suitable cellulases are cellulases originated from Humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a " 43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application No. WO 91/17243.
• suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum described in WO94/21801 , Genencor, published September 29, 1994. Especially suitable cellulases are the cellulases having colour care benefits. Examples of such cellulases are cellulases described in European patent application No. 91202879.2, filed November 6, 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A/S) are especially useful. See also WO91/17244 and WO91/21801. Other suitable cellulases for fabric care and/or cleaning properties are described in WO96/34092, WO96/17994 and WO95/24471.
• Preferred catalytically active amino acid sequences of a cellulolytic enzyme for the laundry detergent and/or fabric care compositions of the present invention are producible by a fungal strain, preferably produced by a strain of Humicola insolens and more preferably is a " 43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity.
• Said modified cellulolytic enzymes are normally incorporated in the laundry detergent and/or fabric care composition at levels from 0.0001 % to 2%, preferably 0.0001% to 0.5%, more preferably 0.0005% to 0.1 % of pure modified enzyme by weight of the detergent composition.
• Preferred catalytically active amino acid sequence of a cellulolytic enzyme for specific applications are derived from alkaline cellulases, i.e. enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of their maximum activity at a pH ranging from 7 to 12, preferably 10.5. More preferred core cellulases are enzymes having their maximum activity at a pH ranging from 7 to 12, preferably 10.5.
• the above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used.
• the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased.
• the variant may be designed such that the optimal pH, bleach or chelant stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular cleaning application.
• the isoelectric point of such enzymes may be modified by the substitution of some charged amino acids, e.g. an increase in isoelectric point 10
• the stability of the enzymes may be further enhanced by the creation of e.g. additional salt bridges and enforcing metal binding sites to increase chelant stability.
• CBD Cellulose Binding Domain
• amino acid sequence comprising a CBD, Cellulose Binding Domain or CBD are intended to indicate an amino acid sequence capable of effecting binding of the cellulase to a cellulosic substrate (e.g., as described in P. Kraulis et al., Determination of the three-dimensional structure of the C terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamically simulated annealing. Biochemistry 28:7241-7257, 1989). The classification and properties of cellulose binding domains are presented in P. Tomme et al., in the symposium “Enzymatic degradation of insoluble polysaccharides” (ACS Symposium Series 618, edited by J.N. Saddler and M.H. Penner, ACS, 1995).
• Cellulose-binding (and other carbohydrate-binding) domains are polypeptide amino acid sequences which occur as integral parts of large polypeptides or proteins consisting of two or more polypeptide amino acid sequence regions, especially in hydrolytic enzymes (hydrolases) which typically comprise a catalytic domain containing the active site for substrate hydrolysis and a carbohydrate- binding domain for binding to the carbohydrate substrate in question.
• hydrolytic enzymes hydrolases
• Such enzymes can comprise more than one catalytic domain and one, two or three carbohydrate-binding domains, and they may further comprise one or more polypeptide amino acid sequence regions linking the carbohydrate-binding domain(s) with the catalytic domain(s), a region of the latter type usually being denoted a "linker".
• Cellulose-binding domains have also been found in algae, e.g. in 11
• cellulose-binding domain is intended to be understood in the same manner as in the latter reference (P. Tomme et al., op. cit. )
• the P. Tomme et al. reference classifies more than 120 "cellulose-binding domains" into 10 families (l-X) which may have different functions or roles in connection with the mechanism of substrate binding. However, it is to be anticipated that new family representatives and additional families will appear in the future.
• a CBD may be located at the N or C terminus or at an internal position.
• the part of a polypeptide or protein (e.g. hydrolytic enzyme) which constitutes a CBD per se typically consists of more than about 30 and less than about 250 amino acid residues.
• those CBDs listed and classified in Family I in accordance with P. Tomme et al. (op. cit.) consist of 33-37 amino acid residues
• those listed and classified in Family lla consist of 95-108 amino acid residues
• those listed and classified in Family VI consist of 85-92 amino acid residues
• one CBD derived from a cellulase from Clostridium thermocellum listed and classified in Family VII consists of 240 amino acid residues.
• the molecular weight of an amino acid sequence constituting a CBD per se will typically be in the range of from about 4kD to about 40kD, and usually below about 35kD.
• Cellulose binding domains can be produced by recombinant techniques as described in H. Stalbrand et al., Applied and Environmental Microbiology, Mar. 1995, pp. 1090-1097; E. Brun et al., (1995) Eur. J. Biochem. 231, pp. 142-148; J.B. Coutinho et al., (1992) Molecular Microbiology 6(9), pp. 1243-1252 12
• a cellulose binding domain of, e.g. a cellulase several genetic engineering approaches may be used.
• One method uses restriction enzyme to remove a portion of the gene and then to fuse the remaining gene-vector fragment in frame to obtain a mutated gene that encodes a protein truncated for a particular gene fragment.
• Another method involves the use of exonucleases such as Ba131 to systematically delete nucleotides either externally from the 5' and the 3' ends of the DNA or internally from a restricted gap within the gene.
• exonucleases such as Ba131 to systematically delete nucleotides either externally from the 5' and the 3' ends of the DNA or internally from a restricted gap within the gene.
• Appropriate substrates for evaluating the binding ability include cellulosic materials such as Avicel TM and cotton fibres.
• Other methods include the use of a selective or specific protease capable of cleaving a CBD, e.g. a terminal CBD, from the remainder of the polypeptide chain of the protein in question.
• nucleotide sequence encoding the substrate-binding (carbohydrate-binding) region may then be manipulated in a variety of ways to fuse it to a DNA sequence encoding the enzyme or enzymatically active amino acid sequence of interest.
• the DNA fragment encoding the carbohydrate- binding amino acid sequence, and the DNA encoding the enzyme or enzymatically active amino acid sequence of interest are then ligated with or without a linker.
• the resulting ligated DNA may then be manipulated in a variety of ways to achieve expression.
• Preferred microbial expression hosts include certain Aspergillus species (e.g. A. niger or A. oryzae), Bacillus species, and organisms such as Escherichia coli or Saccharomyces cerevisiae.
• Microcrystalline cellulose (Avicel PH101) can be obtained from FMC International (Little Island, County Cork, Ireland).
• Bacterial microcrystalline cellulose (BMCC) can be prepared from cultures of Acetobacter xylinum (ATCC 23769) as described in Gilkes at al. 1992.
• Regenerated cellulose (PASC) can be obtained by phosphoric-acid treatment of Avicel PH101 as reported in J. B. Coutinho at al., (1992) Mol. Microbiol. 6, 1243-1252.
• Suitable CBDs for the purpose of the present invention are the CBDs derived from a fungal or bacterial strain, preferably a bacterial strain, more preferably from Family II or IV according the current classification [See P. Tomme et al. (op cit.)]; having a relative binding constant (Kr-a) for binding to amorphous cellulose higher than 2.4l/gcellulose, preferably higher than 3.5l/gcellulose, more preferably higher than 4l/gcellulose cellulase.
• Kr-a relative binding constant
• CBDs are CBDs from family IV as currently classified, derived from organisms selected from Cellulomonas fimi, Clostridium stecorarium (NCIMB11754), Clostridium cellulolyticum, Myxocccus xanthus, Streptomyces reticuli and/or Thermomonospora fusca.
• Most preferred CBDs are the CBDs selected from CBDs of the tandem N-terminal cellulose binding domains from Cellulomonas fimi ⁇ -1 ,4-glucanase CenC which binds amorphous but not crystalline cellulose (P.E. Johnson et al., (1996) Biochem. 35, 13895-13906 and 14381-14394; J.B.
• CBD-dimer from Clostridium stecorarium (NCIMB11754) XynA and/or the CBD E3 from Thermonospora fusca.
• the cellulose binding domains for the purpose of the present invention will be further characterised by having a relative binding constant for crystalline cellulose (Kr-c) lower than 1 l/gcellulose, preferably lower than 0.5l/gcellulose. 14
• the modified enzyme of the present invention comprises a catalytically active amino acid sequence of a cellulolytic enzyme linked to an amino acid sequence comprising a Cellulose Binding Domain (CBD) further characterised by having a relative binding constant (Kr-a) for binding to amorphous cellulose to a relative binding constant for crystalline cellulose (Kr-c) ratio above 3.
• CBD Cellulose Binding Domain
• the modified enzyme comprising a catalytically active (enzymatically active) amino acid sequence of a cellulolytic enzyme linked to CBD as defined in the present invention, will provide an enzymatic hydrolysis activity on phosphoric acid- swollen cellulose higher than 60 moles glucose equivalents released per minute and per mole enzyme. Activities were determined at 37°C and pH7 (N. Din et al., (1995) Prog. Biotech. 10, pp. 261-270).
• linker or “linking region” or “Middle region- MR” is intended to indicate a region that might adjoin the CBD and connect it to the catalytically active amino acid sequence of the cellulolytic enzyme. When present, this linking can be achieved chemically or by recombinant techniques.
• linking regions are amino acid (peptides), some examples thereof are described in N.R. Gilkes et al., Microbiol. Rev. 55, 1991 , pp. 303-315.
• the linking region can comprise from 1 to about 100 amino acid residues, in particular of from 2 to 40 amino acid residues, e.g. from 2 to 15 amino acid residues. As stated above, it is preferred to use amino acids which are less favored by the surrounding proteases.
• Suitable amino acid linking regions are the Humicola insolens family 45 cellulase linker, the NifA gene of Klebsiella pneumoniae-C P linker, the E. coli OmpA gene-CiP linker, the E3 cellulase Thermomonospora fusca linker and the CenA cellulase linker.; preferably the 15
• Non amino acid/proteinic compounds referred to as “non-amino acid” can also be used for the linking of the catalytically active amino acid sequence to the CBD :
• Suitable non-amino acid linking regions are the polyethylene glycol derivatives described in the Shearwater polymers, Inc. catalog of January 1996, such as the nucleophilic PEGs, the carboxyl PEGs, the electrophilically activated
• PEGs the vinyl derivatives, the PEG silanes and the PEG phospholipids.
• suitable non-amino acid linking regions are the heterofunctional PEG,
• (X-PEG-Y) polymers from Shearwater such as PEG(NPC)2, PEG-(NH2)2, t-
• DSS disuccinimidyl suberate
• GMBS ⁇ - maleimidobutyric acid N-hydroxysuccinimide ester
• EDC 1-ethyl- 3-(3-dimethylaminopropyl)carbodiimide hydrochi
• Non-amino acid linking regions are 1-ethyl-3-(3- dimethylaminopropyl) carbodiimide, N-ethyl-5-phenylisoaxolium-3-sulphonate, 1- cyclohexyl-3(2morpholinoethyl) carbodide metho-p-toluene sulphonate, N- ethoxycarbonyl-2-ethoxy 1,2, dihydroquinoline or glutaraldehyde.
• Crosslinkers described in the 1999/2000 Pierce Products Catalogue from the Pierce Company, under the heading "Cross linking reagents : the SMPH, SMCC, LC-SMCC compounds, and preferably the Sulfo-KMUS compound.
• Preferred chemical linking regions are PEG(NPC)2, (NH2)2-PEG, t-BOC-NH- PEG-NH2, MAL-PEG-NHS, VS-PEG-NHS polymers from Shearwater and/or the Sulfo-KMUS compound from Pierce.
• the laundry detergent and/or fabric care compositions of the invention will comprise at least one additional detergent and/or fabric care components.
• the laundry detergent and/or fabric care compositions of the present invention preferably further comprise a detergent ingredient selected from cationic surfactants, dye transfer inhibiting polymers, builders - in particular zeolite A and sodium tripolyphosphate - and/or clays.
• a detergent ingredient selected from cationic surfactants, dye transfer inhibiting polymers, builders - in particular zeolite A and sodium tripolyphosphate - and/or clays.
• the laundry detergent and/or fabric care compositions according to the invention can be liquid, paste, gels, bars, tablets, spray, foam, powder or granular forms.
• Granular compositions can also be in "compact” form, the liquid compositions can also be in a "concentrated” form.
• compositions of the invention may for example, be formulated as hand and machine laundry detergent compositions including laundry additive compositions and compositions suitable for use in the soaking and/or pretreatment of stained fabrics, rinse added fabric softener compositions.
• Pre-or post treatment of fabric include gel, spray and liquid fabric care compositions.
• a rinse cycle with or without the presence of softening agents is also contemplated.
• compositions suitable for use in a laundry machine washing method preferably contain both a surfactant and a builder compound and additionally one or more detergent components preferably selected from organic polymeric compounds, bleaching agents, additional enzymes, suds suppressors, dispersants, lime-soap dispersants, soil suspension and anti-redeposition agents and corrosion inhibitors.
• Laundry compositions can also contain softening agents, as additional detergent components. 17
• compositions of the invention can also be used as detergent additive products in solid or liquid form.
• Such additive products are intended to supplement or boost the performance of conventional detergent compositions and can be added at any stage of the cleaning process.
• the density of the laundry detergent compositions herein ranges from 400 to 1200 g/litre, preferably 600 to 950 g/litre of composition measured at 20°C.
• compositions herein are best reflected by density and, in terms of composition, by the amount of inorganic filler salt; inorganic filler salts are conventional ingredients of detergent compositions in powder form; in conventional detergent compositions, the filler salts are present in substantial amounts, typically 17-35% by weight of the total composition. In the compact compositions, the filler salt is present in amounts not exceeding 15% of the total composition, preferably not exceeding 10%, most preferably not exceeding 5% by weight of the composition.
• the inorganic filler salts, such as meant in the present compositions are selected from the alkali and alkaline-earth-metal salts of sulphates and chlorides. A preferred filler salt is sodium sulphate.
• Liquid detergent compositions according to the present invention can also be in a "concentrated form", in such case, the liquid detergent compositions according the present invention will contain a lower amount of water, compared to conventional liquid detergents.
• the water content of the concentrated liquid detergent is preferably less than 40%, more preferably less than 30%, most preferably less than 20% by weight of the detergent composition.
• the laundry detergent and/or fabric care compositions according to the present invention comprise a surfactant system wherein the surfactant can be selected from nonionic and/or anionic and/or cationic and/or ampholytic and/or zwitterionic and/or semi-polar surfactants.
• Preferred surfactants are cationic surfactants. It has been surprisingly found that the laundry detergent and/or fabric care compositions further comprising a cationic surfactant, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti- shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour appearance and fabric anti-wear properties and benefits and improved fabric cleaning while preventing tensile strength loss.
• the surfactant is typically present at a level of from 0.1% to 60% by weight. More preferred levels of incorporation are 1 % to 35% by weight, most preferably from 1 % to 30% by weight of laundry detergent and/or fabric care compositions in accord with the invention.
• the surfactant is preferably formulated to be compatible with enzyme components present in the composition.
• the surfactant is most preferably formulated such that it promotes, or at least does not degrade, the stability of any enzyme in these compositions.
• Cationic detersive surfactants suitable for use in the laundry detergent and/or fabric care compositions of the present invention are those having one long- chain hydrocarbyl group.
• cationic surfactants include the ammonium surfactants such as alkyltrimethylammonium halogenides, and those surfactants having the formula :
• R2 is an alkyl or alkyl benzyl group having from about 8 to about 18 carbon atoms in the alkyl chain, each R ⁇ is selected from the group consisting of -CH 2 CH 2 -, -CH 2 CH(CH 3 )-, -CH 2 CH(CH 2 OH)-, -CH 2 CH 2 CH 2 -, and mixtures thereof; each R 4 is selected from the group consisting of C1-C4 alkyl, C1-C4 hydroxyalkyl, benzyl ring structures formed by joining the two R 4 groups, - 1 9
• R 6 is any hexose or hexose polymer having a molecular weight less than about 1000, and hydrogen when y is not 0;
• R5 is the same as R 4 or is an alkyl chain wherein the total number of carbon atoms of R2 plus R 5 is not more than about 18; each y is from 0 to about 10 and the sum of the y values is from 0 to about 15; and
• X is any compatible anion.
• Quaternary ammonium surfactant suitable for the present invention has the formula (I):
• R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the formula (II) :
• y is 2-4, preferably 3. whereby R2 is H or a C1-C3 alkyl, whereby x is 0-4, preferably 0-2, most preferably 0, whereby R3, R4 and R5 are either the same or different and can be either a short chain alkyl (C1-C3) or alkoxylated alkyl of the formula III,
• X" is a counterion, preferably a halide, e.g. chloride or methylsulfate.
• R6 is C-
• Preferred quat ammonium surfactants are those as defined in formula I whereby R-
• Highly preferred cationic surfactants are the water-soluble quaternary ammonium compounds useful in the present composition having the formula :
• is CQ-C ⁇ Q alkyl
• each of R 2 , R 3 and R4 is independently C1-C4 alkyl, C1-C4 hydroxy alkyl, benzyl, and -(C 2 H4o) x H where x has a value from 2 to 5, and X is an anion.
• R 2 , R 3 or R4 should be benzyl.
• is C-
• R2R 3 and R4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosulphate, acetate and phosphate ions.
• suitable quaternary ammonium compounds of formulae (i) for use herein are : coconut trimethyl ammonium chloride or bromide; coconut methyl di hydroxyethyl ammonium chloride or bromide; decyl triethyl ammonium chloride; decyl dimethyl hydroxyethyl ammonium chloride or bromide; C ⁇ 2 _i5 dimethyl hydroxyethyl ammonium chloride or bromide; coconut dimethyl hydroxyethyl ammonium chloride or bromide; myristyl trimethyl ammonium methyl sulphate; lauryl dimethyl benzyl ammonium chloride or bromide; lauryl dimethyl (ethenoxy)4 ammonium chloride or bromide; choline esters (com
• Typical cationic fabric softening components include the water-insoluble quaternary-ammonium fabric softening actives or the corresponding amine precursor, the most commonly used having been di-long alkyl chain ammonium chloride or methyl sulfate.
• Preferred cationic softeners among these include the following:
• DTDMAC ditallow dimethylammonium chloride
• DSOEDMAC di(stearoyloxyethyl) dimethylammonium chloride
• Biodegradable quaternary ammonium compounds have been presented as alternatives to the traditionally used di-long alkyl chain ammonium chlorides and methyl sulfates. Such quaternary ammonium compounds contain long chain alk(en)yl groups interrupted by functional groups such as carboxy groups. Said materials and fabric softening compositions containing them are disclosed in numerous publications such as EP-A-0,040,562, and EP-A-0,239,910.
• the quaternary ammonium compounds and amine precursors herein have the formula (I) or (II), below : 22
• Q is selected from -O-C(O)-, -C(0)-0-, -0-C(0)-0-, -NR 4 -C(0)-, -C(O)-
• R 1 is (CH 2 ) n -Q-T2 or T 3 ;
• R 2 is (CH 2 ) m -Q-T 4 or T$ or R 3 ;
• R 3 is C1-C4 alkyl or C1-C4 hydroxyalkyl or H;
• R 4 is H or C1-C4 alkyl or C1-C4 hydroxyalkyl
• T1 , T , T 3 , T 4 , T ⁇ are independently C-j -
• Non-limiting examples of softener-compatible anions include chloride or methyl sulfate.
• the alkyl, or alkenyl, chain T ' ' , ⁇ 2, T 3 , T 4 , T ⁇ must contain at least 11 carbon atoms, preferably at least 16 carbon atoms.
• the chain may be straight or branched.
• Tallow is a convenient and inexpensive source of long chain alkyl and alkenyl material.
• the compounds wherein T1 , T2, T 3 , T 4 , T ⁇ represents the mixture of long chain materials typical for tallow are particularly preferred.
• Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening compositions herein include :
• the laundry detergent and/or fabric care compositions of the present invention typically comprise from 0.2% to about 25%, preferably from about 1 % to about 8% by weight of such cationic surfactants.
• Polyethylene, polypropylene, and polybutylene oxide condensates of alkyl phenols are suitable for use as the nonionic surfactant of the surfactant systems of the present invention, with the polyethylene oxide condensates being preferred.
• These compounds include the condensation products of alkyl phenols having an alkyl group containing from about 6 to about 14 carbon atoms, preferably from about 8 to about 14 carbon atoms, in either a straight-chain or branched-chain configuration with the alkylene oxide.
• the ethylene oxide is present in an amount equal to from about 2 to about 25 moles, more preferably from about 3 to about 15 moles, of ethylene oxide per mole of alkyl phenol.
• nonionic surfactants of this type include IgepalTM CO-630, marketed by the GAF Corporation; and TritonTM ⁇ _45 j ⁇ . 1 ⁇ ⁇ _ ⁇
• the condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide are suitable for use as the nonionic surfactant of the nonionic surfactant systems of the present invention.
• the alkyl chain of the aliphatic alcohol can either be straight or branched, primary or secondary, and generally contains from about 8 to about 22 carbon atoms. Preferred are the condensation products of alcohols having an alkyl 24
• nonionic surfactants of this type include TergitolTM 15-S-9 (the condensation product of C ⁇ ⁇
• NeodolTM 23-3 the condensation product of C-
• Neodof M 45.7 he condensation product of C14-C15 linear alcohol with
• NeodolTM 45.5 the condensation product of C-14-
• nonionic surfactant of the surfactant systems of the present invention are the alkylpolysaccharides disclosed in U.S. Patent 4,565,647, Llenado, issued January 21 , 1986, having a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units.
• a hydrophobic group containing from about 6 to about 30 carbon atoms, preferably from about 10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7 saccharide units.
• Any reducing saccharide containing 5 or 6 carbon atoms can be used, e.g., glucose, galactose and galactosyl moieties can be substituted for the glucosyl moieties (optionally the hydrophobic group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or galactose as opposed to a glucoside or galactoside).
• the intersaccharide bonds can be, e.g., between the one position of the additional saccharide units and the 2-, 3-, 4-, and/or 6- positions on the preceding saccharide units. 25
• the preferred alkylpolyglycosides have the formula
• R2 is selected from the group consisting of alkyl, alkylphenyl, hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which the alkyl groups contain from about 10 to about 18, preferably from about 12 to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 to about 10, preferably 0; and x is from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably from about 1.3 to about 2.7.
• the glycosyl is preferably derived from glucose. To prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed first and then reacted with glucose, or a source of glucose, to form the glucoside (attachment at the 1 -position). The additional glycosyl units can then be attached between their 1 -position and the preceding glycosyl units 2-, 3-, 4- and/or 6-position, preferably predominately the 2-position.
• the condensation products of ethylene oxide with a hydrophobic base formed by the condensation of propylene oxide with propylene glycol are also suitable for use as the additional nonionic surfactant systems of the present invention.
• the hydrophobic portion of these compounds will preferably have a molecular weight of from about 1500 to about 1800 and will exhibit water insolubility.
• the addition of polyoxyethylene moieties to this hydrophobic portion tends to increase the water solubility of the molecule as a whole, and the liquid character of the product is retained up to the point where the polyoxyethylene content is about 50% of the total weight of the condensation product, which corresponds to condensation with up to about 40 moles of ethylene oxide.
• Examples of compounds of this type include certain of the commercially-available Plurafac ⁇ M LF404 and PluronicTM surfactants, marketed by BASF.
• nonionic surfactant of the nonionic surfactant system of the present invention are the condensation products of ethylene oxide with the product resulting from the reaction of propylene oxide and ethylenediamine.
• the hydrophobic moiety of these products consists of the reaction product of ethylenediamine and excess propylene oxide, and generally has a molecular weight of from about 2500 to about 3000. This hydrophobic moiety is condensed with ethylene oxide to the extent that the condensation product 2 6
• nonionic surfactant contains from about 40% to about 80% by weight of polyoxyethylene and has a molecular weight of from about 5,000 to about 11 ,000.
• nonionic surfactant include certain of the commercially available TetronicTM compounds, marketed by BASF.
• Preferred for use as the nonionic surfactant of the surfactant systems of the present invention are polyethylene oxide condensates of alkyl phenols, condensation products of primary and secondary aliphatic alcohols with from about 1 to about 25 moles of ethylene oxide, alkylpolysaccharides, and mixtures thereof. Most preferred are C8-C14 alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and CS-C-J S alcohol ethoxylates (preferably C-
• Highly preferred nonionic surfactants are polyhydroxy fatty acid amide surfactants of the formula.
• Rl is H, or Rl is C-1-.4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R is Cs_ 3 ⁇ hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxylated derivative thereof.
• R1 is methyl
• R2 is a straight C11-.15 alkyl or C-
• Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction.
• Suitable anionic surfactants to be used are linear alkyl benzene sulfonate, alkyl ester sulfonate surfactants including linear esters of C8-C 2 j carboxylic acids
• Suitable starting materials would include natural fatty substances as derived from tallow, palm oil, etc.
• alkyl ester sulfonate surfactant especially for laundry applications, comprise alkyl ester sulfonate surfactants of the structural formula: 27
• R 3 is a C8-C 2 rj hydrocarbyl, preferably an alkyl, or combination thereof,
• R 4 is a C ⁇ -CQ hydrocarbyl, preferably an alkyl, or combination thereof, and M is a cation which forms a water soluble salt with the alkyl ester sulfonate.
• Suitable salt-forming cations include metals such as sodium, potassium, and lithium, and substituted or unsubstituted ammonium cations, such as mono-ethanolamine, diethanolamine, and triethanolamine.
• R 3 is C-
• R 4 is methyl, ethyl or isopropyl.
• the methyl ester sulfonates wherein R 3 is C10-C-15 alkyl.
• alkyl sulfate surfactants which are water soluble salts or acids of the formula ROS0 3 M wherein R preferably is a
• C ⁇ ⁇ o-C 2 4 hydrocarbyl preferably an alkyl or hydroxyalkyl having a C-
• an alkali metal cation e.g. sodium, potassium, lithium
• ammonium or substituted ammonium e.g.
• alkylamines such as ethylamine, diethylamine, triethylamine, and mixtures thereof, and the like.
• alkyl chains of C12-C16 are preferred for lower wash temperatures (e.g. below about 50°C) and C16-I8 a " ⁇ y' chains are preferred for higher wash temperatures (e.g. above about 50°C).
• anionic surfactants useful for detersive purposes can also be included in the laundry detergent and/or fabric care compositions of the present invention.
• salts including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di- and triethanolamine salts
• soap C8-C22 primary of secondary alkanesulfonates, C8-C24 olefinsulfonates, sulfonated polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline earth metal citrates, e.g., as described in British patent specification No.
• alkylpolyglycolethersulfat.es (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty 28
• oleyl glycerol sulfates alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates, alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates, alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates (especially saturated and unsaturated C12-C18 rnonoesters) and diesters of sulfosuccinates (especially saturated and unsaturated C6-C12 diesters), acyl sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of alkylpolyglucoside (the nonionic nonsulfated compounds being described below), branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as those of the formula RO(CH2CH2 ⁇ )
• the laundry detergent compositions of the present invention typically comprise from about 1% to about 40%, preferably from about 3% to about 20% by weight of such anionic surfactants.
• alkyl alkoxylated sulfate surfactants hereof are water soluble salts or acids of the formula RO(A) m S03M wherein R is an unsubstituted C10-C24 alkyl or hydroxyalkyl group having a C10-C24 alkyl component, preferably a C12-C20 alkyl or hydroxyalkyl, more preferably C12-
• A is an ethoxy or propoxy unit
• m is greater than zero, typically between about 0.5 and about 6, more preferably between about 0.5 and about 3
• M is H or a cation which can be, for example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium, etc.), ammonium or substituted-ammonium cation.
• Alkyl ethoxylated sulfates as well as alkyl propoxylated sulfates are contemplated herein.
• substituted ammonium cations include methyl-, dimethyl, trimethyl-ammonium cations and quaternary ammonium cations such as tetramethyl-ammonium and dimethyl piperdinium cations and those derived from alkylamines such as ethylamine, 2 9
• Exemplary surfactants are C12-C18 a' polyethoxylate (1.0) sulfate (Ci2-Ci ⁇ E(1 0)M), C-12-C18 alkyl polyethoxylate (2.25) sulfate (Ci2-C ⁇ E(2.25)M), C12-C18 alkyl polyethoxylate (3.0) sulfate (C ⁇
• the laundry detergent and/or fabric care compositions of the present invention may also contain ampholytic, zwitterionic, and semi-polar surfactants, as well as the nonionic and/or anionic surfactants other than those already described herein.
• Ampholytic surfactants are also suitable for use in the laundry detergent and/or fabric care compositions of the present invention. These surfactants can be broadly described as aliphatic derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical can be straight- or branched-chain.
• One of the aliphatic substituents contains at least about 8 carbon atoms, typically from about 8 to about 18 carbon atoms, and at least one contains an anionic water-solubilizing group, e.g. carboxy, sulfonate, sulfate. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, lines 18-35, for examples of ampholytic surfactants.
• the laundry detergent and/or fabric care compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such ampholytic surfactants.
• Zwitterionic surfactants are also suitable for use in laundry detergent and/or fabric care compositions. These surfactants can be broadly described as derivatives of secondary and tertiary amines, derivatives of heterocyclic secondary and tertiary amines, or derivatives of quaternary ammonium, quaternary phosphonium or tertiary sulfonium compounds. See U.S. Patent No. 3,929,678 to Laughlin et al., issued December 30, 1975 at column 19, line 38 through column 22, line 48, for examples of zwitterionic surfactants. 30
• the laundry detergent and/or fabric care compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such zwitterionic surfactants.
• Semi-polar nonionic surfactants are a special category of nonionic surfactants which include water-soluble amine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and 2 moieties selected from the group consisting of alkyl groups and hydroxyalkyl groups containing from about 1 to about 3 carbon atoms; and water-soluble sulfoxides containing one alkyl moiety of from about 10 to about 18 carbon atoms and a moiety selected from the group consisting of alkyl and hydroxyalkyl moieties of from about 1 to about 3 carbon atoms.
• Semi-polar nonionic detergent surfactants include the amine oxide surfactants having the formula
• R 3 is an alkyl, hydroxyalkyl, or alkyl phenyl group or mixtures therof containing from about 8 to about 22 carbon atoms
• R 4 is an alkylene or hydroxyalkylene group containing from about 2 to about 3 carbon atoms or mixtures thereof
• x is from 0 to about 3
• each R5 is an alkyl or hydroxyalkyl group containing from about 1 to about 3 carbon atoms or a polyethylene oxide group containing from about 1 to about 3 ethylene oxide groups.
• the R5 groups can be attached to each other, e.g., through an oxygen or nitrogen atom, to form a ring structure.
• amine oxide surfactants in particular include C-
• the cleaning compositions of the present invention typically comprise from 0.2% to about 15%, preferably from about 1% to about 10% by weight of such semi-polar nonionic surfactants.
• the laundry detergent and/or fabric care composition of the present invention may further comprise a cosurfactant selected from the group of primary or tertiary amines.
• Suitable primary amines for use herein include amines according to the formula R-
• alkyl chains may be straight or branched and may be interrupted with up to 12, preferably less than 5 ethylene oxide moieties.
• Preferred amines according to the formula herein above are n-alkyl amines.
• Suitable amines for use herein may be selected from 1-hexylamine, 1- octylamine, 1-decylamine and laurylamine.
• Other preferred primary amines include C8-C10 oxypropylamine, octyloxypropylamine, 2-ethylhexyloxypropyl- amine, lauryl amido propylamine and amido propylamine.
• Suitable tertiary amines for use herein include tertiary amines having the formula R-
• R 3 is either a C ⁇ -C- ⁇ , preferably C ⁇ -C-io alkyl chain, or R 3 is R4X(CH2)n > whereby X is -0-, -C(0)NH- or -NH- R4 is a C4-C12, n is between 1 to 5, preferably 2-3.
• R5 is H or C-j-C ⁇ alkyl and x is between 1 to 6 .
• R 3 and R4 may be linear or branched ; R3 alkyl chains may be interrupted with up to 12, preferably less than 5, ethylene oxide moieties.
• Preferred tertiary amines are R-
• is C ⁇ -C-
• n is 2-4, preferably n is 3
• R2 and R 3 is C-1-C4
• Most preferred amines of the present invention include 1-octylamine, 1- hexylamine, 1-decylamine, 1-dodecylamine,C8-10oxypropylamine, N coco 1- 3diaminopropane, coconutalkyldimethylamine, lauryldimethylamine, lauryl bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles propoxylated, octyl amine 2 moles propoxylated, lauryl amidopropyl- dimethylamine, C8-10 amidopropyldimethylamine and C10 amidopropyl- dimethylamine.
• the most preferred amines for use in the compositions herein are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n- dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7 times ethoxylated, lauryl amido propylamine and cocoamido propylamine.
• the laundry detergent and/or fabric care compositions can in addition to the modified cellulase, further comprise one or more enzymes which provide cleaning performance and/or fabric care benefits.
• Said other enzymes include enzymes selected from cellulases without naturally occuring CBDs or with a having a relative binding constant (Kr-a) for binding to amorphous cellulose lower than 2.4l/gcellulose, hemicellulases, peroxidases, proteases, gluco-amylases, amylases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, ⁇ -glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase or mixtures thereof.
• Kr-a relative binding constant
• a preferred combination is a laundry detergent and/or fabric care composition having cocktail of conventional applicable enzymes like protease, amylase, lipase, cutinase and/or cellulase in conjunction with one or more plant cell wall degrading enzymes.
• Suitable proteases are the subtilisins which are obtained from particular strains of B. subtilis and B. licheniformis (subtilisin BPN and BPN').
• One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASE® by Novo Industries A/S of Denmark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1 ,243,784 to Novo.
• Other suitable proteases include ALCALASE®, DURAZYM® and SAVINASE® from Novo and MAXATASE®, MAXACAL®, PROPERASE® and MAXAPEM® (protein engineered Maxacal) from Gist-Brocades.
• Proteolytic enzymes also encompass modified bacterial serine proteases, such as those described in European Patent Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called "Protease A” herein.
• Protease C is a variant of an alkaline serine protease from Bacillus in which lysine replaced arginine at position 27, tyrosine replaced valine at position 104, serine replaced asparagine at position 123, and alanine replaced threonine at position 274.
• Protease C is described in EP 90915958:4, corresponding to WO 91/06637, Published May 16, 1991. Genetically modified variants, particularly of Protease C, are also included herein.
• a preferred protease referred to as "Protease D” is a carbonyl hydrolase variant having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a position in said carbonyl hydrolase equivalent to position +76, preferably also in combination with one or more amino acid residue positions equivalent to those selected from the group consisting of +99, +101 , +103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195, +197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274 according to the numbering of Bacillus amyloliquefaciens subtilisin, as described in WO95/10591 and in the patent application of C. Ghosh, et al, "Bleaching 34
• compositions Comprising Protease Enzymes having US Serial No. 08/322,677, filed October 13, 1994.
• a carbonyl hydrolase variant of the protease described in WO95/10591 having an amino acid sequence derived by replacement of a plurality of amino acid residues replaced in the precursor enzyme corresponding to position +210 in combination with one or more of the following residues : +33, +62, +67, +76, +100, +101 , +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, +218, and +222, where the numbered position corresponds to naturally- occurring subtilisin from Bacillus amyloliquefaciens or to equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin (co-pending patent application US Serial No. 60/048,
• proteases are multiply-substituted protease variants. These protease variants comprise a substitution of an amino acid residue with another naturally occurring amino acid residue at an amino acid residue position corresponding to position 103 of Bacillus amyloliquefaciens subtilisin in combination with a substitution of an amino acid residue positions corresponding to positions 1 , 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21 , 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61 , 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 101 , 102, 104, 106, 107, 109, 111 , 114, 116, 117, 119, 121 , 123, 126, 128, 130, 131 , 133, 134, 137, 140, 141 , 142, 146, 147, 158, 159, 160,
• proteases described in patent applications EP 251 446 and WO 91/06637, protease BLAP® described in
• Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO
• proteolytic enzymes are incorporated in the detergent compositions of the present invention a level of from 0.0001% to 2%, preferably from 0.001% to
• the cellulases without naturally occurring CBDs or with a having a relative binding constant (Kr-a) for binding to amorphous cellulose lower than 2.4l/gcellulose include both bacterial or fungal cellulases. Preferably, they will have a pH optimum of between 5 and 12 and an activity above 50 CEVU (Cellulose Viscosity Unit).
• Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al, J61078384 and WO96/02653 which discloses fungal cellulase produced respectively from Humicola insolens, Trichoderma, Thielavia and Sporotrichum.
• EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable cellulases are also disclosed in GB-A- 2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and W095/26398.
• cellulases examples include cellulases produced by a strain of Humicola insolens (Humicola grisea var. thermoidea), particularly the Humicola strain DSM 1800.
• suitable cellulases are cellulases originated from Humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a " 43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in PCT Patent Application 36
• suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum described in WO94/21801 , Genencor, published September 29, 1994.
• Especially suitable cellulases are the cellulases having color care benefits. Examples of such cellulases are cellulases described in European patent application No. 91202879.2, filed November 6, 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A/S) are especially useful. See also W091/17244 and WO91/21801.
• Other suitable cellulases for fabric care and/or cleaning properties are described in WO96/34092, W096/17994 and W095/24471.
• Said cellulases are normally incorporated in the detergent composition at levels from 0.0001 % to 2% of pure enzyme by weight of the detergent composition.
• Peroxidase enzymes are used in combination with oxygen sources, e.g. percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a phenolic substrate as bleach enhancing molecule. They are used for "solution bleaching", i.e. to prevent transfer of dyes or pigments removed from substrates during wash operations to other substrates in the wash solution.
• Peroxidase enzymes are known in the art, and include, for example, horseradish peroxidase, ligninase and haloperoxidase such as chloro- and bromo-peroxidase.
• Peroxidase- containing detergent compositions are disclosed, for example, in PCT International Application WO 89/099813, WO89/09813 and in European Patent application EP No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme. Enhancers are generally comprised at a level of from 0.1% to 5% by weight of total composition.
• Preferred enhancers are substituted phenthiazine and phenoxasine 10-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4- carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10- methylphenoxazine (described in WO 94/12621) and substituted syringates (C3- C5 substituted alkyl syringates) and phenols.
• Sodium percarbonate or perborate are preferred sources of hydrogen peroxide.
• Said peroxidases are normally incorporated in the detergent composition at levels from 0.0001% to 2% of pure enzyme by weight of the detergent composition.
• lipases Other enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for detergent usage 37
• Suitable lipases include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1 ,372,034.
• Suitable lipases include those which show a positive immunological cross- reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano,” hereinafter referred to as "Amano-P".
• Other suitable commercial lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var.
• lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli.
• lipases such as M1 Lipase ⁇ an( ⁇ LipomaxR (Gist-Brocades) and Lipolase ⁇ and Lipolase Ultra ⁇ (Novo) which have found to be very effective when used in combination with the compositions of the present invention.
• lipolytic enzymes described in EP 258 068, WO 92/05249 and WO 95/22615 by Novo Nordisk and in WO 94/03578, WO 95/35381 and WO 96/00292 by Unilever.
• cutinases [EC 3.1.1.50] which can be considered as a special kind of lipase, namely lipases which do not require interfacial activation. Addition of cutinases to detergent compositions have been described in e.g. WO-A- 88/09367 (Genencor); WO 90/09446 (Plant Genetic System) and WO 94/14963 and WO 94/14964 (Unilever).
• the lipases and/or cutinases are normally incorporated in the detergent composition at levels from 0.0001% to 2% of pure enzyme by weight of the detergent composition.
• Amylases can be included for removal of carbohydrate-based stains.
• WO94/02597 Novo Nordisk A/S published February 03, 1994, describes cleaning compositions which incorporate mutant amylases. See also WO95/10603, Novo Nordisk A/S, published April 20, 1995.
• Other amylases known for use in cleaning compositions include both ⁇ - and ⁇ -amylases.
• ⁇ - Amylases are known in the art and include those disclosed in US Pat. no. 5,003,257; EP 252,666; WO/91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341 ; and British Patent specification no. 1 ,296,839 (Novo).
• Other suitable amylases are stability-enhanced amylases described in W094/18314, published August 18, 1994 and WO96/05295, Genencor, published February 38
• amylase variants having additional modification in the immediate parent available from Novo Nordisk A/S, disclosed in WO 95/10603, published April 95. Also suitable are amylases described in EP 277 216, W095/26397 and W096/23873 (all by Novo Nordisk).
• ⁇ -amylases examples are Purafect Ox Am® from Genencor and Termamyl®, Ban® .Fungamyl® and Duramyl®, all available from Novo Nordisk A/S Denmark.
• W095/26397 describes other suitable amylases : ⁇ -amylases characterised by having a specific activity at least 25% higher than the specific activity of Termamyl® at a temperature range of 25°C to 55°C and at a pH value in the range of 8 to 10, measured by the Phadebas® ⁇ -amylase activity assay. Suitable are variants of the above enzymes, described in W096/23873 (Novo Nordisk).
• amylolytic enzymes with improved properties with respect to the activity level and the combination of thermostability and a higher activity level are described in W095/35382.
• the amylolytic enzymes are incorporated in the detergent compositions of the present invention a level of from 0.0001% to 2%, preferably from 0.00018% to 0.06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition.
• the above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Also included by definition, are mutants of native enzymes. Mutants can be obtained e.g. by protein and/or genetic engineering, chemical and/or physical modifications of native enzymes. Common practice as well is the expression of the enzyme via host organisms in which the genetic material responsible for the production of the enzyme has been cloned.
• Said enzymes are normally incorporated in the detergent composition at levels from 0.0001% to 2% of pure enzyme by weight of the detergent composition.
• the enzymes can be added as separate single ingredients (prills, granulates, stabilized liquids, etc. containing one enzyme ) or as mixtures of two or more enzymes ( e.g. cogranulates ).
• enzyme oxidation scavengers which are described in Copending European Patent application 92870018.6 filed on January 31 , 1992.
• enzyme oxidation scavengers are ethoxylated tetraethylene polyamines.
• a range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 A and WO 9307260 A to Genencor International, WO 8908694 A to Novo, and U.S. 3,553,139, January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S. 4,101 ,457, Place et al, July 18, 1978, and in U.S. 4,507,219, Hughes, March 26, 1985. Enzyme materials useful for liquid detergent formulations, and their incorporation into such formulations, are disclosed in U.S. 4,261 ,868, Hora et al, April 14, 1981. Enzymes for use in detergents can be stabilised by various techniques.
• Enzyme stabilisation techniques are disclosed and exemplified in U.S. 3,600,319, August 17, 1971 , Gedge et al, EP 199,405 and EP 200,586, October 29, 1986, Venegas. Enzyme stabilisation systems are also described, for example, in U.S. 3,519,570. A useful Bacillus, sp. AC13 giving proteases, xylanases and cellulases, is described in WO 9401532 A to Novo.
• Fabric softening agents can also be incorporated into laundry detergent and/or fabric care compositions in accordance with the present invention. These agents may be inorganic or organic in type. Inorganic softening agents are exemplified by the smectite clays disclosed in GB-A-1 400 898 and in USP 5,019,292. Organic fabric softening agents include the water insoluble tertiary amines as disclosed in GB-A1 514 276 and EP-B0 011 340 and their combination with 40
• Preferred fabric softening agent for the purpose of the present invention is a smectite clay. It has been surprisingly found that the laundry detergent and/or fabric care compositions of the present invention further comprising a smectite clay, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour appearance and fabric anti-wear properties and benefits while preventing tensile strength loss.
• Levels of smectite clay are normally in the range from 2% to 20%, more preferably from 5% to 15% by weight, with the material being added as a dry mixed component to the remainder of the formulation.
• Organic fabric softening agents such as the water-insoluble tertiary amines or dilong chain amide materials are incorporated at levels of from 0.5% to 5% by weight, normally from 1 % to 3% by weight whilst the high molecular weight polyethylene oxide materials and the water soluble cationic materials are added at levels of from 0.1% to 2%, normally from 0.15% to 1.5% by weight.
• These materials are normally added to the spray dried portion of the composition, although in some instances it may be more convenient to add them as a dry mixed particulate, or spray them as molten liquid on to other solid components of the composition.
• laundry detergent and/or fabric care compositions of the present invention include bleaching agents.
• Bleaching agents include hydrogen peroxide, PB1 , PB4 and percarbonate with a particle size of 400-800 microns. These bleaching agent components can include one or more oxygen bleaching agents and, depending upon the bleaching agent chosen, one or more bleach activators. When present oxygen bleaching compounds will typically be present at levels of from about 1% to about 25%. 4 1
• the bleaching agent component for use herein can be any of the bleaching agents useful for cleaning compositions including oxygen bleaches as well as others known in the art.
• the bleaching agent suitable for the present invention can be an activated or non-activated bleaching agent.
• oxygen bleaching agent that can be used encompasses percarboxylic acid bleaching agents and salts thereof. Suitable examples of this class of agents include magnesium monoperoxyphthalate hexahydrate, the magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino-4- oxoperoxybutyric acid and diperoxydodecanedioic acid.
• Such bleaching agents are disclosed in U.S. Patent 4,483,781 , U.S. Patent Application 740,446, European Patent Application 0,133,354 and U.S. Patent 4,412,934.
• Highly preferred bleaching agents also include 6-nonylamino-6-oxoperoxycaproic acid as described in U.S. Patent 4,634,551.
• bleaching agents that can be used encompasses the halogen bleaching agents.
• hypohalite bleaching agents include trichloro isocyanuric acid and the sodium and potassium dichloroisocyanurates and N-chloro and N-bromo alkane sulphonamides. Such materials are normally added at 0.5-10% by weight of the finished product, preferably 1-5% by weight.
• the hydrogen peroxide releasing agents can be used in combination with bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene- sulfonate (NOBS, described in US 4,412,934), 3,5,- trimethylhexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6- aminocaproic acid (NACA-OBS, described in WO94/28106), which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect.
• bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene- sulfonate (NOBS, described in US 4,412,934), 3,5,- trimethylhexanoloxybenzenesulf
• bleaching agents including peroxyacids and bleaching systems comprising bleach activators and peroxygen bleaching compounds for use in detergent compositions according to the invention are described in our co- 42
• the hydrogen peroxide may also be present by adding an enzymatic system (i.e., an enzyme and a substrate therefore) which is capable of generating hydrogen peroxide at the beginning or during the washing and/or rinsing process.
• an enzymatic system i.e., an enzyme and a substrate therefore
• Such enzymatic systems are disclosed in EP Patent Application 91202655.6 filed October 9, 1991.
• Metal-containing catalysts for use in bleach compositions include cobalt- containing catalysts such as Pentaamine acetate cobalt(lll) salts and manganese-containing catalysts such as those described in EPA 549 271 ; EPA 549 272; EPA 458 397; US 5,246,621 ; EPA 458 398; US 5,194,416 and US 5,114,611.
• Bleaching composition comprising a peroxy compound, a manganese-containing bleach catalyst and a chelating agent is described in the patent application No 94870206.3.
• Bleaching agents other than oxygen bleaching agents are also known in the art and can be utilized herein.
• One type of non-oxygen bleaching agent of particular interest includes photoactivated bleaching agents such as the sulfonated zinc and/or aluminum phthalocyanines. These materials can be deposited upon the substrate during the washing process. Upon irradiation with light, in the presence of oxygen, such as by hanging clothes out to dry in the daylight, the sulfonated zinc phthalocyanine is activated and, consequently, the substrate is bleached.
• Preferred zinc phthalocyanine and a photoactivated bleaching process are described in U.S. Patent 4,033,718.
• detergent compositions will contain about 0.025% to about 1.25%, by weight, of sulfonated zinc phthalocyanine.
• compositions according to the present invention may further comprise a builder system. It has been surprisingly found that said laundry detergent and/or fabric care compositions further comprising a builder, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties to fabrics, as well as provide enhanced static control, fabric softness, colour 43
• Preferred builders are zeolite A and sodium tripolyphosphate.
• Any conventional builder system is suitable for use herein including aluminosilicate materials, silicates, polycarboxylates, alkyl- or alkenyl-succinic acid and fatty acids, materials such as ethylenediamine tetraacetate, diethylene triamine pentamethyleneacetate, metal ion sequestrants such as aminopoly- phosphonates, particularly ethylenediamine tetramethylene phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
• Phosphate builders can also be used herein.
• Suitable builders can be an inorganic ion exchange material, commonly an inorganic hydrated aluminosilicate material, more particularly a hydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.
• Another suitable inorganic builder material is layered silicate, e.g. SKS-6
• SKS-6 is a crystalline layered silicate consisting of sodium silicate (Na 2 Si 2 0 5 ).
• Suitable polycarboxylates containing one carboxy group include lactic acid, glycolic acid and ether derivatives thereof as disclosed in Belgian Patent Nos. 831 ,368, 821 ,369 and 821 ,370.
• Polycarboxylates containing two carboxy groups include the water-soluble salts of succinic acid, malonic acid, (ethylenedioxy) diacetic acid, maleic acid, diglycollic acid, tartaric acid, tartronic acid and fumaric acid, as well as the ether carboxylates described in German Offenlegenschrift 2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and the sulfinyl carboxylates described in Belgian Patent No. 840,623.
• Polycarboxylates containing three carboxy groups include, in particular, water-soluble citrates, aconitrates and citraconates as well as succinate derivatives such as the carboxymethyloxysuccinates described in British Patent No. 1 ,379,241 , lactoxysuccinates described in Netherlands Application 7205873, and the oxypolycarboxylate materials such as 2-oxa-1 ,1 ,3-propane tricarboxylates described in British Patent No. 1 ,387,447.
• Polycarboxylates containing four carboxy groups include oxydisuccinates disclosed in British Patent No. 1 ,261 ,829, 1 ,1 ,2,2-ethane tetracarboxylates, 1 ,1 ,3,3-propane tetracarboxylates and 1 ,1 ,2,3-propane tetracarboxylates. 44
• Polycarboxylates containing sulfo substituents include the sulfosuccinate derivatives disclosed in British Patent Nos. 1 ,398,421 and 1 ,398,422 and in U.S. Patent No. 3,936,448, and the sulfonated pyrolysed citrates described in British Patent No. 1 ,082,179, while polycarboxylates containing phosphone substituents are disclosed in British Patent No. 1 ,439,000.
• Alicyclic and heterocyclic polycarboxylates include cyclopentane-cis,cis,cis- tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-tetrahydro-furan - cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan -cis - dicarboxylates, 2,2,5,5-tetrahydrofuran - tetracarboxylates, 1 ,2,3,4,5,6-hexane -hexa- carboxylates and and carboxymethyl derivatives of polyhydric alcohols such as sorbitol, mannitol and xylitol.
• Aromatic poly-carboxylates include mellitic acid, pyromellitic acid and the phthalic acid derivatives disclosed in British Patent No. 1 ,425,343.
• the preferred polycarboxylates are hydroxycarboxylates containing up to three carboxy groups per molecule, more particularly citrates.
• Preferred builder systems for use in the present compositions include a mixture of a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6), and a water-soluble carboxylate chelating agent such as citric acid.
• a water-insoluble aluminosilicate builder such as zeolite A or of a layered silicate (SKS-6)
• a water-soluble carboxylate chelating agent such as citric acid.
• Preferred builder systems include a mixture of a water-insoluble aluminosilicate builder such as zeolite A, and a watersoluble carboxylate chelating agent such as citric acid.
• Preferred builder systems for use in liquid detergent compositions of the present invention are soaps and polycarboxylates.
• Suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms. 45
• Polymers of this type are disclosed in GB-A-1 ,596,756.
• Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 20,000 to 70,000, especially about 40,000.
• Detergency builder salts are normally included in amounts of from 5% to 80% by weight of the composition preferably from 10% to 70% and most usually from 30% to 60% by weight.
• the laundry detergent and/or fabric care compositions herein may also optionally contain one or more iron and/or manganese chelating agents.
• chelating agents can be selected from the group consisting of amino carboxylates, amino phosphonates, polyfunctionally-substituted aromatic chelating agents and mixtures therein, all as hereinafter defined. Without intending to be bound by theory, it is believed that the benefit of these materials is due in part to their exceptional ability to remove iron and manganese ions from washing solutions by formation of soluble chelates.
• Amino carboxylates useful as optional chelating agents include ethylenediaminetetracetates, N-hydroxyethylethylenediaminetriacetates, nitrilo- triacetates, ethylenediamine tetraproprionates, triethylenetetraamine- hexacetates, diethylenetriaminepentaacetates, and ethanoldiglycines, alkali metal, ammonium, and substituted ammonium salts therein and mixtures therein.
• Amino phosphonates are also suitable for use as chelating agents in the compositions of the invention when at lease low levels of total phosphorus are permitted in detergent compositions, and include ethylenediaminetetrakis (methylenephosphonates) as DEQUEST. Preferred, these amino phosphonates do not contain alkyl or alkenyl groups with more than about 6 carbon atoms.
• Polyfunctionally-substituted aromatic chelating agents are also useful in the compositions herein. See U.S. Patent 3,812,044, issued May 21 , 1974, to Connor et al.
• Preferred compounds of this type in acid form are dihydroxydisulfobenzenes such as 1 ,2-dihydroxy-3,5-disulfobenzene. 4 6
• EDDS ethylenediamine disuccinate
• [S,S] isomer as described in U.S. Patent 4,704,233, November 3, 1987, to Hartman and Perkins.
• compositions herein may also contain water-soluble methyl glycine diacetic acid (MGDA) salts (or acid form) as a chelant or co-builder useful with, for example, insoluble builders such as zeolites, layered silicates and the like.
• MGDA water-soluble methyl glycine diacetic acid
• these chelating agents will generally comprise from about 0.1% to about 15% by weight of the detergent compositions herein. More preferably, if utilized, the chelating agents will comprise from about 0.1 % to about 3.0% by weight of such compositions.
• a suds suppressor exemplified by silicones, and silica-silicone mixtures.
• Silicones can be generally represented by alkylated polysiloxane materials while silica is normally used in finely divided forms exemplified by silica aerogels and xerogels and hydrophobic silicas of various types. These materials can be incorporated as particulates in which the suds suppressor is advantageously releasably incorporated in a water-soluble or water-dispersible, substantially non-surface-active detergent impermeable carrier.
• the suds suppressor can be dissolved or dispersed in a liquid carrier and applied by spraying on to one or more of the other components.
• a preferred silicone suds controlling agent is disclosed in Bartollota et al. U.S. Patent 3 933 672.
• Other particularly useful suds suppressors are the self- emulsifying silicone suds suppressors, described in German Patent Application DTOS 2 646 126 published April 28, 1977.
• An example of such a compound is DC-544, commercially available from Dow Corning, which is a siloxane-glycol copolymer.
• Especially preferred suds controlling agent are the suds suppressor system comprising a mixture of silicone oils and 2-alkyl-alcanols.
• Suitable 2- alkyl-alkanols are 2-butyl-octanol which are commercially available under the trade name Isofol 12 R. 4 7
• compositions can comprise a silicone/silica mixture in combination with fumed nonporous silica such as
• Aerosil .
• the suds suppressors described above are normally employed at levels of from 0.001% to 2% by weight of the composition, preferably from 0.01% to 1 % by weight.
• compositions such as soil-suspending agents, soil-release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or non-encapsulated perfumes may be employed.
• encapsulating materials are water soluble capsules which consist of a matrix of polysaccharide and polyhydroxy compounds such as described in GB 1 ,464,616.
• Suitable water soluble encapsulating materials comprise dextrins derived from ungelatinized starch acid-esters of substituted dicarboxylic acids such as described in US 3,455,838. These acid-ester dextrins are,preferably, prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and potato. Suitable examples of said encapsulating materials include N-Lok manufactured by National Starch. The N-Lok encapsulating material consists of a modified maize starch and glucose. The starch is modified by adding monofunctional substituted groups such as octenyl succinic acid anhydride.
• Antiredeposifion and soil suspension agents suitable herein include cellulose derivatives such as methylcellulose, carboxymethylcellulose and hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their salts.
• Polymers of this type include the polyacrylates and maleic anhydride- acrylic acid copolymers previously mentioned as builders, as well as copolymers of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the 4 8
• maleic anhydride constituting at least 20 mole percent of the copolymer.
• These materials are normally used at levels of from 0.5% to 10% by weight, more preferably from 0.75% to 8%, most preferably from 1 % to 6% by weight of the composition.
• Preferred optical brighteners are anionic in character, examples of which are disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-2:2' disulphonate, disodium 4, - 4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino- stilbene-2:2' - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin-6- ylamino)stilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-tri- azin-6 ylamino)stilbene-2-sulphonate, disodium 4,4' -bis-(2-anilino-4-(N-methyl- N-2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2'
• polyethylene glycols particulariy those of molecular weight 1000-10000, more particularly 2000 to 8000 and most preferably about 4000. These are used at levels of from 0.20% to 5% more preferably from 0.25% to 2.5% by weight. These polymers and the previously mentioned homo- or co-polymeric polycarboxylate salts are valuable for improving whiteness maintenance, fabric ash deposition, and cleaning performance on clay, proteinaceous and oxidizable soils in the presence of transition metal impurities.
• Soil release agents useful in compositions of the present invention are conventionally copolymers or terpolymers of terephthalic acid with ethylene glycol and/or propylene glycol units in various arrangements. Examples of such polymers are disclosed in the commonly assigned US Patent Nos. 4116885 and 4711730 and European Published Patent Application No. 0 272 033. A particular preferred polymer in accordance with EP-A-0 272 033 has the formula 4 9
• PEG is -(OC2H4)0-,PO is (OC 3 HeO) and T is (pcOC ⁇ CO).
• modified polyesters as random copolymers of dimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2 propane diol, the end groups consisting primarily of sulphobenzoate and secondarily of mono esters of ethylene glycol and/or propane-diol.
• the target is to obtain a polymer capped at both end by sulphobenzoate groups, "primarily", in the present context most of said copolymers herein will be end-capped by sulphobenzoate groups.
• some copolymers will be less than fully capped, and therefore their end groups may consist of monoester of ethylene glycol and/or propane 1- 2 diol, thereof consist “secondarily” of such species.
• the selected polyesters herein contain about 46% by weight of dimethyl terephthalic acid, about 16% by weight of propane -1.2 diol, about 10% by weight ethylene glycol about 13% by weight of dimethyl sulfobenzoic acid and about 15% by weight of sulfoisophthalic acid, and have a molecular weight of about 3.000.
• the polyesters and their method of preparation are described in detail in EPA 311 342.
• chlorine scavenger such as perborate, ammonium sulfate, sodium sulphite or polyethyleneimine at a level above 0.1 % by weight of total composition, in the formulas will provide improved through the wash stability of the detergent enzymes.
• Compositions comprising chlorine scavenger are described in the European patent application 92870018.6 filed January 31 , 1992.
• Alkoxylated polycarboxylates such as those prepared from polyacrylates are useful herein to provide additional grease removal performance. Such materials are described in WO 91/08281 and PCT 90/01815 at p. 4 et seq., incorporated herein by reference. Chemically, these materials comprise polyacrylates having one ethoxy side-chain per every 7-8 acrylate units.
• the side-chains are of the formula -(CH2CH2 ⁇ ) m (CH2) n CH 3 wherein m is 2-3 and n is 6-12.
• alkoxylated polycarboxylates can comprise from about 0.05% to about 10%, by weight, of the compositions herein.
• the laundry detergent and/or fabric care composition of the present invention can also contain dispersants :
• Suitable water-soluble organic salts are the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
• Polymers of this type are disclosed in GB-A- 1 ,596, 756.
• Examples of such salts are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride, such copolymers having a molecular weight of from 1 ,000 to 100,000.
• copolymer of acrylate and methylacrylate such as the 480N having a molecular weight of 4000, at a level from 0.5-20% by weight of composition can be added in the laundry detergent and/or fabric care compositions of the present invention.
• compositions of the invention may contain a lime soap peptiser compound, which has preferably a lime soap dispersing power (LSDP), as defined hereinafter of no more than 8, preferably no more than 7, most preferably no more than 6.
• LSDP lime soap dispersing power
• the lime soap peptiser compound is preferably present at a level from 0% to 20% by weight.
• LSDP lime soap dispersant power
• the LSDP is the % weight ratio of dispersing agent to sodium oleate required to disperse the lime soap deposits formed by 0.025g of sodium oleate in 30ml of water of 333ppm CaCo 3
• Surfactants having good lime soap peptiser capability will include certain amine oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated alcohols.
• Exemplary surfactants having a LSDP of no more than 8 for use in accord with the present invention include C-
• Polymeric lime soap peptisers suitable for use herein are described in the article by M.K. Nagarajan, W.F. Masler, to be found in Cosmetics and Toiletries, volume 104, pages 71-73, (1989).
• Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulfonate, 4-[N-decanoyI-6- aminohexanoyrjbenzene sulfonate and mixtures thereof; and nonanoyloxy benzene sulfonate together with hydrophilic / hydrophobic bleach formulations can also be used as lime soap peptisers compounds.
• the laundry detergent and/or fabric care compositions of the present invention can preferably include compounds for inhibiting dye transfer from one fabric to another of solubilized and suspended dyes encountered during fabric laundering operations involving colored fabrics. It has been surprisingly found that the laundry detergent and/or fabric care compositions of the present invention further comprising a dye transfer inhibition polymer, achieve improved fabric care, including improved anti-wrinkle, anti-bobbling and anti-shrinkage properties 52
• the laundry detergent and/or fabric care compositions according to the present invention may also comprise from 0.001 % to 10 %, preferably from 0.01% to 2%, more preferably from 0.05% to 1% by weight of polymeric dye transfer inhibiting agents.
• Said polymeric dye transfer inhibiting agents are normally incorporated into cleaning compositions in order to inhibit the transfer of dyes from colored fabrics onto fabrics washed therewith. These polymers have the ability to complex or adsorb the fugitive dyes washed out of dyed fabrics before the dyes have the opportunity to become attached to other articles in the wash.
• polymeric dye transfer inhibiting agents are polyamine N- oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole, polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
• polyamine N-oxide polymers suitable for use contain units having the following structure formula :
• P is a polymerisable unit, whereto the R-N-0 group can be attached to or wherein the R-N-0 group forms part of the polymerisable unit or a combination of both.
• A is NC, CO, C, -0-,-S-, -N- ; x is O or 1 ;
• R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclic or alicyclic groups or any combination thereof whereto the nitrogen of the N-0 group can be attached or wherein the nitrogen of the N-0 group is part of these groups.
• the N-0 group can be represented by the following general structures :
• R1 , R2, and R3 are aliphatic groups, aromatic, heterocyclic or alicyclic groups or combinations thereof, x or/and y or/and z is 0 or 1 and wherein the nitrogen of the N-0 group can be attached or wherein the nitrogen of the N-0 group forms part of these groups.
• the N-0 group can be part of the polymerisable unit (P) or can be attached to the polymeric backbone or a combination of both.
• Suitable polyamine N-oxides wherein the N-0 group forms part of the polymerisable unit comprise polyamine N-oxides wherein R is selected from aliphatic, aromatic, alicyclic or heterocyclic groups.
• One class of said polyamine N-oxides comprises the group of polyamine N- oxides wherein the nitrogen of the N-0 group forms part of the R-group.
• Preferred polyamine N-oxides are those wherein R is a heterocyclic group such as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and derivatives thereof.
• Another class of said polyamine N-oxides comprises the group of polyamine N- oxides wherein the nitrogen of the N-0 group is attached to the R-group.
• polyamine N-oxides are the polyamine oxides whereto the N-0 group is attached to the polymerisable unit. 54
• Preferred class of these polyamine N-oxides are the polyamine N-oxides having the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the N-0 functional group is part of said R group.
• examples of these classes are polyamine oxides wherein R is a heterocyclic compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
• Another preferred class of polyamine N-oxides are the polyamine oxides having the general formula (I) wherein R are aromatic, heterocyclic or alicyclic groups wherein the nitrogen of the N-0 functional group is attached to said R groups. Examples of these classes are polyamine oxides wherein R groups can be aromatic such as phenyl.
• Any polymer backbone can be used as long as the amine oxide polymer formed is water-soluble and has dye transfer inhibiting properties.
• suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters, polyethers, polyamide, polyimides, polyacrylates and mixtures thereof.
• the amine N-oxide polymers of the present invention typically have a ratio of amine to the amine N-oxide of 10:1 to 1 :1000000.
• the amount of amine oxide groups present in the polyamine oxide polymer can be varied by appropriate copolymerization or by appropriate degree of N-oxidation.
• the ratio of amine to amine N-oxide is from 2:3 to 1 :1000000. More preferably from 1 :4 to 1 :1000000, most preferably from 1 :7 to 1 :1000000.
• the polymers of the present invention actually encompass random or block copolymers where one monomer type is an amine N-oxide and the other monomer type is either an amine N-oxide or not.
• the amine oxide unit of the polyamine N-oxides has a PKa ⁇ 10, preferably PKa ⁇ 7, more preferred PKa ⁇ 6.
• the polyamine oxides can be obtained in almost any degree of polymerisation.
• the degree of polymerisation is not critical provided the material has the desired water-solubility and dye-suspending power.
• the average molecular weight is within the range of 500 to 1000,000; preferably from 1 ,000 to 50,000, more preferably from 2,000 to 30,000, most preferably from 3,000 to 20,000.
• N-vinylimidazole N-vinylpyrrolidone polymers used in the present invention have an average molecular weight range from 5,000-1 ,000,000, preferably from
• Highly preferred polymers for use in detergent compositions according to the present invention comprise a polymer selected from N-vinylimidazole N- vinylpyrrolidone copolymers wherein said polymer has an average molecular weight range from 5,000 to 50,000 more preferably from 8,000 to 30,000, most preferably from 10,000 to 20,000.
• the average molecular weight range was determined by light scattering as described in Barth H.G. and Mays J.W. Chemical Analysis Vol 113, "Modern
• N-vinylimidazole N-vinylpyrrolidone copolymers have an average molecular weight range from 5,000 to 50,000; more preferably from
• N-vinylimidazole N-vinylpyrrolidone copolymers characterized by having said average molecular weight range provide excellent dye transfer inhibiting properties while not adversely affecting the cleaning performance of detergent compositions formulated therewith.
• the N-vinylimidazole N-vinylpyrrolidone copolymer of the present invention has a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to 0.2, more preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4 .
• the detergent compositions of the present invention may also utilize polyvinylpyrrolidone ("PVP") having an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000.
• PVP polyvinylpyrrolidone
• Suitable polyvinylpyrrolidones are commercially vailable from ISP Corporation, New York, NY and Montreal, Canada under the product names PVP K-15 (viscosity molecular weight of 10,000), PVP K-30 (average molecular weight of 40,000), PVP K-60 (average molecular weight of 160,000), and PVP K-90 (average molecular weight of 360,000).
• PVP K-15 viscosity molecular weight of 10,000
• PVP K-30 average molecular weight of 40,000
• PVP K-60 average molecular weight of 160,000
• PVP K-90 average molecular weight of 360,000.
• the detergent compositions of the present invention may also utilize polyvinyloxazolidone as a polymeric dye transfer inhibiting agent.
• Said polyvinyloxazolidones have an average molecular weight of from about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000.
• the detergent compositions of the present invention may also utilize polyvinylimidazole as polymeric dye transfer inhibiting agent.
• Said polyvinylimidazoles have an average of about 2,500 to about 400,000, preferably from about 5,000 to about 200,000, more preferably from about 5,000 to about 50,000, and most preferably from about 5,000 to about 15,000.
• Cross-linked polymers are polymers whose backbone are interconnected to a certain degree; these links can be of chemical or physical nature, possibly with active groups n the backbone or on branches; cross-linked polymers have been described in the Journal of Polymer Science, volume 22, pages 1035-1039.
• the cross-linked polymers are made in such a way that they form a three-dimensional rigid structure, which can entrap dyes in the pores formed by the three-dimensional structure.
• the cross- linked polymers entrap the dyes by swelling.
• compositions of the invention may be used in essentially any washing, cleaning and/or fabric care methods, including soaking methods, pre-treatment methods, methods with rinsing steps for which a separate rinse aid composition may be added and post-treatment methods.
• the process described herein comprises contacting fabrics with a laundering solution in the usual manner and exemplified hereunder.
• a conventional laundry method comprises treating soiled fabric with an aqueous liquid having dissolved or dispensed therein an effective amount of the laundry detergent and/or fabric care composition.
• the process of the invention is conveniently carried out in the course of the cleaning process.
• the method of cleaning is preferably carried out at 5°C to 95°C, especially between 10°C and 60°C.
• the pH of the treatment solution is preferably from 7 to 12.
• the enzymes levels are expressed by pure enzyme by weight of the total composition and unless otherwise specified, the detergent ingredients are expressed by weight of the total compositions.
• the abbreviated component identifications therein have the following meanings:
• LAS Sodium linear C-j ⁇ _ ⁇ alkyl benzene sulphonate.
• TAS Sodium tallow alkyl sulphate.
• CxyAS Sodium C-
• CxySAS Sodium C «
• CxyEz C-
• CxyEzS C-
• DTDMAMS Ditalllow dimethyl ammonium methylsulfate. SDASA 1 :2 ratio of stearyldimethyl amine:triple-pressed stearic acid.
• Zeolite A Hydrated Sodium Aluminosilicate of formula Na-
• Citric Anhydrous citric acid Citric Anhydrous citric acid.
• Carbonate Anhydrous sodium carbonate with a particle size between 200 and 900 micrometres.
• Bicarbonate Anhydrous sodium hydrogen carbonate with a particle size distribution between 400 and 1200 micrometres.
• Percarbonate Anhydrous sodium percarbonate of nominal formula 2Na2C0 3 .3H 2 0 2 .
• TAED Tetraacetylethylenediamine.
• NOBS Nonanoyloxybenzene sulfonate in the form of the sodium salt.
• NACA-OBS (6-nonamidocaproyl) oxybenzene sulfonate.
• DTPA Diethylene triamine pentaacetic acid.
• Photoactivated Sulfonated alumino phtalocyanine encapsulated in Bleach 1 dextrin soluble polymer Protease Proteolytic enzyme sold under the tradename Savinase,
• Lipase Lipolytic enzyme sold under the tradename Lipolase
• CBD-Cellulase Cellulytic enzyme core derived from the enzyme sold under the tradename Carezyme by Novo Nordisk A/S linked to the CBD of the CenC cellulase of Cellulomonas fimi, either the tandem CBDN1 N2 or the single CBDN1 or CBDN2 and/or linked to the CBD from the cellulase
• Cellulytic enzyme core derived from the enzyme sold under the tradename Carezyme by Novo Nordisk A/S linked by the Humicola Insolens family 45 cellulase linker to the CBD of the CenC cellulase of Cellulomonas fimi, either the tandem CBDN1 N2 or the single CBDN1 or
• CBDN2 and/or
• PVNO Polyvinylpyridine-N-Oxide with an average molecular weight of 50,000.
• PVPVI Copolymer of vinylimidazole and vinylpyrrolidone with an average molecular weight of 20,000.
• Brightener 1 Disodium 4,4'-bis(2-sulphostyryl)biphenyl.
• Brightener 2 Disodium 4,4'-bis(4-anilino-6-morpholino-1.3.5-triazin-2- yl) stilbene-2:2'-disulfonate.
• Opacifier Water based monostyrene latex mixture, sold by BASF
• SRP 1 Anionically end capped poly esters.
• SRP 2 Diethoxylated poly (1 ,2 propylene terephtalate) short block polymer.
• HMWPEO High molecular weight polyethylene oxide.
• PEGx Polyethylene glycol of a molecular weight of x .
• PEO Polyethylene oxide with an average molecular weight of
• Brightener 1 0.09 0.09 0.09 - 0.09 0.09
• Brightener 1 0.08 0.2 - - 0.09 0.15
• Brightener 1 0.2 0.2 0.2 0.2 0.2
• Brightener 1 0.05 - - 0.05
• Zeolite A 10.0 18.0 14.0 12.0 10.0 10.0
• Brightener 2 0.3 0.2 0.3 - 0.1 0.3
• Brightener 1 0.2 0.2 0.2 0.2 0.2
• Zeolite A 15.0 15.0 15.0
• Photoactivated bleach 30 ppm 20 ppm - 10 ppm
• liquid detergent formulations were prepared according to the present invention (Levels are given in parts per weight) :
• liquid detergent formulations were prepared according to the present invention (Levels are given in parts per weight) :
• liquid detergent formulafions were prepared according to the present invenfion (Levels are given in parts per weight) :
• Rapeseed fatty acid 1.0 - 3.5 -
• Brightener 1 0.1 0.2 0.3 -
• liquid detergent compositions were prepared according to the present invention (Levels are given in parts by weight) :

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• 1998
  • 1998-05-01 WO PCT/US1998/008904 patent/WO1999057257A1/en not_active Application Discontinuation
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