Source: https://patents.google.com/patent/US6204234
Timestamp: 2018-03-23 09:26:42
Document Index: 610565557

Matched Legal Cases: ['application No. 91202879', 'Application No. 91870207', 'Application No. 92870181', 'Application No. 96870140', 'in fine', 'application No. 95201943']

US6204234B1 - Cleaning compositions comprising a specific oxygenase - Google Patents
Cleaning compositions comprising a specific oxygenase Download PDF
US6204234B1
US6204234B1 US09462560 US46256000A US6204234B1 US 6204234 B1 US6204234 B1 US 6204234B1 US 09462560 US09462560 US 09462560 US 46256000 A US46256000 A US 46256000A US 6204234 B1 US6204234 B1 US 6204234B1
US09462560
The present invention relates to cleaning compositions, including laundry, dishwashing, hard surface cleaner, oral/dental cleaning compositions, comprising a proteinic substrate based oxygenase, which provide effective and efficient cleaning of proteic based stains and/or soils such as protein containing food stains/soils and everyday body soils and provide sanitisation of the treated surfaces. Furthermore, the cleaning compositions of the present invention provide fabric realistic items cleaning and whitening performance when formulated as a laundry detergent composition.
The present invention relates to cleaning compositions, including laundry, dishwashing, hard surface cleaner, oral/dental cleaning compositions, comprising a proteinic substrate based oxygenase.
Many consumer relevant stains contain proteinic components and are difficult to remove from the washed surfaces. Food stains originating from dairy products as such, like milk or egg, or processed within food or drink products, are particularly challenging to remove.
In addition, the complex nature of everyday “body” soils typically found on pillow cases, T-shirts, collars and socks, provides a continuous thorough cleaning challenge for detergents. These soils are difficult to remove completely and often residues build up on fabric leading to dinginess and yellowing. Moreover, body fluids stains, such as blood and menstrual fluids, are often difficult to remove effectively from a soiled item, especially when the stains have been ageing. Everyday body soils are also found on sanitary and kitchen surfaces such as bathtubs, toilet bowl and dishware.
The items can be fabrics, hard surfaces, dishware such as plasticware, glassware or chinaware, teeth and mouth.
Traditionally, protease enzymes and/or high levels of bleaching compounds, optionally with bleach precursors and/or bleach enhancers, are incorporated in cleaning compositions. Bleaching agents are compounds which are precursors of hydrogen peroxide which is formed in the course of the washing procedure. Perborates and percarbonates are the most important examples of such hydrogen peroxide precursors.
In view of the above, there exits clearly a continuous need to provide cleaning compositions which have an excellent detergency performance. Accordingly it is an object of the present invention to provide a cleaning composition which provides effective and efficient cleaning of proteic based stains and/or soils such as protein containing food stains/soils and everyday body soils. It is a further object to provide a cleaning composition which provides fabric realistic items cleaning and whitening.
The above objective has been met by formulating cleaning compositions comprising a proteinic substrate based oxygenase.
It has been surprisingly found that an enzymatic bleach system based on a proteinic substrate based oxygenase delivers in a cleaning composition, bleach-like benefits in an unexpected broad range of performance areas such as dingy cleaning, whiteness maintenance and stain removal. It has also been found that the cleaning compositions of the present invention provide sanitisation of the treated surfaces.
It has been further found that the performance of the cleaning compositions of the present invention is improved by the addition of another enzymatic bleach system, a conventional activated bleach system, a metallo catalyst based bleach system and/or another detergent enzyme, especially a protease.
In a preferred embodiment, the present invention relates to a laundry composition comprising a proteinic substrate based oxygenase, further providing fabric realistic items cleaning and whitening. In a second embodiment, the present invention relates to dishwashing or household cleaning compositions comprising a proteinic substrate based oxygenase and in a third embodiment, the present invention relates to oral/dental care compositions comprising a proteinic substrate based oxygenase.
The use of a proteinic substrate based oxygenase in a cleaning composition for substantive removal of proteic based stains/soils such as protein containing food stains/soils and everyday body soils and for sanitisation, has never been previously recognised. Nor have been recognised the substantive fabric realistic items cleaning and whitening performance when the proteinic substrate based oxygenase is used within a laundry detergent composition.
The present invention relates to cleaning compositions, including laundry, dishwashing, hard surface cleaner, oral/dental cleaning compositions, comprising a proteinic substrate based oxygenase, which provide effective and efficient cleaning of proteinic based stains and/or soils such as protein containing food stains/soils and/or everyday body soils and provide sanitisation of the treated surfaces.
Furthermore, the cleaning compositions of the present invention provide fabric realistic items cleaning and whitening performance when formulated as a laundry detergent composition.
The essential component of the cleaning compositions of the present invention is a proteinic substrate based oxygenase. Preferably said enzyme is further characterised by being an iron sulphur or iron heme oxygenase and/or a heavy metal dependant oxygenase.
The small scale test is done in a launderometer Washtec ROACHES equipped with stainless steel jars of 500 ml. The small scale test is done at 30-40° C. with total wash time of 30 minutes. Tests is done in a 1% detergent solution using the detergent as described in example 10, composition 5. The detergent is dissolved in 400 ml of water with a total hardness between 2.0-3.0 mmol Ca2+/L. The pH of the 1% detergent solution is adjusted with an acid (citric acid) or an alkali (NaOH) to pH 8-9. Each jar also contains 15 steel ball for better agitation. Standard stain test fabrics are supplied by wfk-Testgewebe Gmbh (Christenfeld,10-Brueggen, Germany). At least two replicates are run per test. The size of the stains is 3 cm×4 cm. The standard test fabric having the protein substrate are the wfk F1 OEM (eggyolk+milk stained cotton). The enzyme level in this small scale test is 1 mg enzyme protein/L. Levels of cofactor(s) when required are calculated according to the enzyme to cofactor(s) ratio known from literature.
The stain removal performance of the enzyme is analyzed by visual grading by an expert panel or preferentially by an instrumental stain removal measurement e.g. with the Spectraflash 500 apparatus from Datacolor. The Spectraflash 500 settings used for this test are:specular excluded, aperture 'small and U.V. filter FL40 (=UV cut off filter at 400 nm) and calibration is done versus a standard white and black.
The result expressed in color difference (Cielab) dE, is calculated between the test and reference treatment. Test 1 comprises the proteinic substrate based oxygenase of the present invention, test 2 comprises a monophenol monooxygenase of EC 1.14.18.1. The enzymes of the invention (Test 1) have a dE of 1 or more versus the monophenol monooxygenase (Test 2) tested in same conditions.
It has been found that the cleaning compositions of the present invention provide effective and efficient cleaning of proteinic based stains and/or soils such as protein containing food stains/soils and everyday body soils, and in particular, achieve fabric realistic items cleaning and whitening when formulated as laundry detergent composition. Indeed it has been surprisingly found that the proteinic substrate based oxygenase can be efficient on a broader range of proteic materials than the current detergent proteases and on protein compounds not degraded by current detergent proteases.
Without wishing to be bound by theory, It is believed that the performance of this enzyme is achieved through decyclising, decarboxylation and side chain cleavage reactions of the amino acids, peptides and proteins orignating from the protein fraction of the glycoproteins and lipoproteins found in the stains/soils. These reactions are achieved by catalytical direct insertion of molecular oxygen into the amino acids structure.
In addition, the cleaning compositions of the present invention provide sanitisation of the treated surfaces.
The sanitisation potential of the cleaning compositions of the present invention can be enhanced by the addition of chemical sanitisers such as Triclosan and/or hexemidine. Parfums Cosmetiques Actualités No 125, November, 1995, 51-4 describes suitable chemical sanitisers.
The sanitisation benefits of the cleaning compositions of the present invention can be evaluated by the Minimum Inhibitory Concentration (MIC) as described in Tuber. Lung. Dis. 1994 August; 75(4):286-90; J. Clin. Microbiol. 1994 May; 32(5):1261-7 and J. Clin. Microbiol. 1992 October; 30(10):2692-7.
Without wishing to be bound by theory, it is believed that “everyday body soils” contain sebum excreted by the human body. Sebum is believed to contain large quantities of saturated and unsaturated fatty acids, sterols and sterols esters (The physiology and Pathology of the skin, Vol. 9, A. Jarret, (1986)). The fragmentation of the substrate and the formation of ionizable groups or hydrophilic substituents by a proteinic substrate based oxygenase enzyme renders the enzymatic reaction products more soluble and hence easier to be removed from the soiled items.
Suitable proteinic substrate based oxygenases for the purpose of the present invention are listed below:
1.14.11.2 PROCOLLAGEN-PROLIN,2-OXOGLUTARATE 4-
1.14.11.4 PROCOLLAGEN-LYSINE,2-OXOGLUTARATE 5-
1.14.11.7 PROCOLLAGEN-PROLIN,2-OXOGLUTARATE 3-
1.14.11.8 TRIMETHYLLYSINE,2-OXOGLUTARATE
Some of the polyphenol/hetyerocyclic substrate based oxygenases of the present invention require the presence of a cofactor. In this instance, the cleaning compositions of the present invention will further comprise a cofactor such as Ascorbate, oxoglutarate, Flavine Mononucleotide (FMN), Flavine Adenine Dinucleotide (FAD), Nicotine amide Adenine Dinucleotide (Phosphate) (NAD(P)H). When therein include, the cofactor will be comprised at a weight ratio of pure oxygenase to cofactor comprised generally between 10:1 to 1:10, preferably between 5:1 to 1:8, more preferably between 1:2 to 1:5.
The proteinic substrate based oxygenase enzyme is incorporated into the cleaning compositions in accordance with the invention preferably at a level of from 0.0001% to 2%, more preferably from 0.001% to 0.5%, most preferably from 0.002% to 0.1% pure enzyme by weight of the composition.
Preferred proteinic substrate based oxygenases for specific applications are alkaline proteinic substrate based oxygenases, i.e. enzymes having an enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of its maximum activity at a pH ranging from 7 to 12. More preferred proteinic substrate based oxygenases are enzymes having their maximum activity at a pH ranging from 7 to 12.
Enzymes homologue to the proteinic substrate based oxygenase of the present invention are also contemplated. The term “homologue” is intended to indicate a polypeptide encode by DNA which hybridises to the same probe as the DNA coding for the proteinic substrate based oxygenase enzyme with this amino acid sequence under certain specific conditions (such as presoaking in 5×SSC and prehybridising for 1 h at ˜40° C. in a solution of 20% formamide, 5×Denhardt's solution, 50 mM sodium phosphate, pH 6.8, and 50 μg of denaturated sonicated calf thymus DNA, followed by hybridisation in the same solution supplemented with 100 μM ATP for 18 h at ˜40° C.). The term is intended to include derivatives of the proteinic substrate based oxygenase enzyme sequence obtained by addition of one or more amino acid residues to either or both the C- and N-terminal of the native sequence, substitution of one or more amino acid residues at one or more sites in the native sequence, deletion of one or more amino acid residues at either or both ends of the native amino acid sequence or at one or more sites within the native sequence, or insertion of one or more amino acid residues at one or more sites of the native sequence.
The cleaning compositions of the present invention may also contain additional detergent components. The precise nature of these additional components, and levels of incorporation thereof will depend on the physical form of the composition, and the nature of the cleaning operation for which it is to be used.
The cleaning compositions preferably further comprise another enzymatic bleach system, a conventional activated bleach system, a metallo catalyst based bleach system and/or another detergent enzyme.
In a preferred embodiment, the present invention relates to a laundry and/or fabric care composition comprising a proteinic substrate based oxygenase (Examples 1-18). In a second embodiment, the present invention relates to dishwashing or household cleaning compositions including sanitisation compositions (Examples 19-28), and in a third embodiment, the present invention relates to oral/dental care compositions (Examples 29-31).
The cleaning 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.
The compositions of the invention may for example, be formulated as hand and machine dishwashing compositions, 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, and compositions for use in general household hard surface cleaning operations. Compositions containing such proteinic substrate based oxygenase can also be formulated as oral/dental care compositions.
When formulated as compositions for use in manual dishwashing methods the compositions of the invention preferably contain a surfactant and preferably other detergent compounds selected from organic polymeric compounds, suds enhancing agents, group 11 metal ions, solvents, hydrotropes and additional enzymes.
Such compositions containing proteinic subtrate based oxygenase can provide fabric cleaning, stain removal, whiteness maintenance, softening, colour appearance, dye transfer inhibition and sanitisation when formulated as laundry detergent compositions.
The cleaning compositions of the present invention can in addition to the proteinic substrate based oxygenase enzyme further comprise one or more enzymes which provide cleaning performance, fabric care and/or sanitisation benefits. It has been found that the combination of said specific oxygenase with a detergent enzyme provides improved cleaning of proteic based stains and/or soils such as protein containing food stains/soils and everyday body soils and when formulated as laundry composition, improved fabric realistic items cleaning and whitening.
Preferably, the cleaning compositions of the present invention will comprise a protease. Indeed it has been surprisingly found that the proteinic substrate based oxygenase can be efficient on a broader range of proteic materials than current detergent proteases and on protein compounds not degraded by current detergent proteases. The combination of the proteinic substrate based oxygenase and a protease gives synergistic performance on removal of proteic based stains/soils and everyday body soils.
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®D, 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 Apr. 28, 1987 (particularly pages 17, 24 and 98), and which is called herein “Protease B”, and in European Patent Application 199,404, Venegas, published Oct. 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called “Protease A” herein. Suitable is what is called herein “Protease C”, which 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 Compositions Comprising Protease Enzymes” having U.S. Ser. No. 08/322,677, filed Oct. 13, 1994. Also suitable are variants having a different proteolytic activity, stability, substrate specificity, pH profile and/or performance characteristic as compared to the precursor carbonyl hydrolase from which the amino acid sequence of the variant is derived. As stated earlier, the protease enzymes are designed to have trypsin-like specificity and preferably also be bleach stable. The precursor carbonyl hydrolase may be a naturally-occurring carbonyl hydrolase or recombinant hydrolase. Specifically, such carbonyl hydrolase variants have an amino acid sequence not found in nature, which is derived by replacement of a plurality of amino acid residues of a precursor carbonyl hydrolase with different amino acids. The plurality of amino acid residues of the precursor enzyme correspond 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.
The carbonyl hydrolase variants which are protease enzymes useful in the present invention compositions comprise replacement of amino acid residue +210 in combination with one or more additional modifications. While any combination of the above listed amino acid substitutions may be employed, the preferred variant protease enzymes useful for the present invention comprise the substitution, deletion or insertion of amino acid residues in the following combinations: 210/156; 210/166; 210/76; 210/103; 210/104; 210/217; 210/156/166; 210/156/217; 210/166/217; 210/76/156; 210/76/166; 210/76/217; 210/76/156/166; 210/76/156/217; 210/76/166/217; 210/76/103/156; 210/76/103/166; 210/76/103/217; 210/76/104/156; 210/76/104/166; 210/76/104/217; 210/76/103/104/156; 210/76/103/104/166; 210/76/103/104/217; 210/76/103/104/156/166; 210/76/103/104/156/217; 210/76/103/104/166/217 and/or 210/76/103/104/156/166/217; 210176/103/104/166/222; 210/67/76/103/104/166/222; 210/67/76/103/104/166/218/222. Most preferably the variant enzymes useful for the present invention comprise the substitution, deletion or insertion of an amino acid residue in the following combination of residues: 210/156; 210/166; 210/217; 210/156/166; 210/156/217; 210/166/217; 210/76/156/166; 210/76/103/156/166 and 210/76/103/104/1561166 of B. lentus subtilisin with 210/76/103/104/156/166 being the most preferred.
Variant DNA sequences encoding such carbonyl hydrolase or subtilisin variants are derived from a precursor DNA sequence which encodes a naturally-occurring or recombinant precursor enzyme. The variant DNA sequences are derived by modifying the precursor DNA sequence to encode the substitution of one or more specific amino acid residues encoded by the precursor DNA sequence corresponding to positions +210, +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 in Bacillus lentus or any combination thereof. Although the amino acid residues identified for modification herein are identified according to the numbering applicable to B. amyloliquefaciens (which has become the conventional method for identifying residue positions in all subtilisins), the preferred precursor DNA sequence useful for the present invention is the DNA sequence of Bacillus lentus. These recombinant DNA sequences encode carbonyl hydrolase variants having a novel amino acid sequence and, in general, at least one property which is substantially different from the same property of the enzyme encoded by the precursor carbonyl hydrolase DNA sequence. Such properties include proteolytic activity, substrate specificity, stability, altered pH profile and/or enhanced performance characteristics.
Preferably, the substitution to be made at each of the identified amino acid residue positions include but are not limited to substitutions at position +210 including I, V, L, and A, substitutions at positions +33, +62, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, and +218 of D or E, substitutions at position 76 including D, H, E, G, F, K, P and N; substitutions at position 103 including Q, T, D, E, Y, K, G, R and S; and substitutions at position 104 including S, Y, I, L, M, A, W, D, T, G and V; and substitutions at position 222 including S, C, A. The specifically preferred amino acid(s) to be substituted at each such position are designated below in Table I. Although specific amino acids are shown in Table I, it should be understood that any amino acid may be substituted at the identified residues.
+210 I, V, L, A
+33, +62, +100, +101, +107 D, E
+128, +129, +130, +135
+156, +158; +164, +166
+167, +170, +209, +215
+217 and +218
+76 D, H
+103 A, Q, T, D, E, Y, K, G, R
+104 I, Y, S, L, A, T, G
+222 S, C, A
A comparison of the preferred amino acid residues identified herein for substitution versus the preferred substitution for each such position is provided in Table II.
+210 +156 +166 +217 +76 +103 +104
B. amyloliquefaciens P E G Y N Q Y
B. lentus (wild-type) P S S L N S V
Most Preferred I E/D E/D E/D D A I/Y
Preferred proteases for the purpose of the present invention is a serine protease, more preferably a a bacterial serine protease obtained from Bacillus, preferably Bacillus subtilis and/or Bacillus licheniformis.
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 an activity above 50 CEVU (Cellulose Viscosity Unit). Suitable cellulases are disclosed in U.S. Pat. No. 4,435,307, Barbesgoard et al, J61078384 and W096/02653 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.
Examples of such cellulases are cellulases produced by a strain of Humicoia 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 50 KDa, an isoetectric point of 5.5 and containing 415 amino acids; and a −43 kD 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. Also suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum described in WO94/21801, Genencor, published Sep. 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 Nov. 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.
Other preferred enzymes that can be included in the detergent compositions of the present invention include lipases. Suitable lipase enzymes for detergent usage 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. Especially suitable lipases are lipases such as M1 LipaseR and LipomaxR (Gist-Brocades) and LipolaseR and Lipolase UltraR(Novo) which have found to be very effective when used in combination with the compositions of the present invention. Also suitables are the 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.
Examples of commercial α-amylases products are Purafect Ox Am® from Genencor and Termamyl®, Ban® Fungamyl® and Duramyl®, all available from Novo Nordisk A/S Denmark. WO95/26397 describes other suitable amylases: α-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® α-amylase activity assay. Suitable are variants of the above enzymes, described in WO96/23873 (Novo Nordisk). Other amylolytic enzymes with improved properties with respect to the activity level and the combination of thermostability and a higher activity level are described in WO95/35382.
Preferred additional optional detergent ingredients that can be included in the cleaning compositions of the present invention include conventional activated-, other enzymatic- and/or metallo catalyst- based bleach systems. It has been found that the combination of said specific oxygenase with another bleach system provides improved cleaning of proteic based stains and/or soils such as protein containing food stains/soils and everyday body soils and when formulated as laundry composition, improved fabric realistic items cleaning and whitening while providing colour safety.
The hydrogen peroxide releasing agents can be used in combination with bleach activators such as tetraacetylethylenediamine (TAED), nonanoyloxybenzene-sulfonate (NOBS, described in U.S. Pat. No. 4,412,934), 3,5,-trimethyihexanoloxybenzenesulfonate (ISONOBS, described in EP 120,591) or pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-aminocaproic acid (NACA-OBS, described in W094128106), which are perhydrolyzed to form a peracid as the active bleaching species, leading to improved bleaching effect. Also suitable activators are acylated citrate esters such as disclosed in Copending European Patent Application No. 91870207.7 and unsymetrical acyclic imide bleach activator of the following formula as disclosed in the Procter & Gamble co-pending patent applications U.S. Ser. No. 60/022,786 (filed Jul. 30, 1996) and Ser. No. 60/028,122 (filed Oct. 15, 1996):
wherein R1 is a C7-C13 linear or branched chain saturated or unsaturated alkyl group, R2 is a C1-C8 linear or branched chain saturated or unsaturated alkyl group and R3 is a C1-C4 linear or branched chain saturated or unsaturated alkyl group.
Useful 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- pending applications U.S. Ser. No. 08/136,626, PCT/US95/07823, WO95/27772, WO95/27773, WO95/27774 and WO95/27775.
Suitable transition metals e.g., Mn are illustrated hereinafter. “Macropolycyclic” means a MRL is both a macrocycle and is polycyclic. “Polycyclic” means at least bicyclic. The term “rigid” as used herein herein includes “having a superstructure” and “cross-bridged”. “Rigid” has been defined as the constrained converse of flexibility: see D. H. Busch., Chemical Reviews., (1993), 93, 847-860, incorporated by reference. More particularly, “rigid” as used herein means that the MRL must be determinably more rigid than a macrocycle (“parent macrocycle”) which is otherwise identical (having the same ring size and type and number of atoms in the main ring) but lacking a superstructure (especially linking moieties or, preferably cross-bridging moieties) found in the MRL's. In determining the comparative rigidity of macrocycles with and without superstructures, the practitioner will use the free form (not the metal-bound form) of the macrocycies. Rigidity is well-known to be useful in comparing macrocycles; suitable tools for determining, measuring or comparing rigidity include computational methods (see, for example, Zimmer, Chemical Reviews, (1995), 95(38), 2629-2648 or Hancock et al., Inorganica Chimica Acta (1989), 164, 73-84. A determination of whether one macrocycle is more rigid than another can be often made by simply making a molecular model, thus it is not in general essential to know configurational energies in absolute terms or to precisely compute them. Excellent comparative determinations of rigidity of one macrocycle vs. another can be made using inexpensive personal computer-based computational tools, such as ALCHEMY III, commercially available from Tripos Associates. Tripos also has available more expensive software permitting not only comparative, but absolute determinations; alternately, SHAPES can be used (see Zimmer cited supra). One observation which is significant in the context of the present invention is that there is an optimum for the present purposes when the parent macrocycle is distinctly flexible as compared to the cross-bridged form. Thus, unexpectedly, it is preferred to use parent macrocycles containing at least four donor atoms, such as cyciam derivatives, and to cross-bridge them, rather than to start with a more rigid parent macrocycle. Another observation is that cross-bridged macrocycles are significantly preferred over macrocycles which are bridged in other manners.
Suitable metals in the rigid ligand complexes include Mn(II), Mn(III), Mn(IV), Mn(V), Fe(II), Fe(III), Fe(IV), Co(I), Co(II), Co(III), Ni(I), Ni(II), Ni(III), Cu(I), Cu(II), Cu(III), Cr(II), Cr(III), Cr(IV), Cr(V), Cr(VI), V(III), V(IV), V(V), Mo(IV), Mo(V), Mo(VI), W(IV), W(V), W(VI), Pd(II), Ru(II), Ru(III), and Ru(IV). Preferred transition-metals in the instant transition-metal bleach catalyst include manganese, iron and chromium. Preferred oxidation states include the (II) and (III) oxidation states. Manganese(II) in both the low-spin configuration and high spin complexes are included. It is to be noted that complexes such as low-spin Mn(II) complexes are rather rare in all of coordination chemistry. The designation (II) or (III) denotes a coordinated transition metal having the requisite oxidation state; the coordinated metal atom is not a free ion or one having only water as a ligand.
wherein m and n are integers from about 1 to 8, more preferably from 1 to 3; Z is N or CH; and T is a compatible substituent, for example H, alkyl, triaikyl-ammonium, halogen, nitro, sulfonate, or the like. The aromatic ring in 1.10 can be replaced by a saturated ring, in which the atom in Z connecting into the ring can contain N, O, S or C.
Without intending to be limited by theory, it is believed that the preorganization built into the MRL's herein that leads to extra kinetic and/or thermodynamic stability of their metal complexes arises from either or both of topological constraints and enhanced rigidity (loss of flexibility) compared to the free parent macrocycle which has no superstructure. The MRL's as defined herein and their preferred cross-bridged sub-family, which can be said to be “ultra-rigid”, combine two sources of fixed preorganization. In preferred MRL's herein, the linking moieties and parent macrocycle rings are combined to form ligands which have a significant extent of “fold”, typically greater than in many known superstructured ligands in which a superstructure is attached to a largely planar, often unsaturated macrocycle. See, for example: D. H. Busch, Chemical Reviews, (1993), 93, 847-880. Further, the preferred MRL's herein have a number of particular properties, including (1) they are characterized by very high proton affinities, as in so-called “proton sponges”; (2) they tend to react slowly with multivalent transition metals, which when combined with (1) above, renders synthesis of their complexes with certain hydrolyzable metal ions difficult in hydroxylic solvents; (3) when they are coordinated to transition metal atoms as identified herein, the MRL's result in complexes that have exceptional kinetic stability such that the metal ions only dissociate extremely slowly under conditions that would destroy complexes with ordinary ligands; and (4) these complexes have exceptional thermodynamic stability; however, the unusual kinetics of MRL dissociation from the transition metal may defeat conventional equilibrium measurements that might quantitate this property.
Dichloro 5,12-dimethyl-4-phenyl-1,5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(II)
Dichloro-3,3,5,10,10,12-hexamethyl-1,5,8,12-tetraazabicyclo[6.6.2)hexadecane Manganese(II)
Dichioro-1,4,7,10-tetraazabicyclo[5.5.2]tetradecane Iron(II)
Aquo-chloro-2-(2-hydroxyphenyl)-5,12-dimethyl1,5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(II)
Chloro-2-(2-hydroxybenzyl)-5-methyl1,5,8,12-tetraazabicyclo[6.6.2]hexadecane Manganese(II)
Chloro-10-(2-hydroxybenzyl)-4-methyl-1,4,7,10-tetraazabicycio[5.5.2]tetradecane Manganese(II)
Dichioro-5,12-dimethyl-1,5,8,12-tetraazabicyclo[7.6.2]heptadecane Manganese(II)
Trifluoromethanesulfono-20-methyl-1,9,20,24,25-pentaaza-tetracyclo[7.7.7.13,7.111,15.]pentacosa-3,5,7(24),11,13,1 5(25)-hexaene Manganese(lI) Trifluoromethanesulfonate
Chloro-5,12,17-trimethyl-1,5,8,12,17-pentaazabicycio[6.6.5]nonadecane Manganese(II) Hexafluorophosphate
Chloro-4,10,15-trimethyl-1,4,7,10,15-pentaazabicyclof5.5.5]heptadecane Manganese(II) Hexafluorophosphate
The practitioner may further benefit if certain terms receive additional definition and illustration. As used herein, “macrocyclic rings” are covalently connected rings formed from four or more donor atoms (i.e., heteroatoms such as nitrogen or oxygen) with carbon chains connecting them, and any macrocycle ring as defined herein must contain a total of at least ten, preferably at least twelve, atoms in the macrocycle ring. A MRL herein may contain more than one ring of any sort per ligand, but at least one macrocycle ring must be identifiable. Moreover, in the preferred embodiments, no two hetero-atoms are directly connected. Preferred transition-metal bleach catalysts are those wherein the MRL comprises an organic macrocycle ring (main ring) containing at least 10-20 atoms, preferably 12-18 atoms, more preferably from about 12 to about 20 atoms, most preferably 12 to 16 atoms. “Donor atoms” herein are heteroatoms such as nitrogen, oxygen, phosphorus or sulfur, which when incorporated into a ligand still have at least one lone pair of electrons available for forming a donor-acceptor bond with a metal. Preferred transition-metal bleach catalysts are those wherein the donor atoms in the organic macrocycle ring of the cross-bridged MRL are selected from the group consisting of N, O, S, and P, preferably N and O, and most preferably all N. Also preferred are cross-bridged MRL's comprising 4 or 5 donor atoms, all of which are coordinated to the same transition metal. Most preferred transition-metal bleach catalysts are those wherein the cross-bridged MRL comprises 4 nitrogen donor atoms all coordinated to the same transition metal, and those wherein the cross-bridged MRL comprises 5 nitrogen atoms all coordinated to the same transition metal. “Non-donor atoms” of the MRL herein are most commonly carbon, though a number of atom types can be included, especially in optional exocyclic substituents (such as “pendant” moieties, illustrated hereinafter) of the macrocycles, which are neither donor atoms for purposes essential to form the metal catalysts, nor are they carbon. Thus, in the broadest sense, the term “non-donor atoms” can refer to any atom not essential to forming donor bonds with the metal of the catalyst. Examples of such atoms could include heteroatoms such as sulfur as incorporated in a non-coordinatable sulfonate group, phosphorus as incorporated into a phosphonium salt moiety, phosphorus as incorporated into a P(V) oxide, a non-transition metal, or the like. In certain preferred embodiments, all non-donor atoms are carbon.
“Bcyclam” (5,12-dimethyl-1,5,8,12-tetraaza-bicyclo[6.6.21hexadecane) is prepared by a synthesis method described by G. R. Weisman, et al., J.Amer.Chem.Soc., (1990), 112, 8604. Bcyclam (1.00 g., 3.93 mmol) is dissolved in dry CH3CN (35 mL, distilled from CaH2). The solution is then evacuated at 15 mm until the CH3CN begins to boil. The flask is then brought to atmospheric pressure with Ar. This degassing procedure is repeated 4 times. Mn(pyridine)2Cl2 (1.12 g., 3.93 mmol), synthesized according to the literature procedure of H. T. Witteveen et al., J. Inorg. Nucl. Chem., (1974), 36, 1535, is added under Ar. The cloudy reaction solution slowly begins to darken. After stirring overnight at room temperature, the reaction solution becomes dark brown with suspended fine particulates. The reaction solution is filtered with a 0.2μ filter. The filtrate is a light tan color. This filtrate is evaporated to dryness using a rotoevaporator. After drying overnight at 0.05 mm at room temperature, 1.35 g. off-white solid product is collected, 90% yield. Elemental Analysis: %Mn, 14.45; %C, 44.22; %H, 7.95; theoretical for [Mn(Bcyclam)Cl2], MnC14H30N4Cl2, MW=380.26. Found: %Mn, 14.98; %C, 44.48; %H, 7.86; Ion Spray Mass Spectroscopy shows one major peak at 354 mu corresponding to [Mn(Bcyclam)(formate)]+.
Freshly distilled Bcyclam (25.00 g., 0.0984 mol), which is prepared by the same method as above, is dissolved in dry CH3CN (900 mL, distilled from CaH2). The solution is then evacuated at 15 mm until the CH3CN begins to boil. The flask is then brought to atmospheric pressure with Ar. This degassing procedure is repeated 4 times. MnCl2 (11.25 g., 0.0894 mol) is added under Ar. The cloudy reaction solution immediately darkens. After stirring 4 hrs. under reflux, the reaction solution becomes dark brown with suspended fine particulates. The reaction solution is filtered through a 0.2 μ filter under dry conditions. The filtrate is a light tan color. This filtrate is evaporated to dryness using a rotoevaporator. The resulting tan solid is dried overnight at 0.05 mm at room temperature. The solid is suspended in toluene (100 mL) and heated to reflux. The toluene is decanted off and the procedure is repeated with another 100 mL of toluene. The balance of the toluene is removed using a rotoevaporator. After drying overnight at 0.05 mm at room temperature, 31.75 g. of a light blue solid product is collected, 93.5% yield. Elemental Analysis: %Mn, 14.45; %C, 44.22; %H, 7.95; %N, 14.73; %Cl, 18.65; theoretical for [Mn(Bcyclam)Cl2], MnC14H30N4Cl2, MW=380.26. Found: %Mn, 14.69; %C, 44.69; %H, 7.99; %N, 14.78; %Cl, 18.90 (Karl Fischer Water, 0.68%). Ion Spray Mass Spectroscopy shows one major peak at 354 mu corresponding to [Mn(Bcyclam)(formate)]+.
The cleaning compositions according to the present invention generally 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.
Also useful as the nonionic surfactant of the surfactant systems of the present invention are the alkylpolysaccharides disclosed in U.S. Pat. No. 4,565,647, Llenado, issued Jan. 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. 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. The preferred alkylpolyglycosides have the formula
wherein R1 is H, or R1 is C1-4 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R2 is C5-31 hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to the chain, or an alkoxyiated derivative thereof. Preferably, R1 is methyl, R2 is a straight C11-15 alkyl or C16-18 alkyl or alkenyl chain such as coconut alkyl or mixtures thereof, and Z is derived from a reducing sugar such as glucose, fructose, maltose, lactose, in a reductive amination reaction.
The preferred alkyl ester sulfonate surfactant, especially for laundry applications, comprise alkyl ester sulfonate surfactants of the structural formula
wherein R3 is a C8-C20 hydrocarbyl, preferably an alkyl, or combination thereof, R4 is a C1-C6 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 monoethanolamine, diethanolamine, and triethanoiamine. Preferably, R3 is C10-C16 alkyl, and R4 is methyl, ethyl or isopropyl. Especially preferred are the methyl ester sulfonates wherein R3 is C10-C16 alkyl.
Other anionic surfactants useful for detersive purposes can also be included in the cleaning compositions of the present invention. These can include salts (including, for example, sodium, potassium, ammonium, and substituted ammonium salts such as mono-, di- and triethanolamine salts) of 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. 1,082,179, C8-C24 alkylpolyglycolethersulfates (containing up to 10 moles of ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty 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 monoesters) 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(CH2CH2O)k-CH2COO—M+ wherein R is a C8-C22 alkyl, k is an integer from 1 to 10, and M is a soluble salt-forming cation. Resin acids and hydrogenated resin acids are also suitable, such as rosin, hydrogenated rosin, and resin acids and hydrogenated resin acids present in or derived from tall oil.
R3, R4═CH3 and R5═CH2CH2OH.
R1R2R3R4N+X−(i)
The preferred alkyl chain length for R1 is C12-C15 particularly where the alkyl group is a mixture of chain lengths derived from coconut or palm kernel fat or is derived synthetically by olefin build up or OXO alcohols synthesis. Preferred groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X may be selected from halide, methosulphate, acetate and phosphate ions. Examples of suitable quaternary ammonium compounds of formulae (i) for use herein are:
5) dioleyl dimethylammonium chloride:
The quaternary ammonium compounds and amine precursors herein have the formula (I) or (il), below
Specific examples of quaternary ammonium compounds suitable for use in the aqueous fabric softening compositions herein include
4) N ,N-di(2-tallowyl-oxy-ethylcarbonyl-oxy-ethyl)-N,N-dimethyl ammonium chloride;
Ampholytic surfactants are also suitable for use in the cleaning 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. Pat. No. 3,929,678 to Laughlin et al., issued Dec. 30, 1975 at column 19, lines 18-35, for examples of ampholytic surfactants. When included therein, 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 ampholytic surfactants.
The cleaning 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 R1NH2 wherein R1 is a C6-C12, preferably C6-C10 alkyl chain or R4X(CH2)n, X is —O—,—C(O)NH— or —NH—, R4 is a C6-C12 alkyl chain n is between 1 to 5, preferably 3. R1 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, octyloxypropyiamine, 2-ethylhexyl-oxypropylamine, lauryl amido propylamine and amido propylamine.
R3 is either a C6-C12, preferably C6-C10 alkyl chain, or R3 is R4X(CH2)n, whereby X is —O—, —C(O)NH— or —NH—, R4 is a C4-C12, n is between 1 to 5, preferably 2-3. R5 is H or C1-C2 alkyl and x is between 1 to 6 .
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 amidopropyidimethylamine, C8-10 amidopropyldimethylamine and C10 amidopropyidimethylamine.
The most preferred amines for use in the compositions herein are 1-hexylamine, 1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n- dodecyidimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7 times ethoxylated, lauryl amido propylamine and cocoamido propylamine.
Technologies which provide a type of color care benefit can also be included. Examples of these technologies are metallo catalysts for color maintenance. Such metallo catalysts are described in copending European Patent Application No. 92870181.2. Dye fixing agents, polyolefin dispersion for anti-wrinkles and improved water absorbancy, perfume and amino-functional polymer for color care treatment and perfume substantivity are further examples of color care/fabric care technologies and are described in the co-pending Patent Application No. 96870140.9, filed November 07, 1996.
Fabric softening agents can also be incorporated into cleaning 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-Al 514 276 and EP-BO 011 340 and their combination with mono C12-C14 quaternary ammonium salts are disclosed in EP-B-0 026 527 and EP-B-0 026 528 and di-long-chain amides as disclosed in EP-B-0 242 919. Other useful organic ingredients of fabric softening systems include high molecular weight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0 313 146.
Alicyclic and heterocyclic polycarboxylates include cyclopentane- cis, cis,cis-tetracarboxylates, cyclopentad ien ide pentacarboxylates, 2,3,4,5-tetrahydro-furan-cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan-cis-dicarboxylates, 2,2,5,5-tetrahydrofuran-tetracarboxyiates, 1,2,3,4,5,6-hexane-hexacar-boxylates 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 cleaning compositions herein may also optionally contain one or more iron and/or manganese chelating agents. Such 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.
Another optional ingredient is a suds suppressor, exemplified by silicones, and silica-siiicone 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. Alternatively 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. Pat. No. 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 Apr. 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. Such suds suppressor system are described in Copending European Patent application N 92870174.7 filed Nov. 10, 1992.
Other components used in cleaning compositions may be employed, such as soil-suspending agents, soil-release agents, optical brighteners, abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encapsulated or non- encapsulated perfumes.
Antiredeposition and soil suspension agents suitable herein include cellulose derivatives such as methyicellulose, 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 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′-disulphonate, di-sodium 4,4′-bis-(4-phenyl-2,1,3-triazol-2-yl)-stilbene-2,2′disulphonate, di-so-dium 4,4′bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-6-ylami-no)stilbene-2,2′disulphonate, sodium 2(stilbyl-4″-(naphtho-1′,2′:4,5)-1,2,3-triazole-2″-sulphonate and 4,4′-bis(2-sulphostyryl)biphenyl. Highly preferred brighteners are the specific brighteners of copending European Patent application No. 95201943.8.
where PEG is —(OC2H4)O—,PO is (OC3H6O) and T is (pcOC6H4CO).
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.
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 90101815 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 —(CH2CH2O)m(CH2)nCH3 wherein m is 2-3 and n is 6-12. The side-chains are ester-linked to the polyacrylate “backbone” to provide a “comb” polymer type structure. The molecular weight can vary, but is typically in the range of about 2000 to about 50,000. Such alkoxylated polycarboxylates can comprise from about 0.05% to about 10%, by weight, of the compositions herein.
The cleaning compositions 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.
Polymeric lime soap peptisers suitable for use herein are described in the article by M. K. Nagaraian, W. F. Masler, to be found in Cosmetics and Toiletries, volume 104, pages 71-73, (1989).
The cleaning compositions of the present invention can also include compounds for inhibiting dye transfer from one fabric to another of solubilized and suspended dyes encountered during fabric laundering operations involving colored fabrics.
The cleaning compositions according to the present invention 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.
P is a polymerisable unit, whereto the R—N—O group can be attached to or wherein the R—N—O group forms part of the polymerisable unit or a combination of both.
The N—O group can be represented by the following general structures
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.
The N-vinylimidazole N-vinylpyrroiidone 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 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. Suitable poiyvinylpyrrolidones are commercially vailable from ISP Corporation, New York, N.Y. 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). Other suitable polyvinylpyrrolidones which are commercially available from BASF Cooperation include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones known to persons skilled in the detergent field (see for example EP-A-262,897 and EP-A-256,696).
The detergent compositions of the present invention may also utilize polyvinylimidazole as polymeric dye transfer inhibiting agent. Said polyvinylimidazoles have an average
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.
In one embodiment, 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. In another embodiment, the cross- linked polymers entrap the dyes by swelling.
Such cross-iinked polymers are described in the co-pending patent application 94870213.9
A preferred machine dishwashing method comprises treating soiled articles with an aqueous liquid having dissolved or dispensed therein an effective amount of the machine diswashing or rinsing composition. A conventional effective amount of the machine dishwashing composition means from 8-60 g of product dissolved or dispersed in a wash volume from 3-10 liters. According to a manual dishwashing method, soiled dishes are contacted with an effective amount of the diswashing composition, typically from 0.5-20 g (per 25 dishes being treated). Preferred manual dishwashing methods include the application of a concentrated solution to the surfaces of the dishes or the soaking in large volume of dilute solution of the detergent composition.
In the cleaning compositions, 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:
Neodol C14-C15 linear primary alcohol ethoxylate, sold by Shell
45-13 Chemical CO.
Polygel/ High molecular weight crosslinked polyacrylates.
Photo- Sulfonated zinc phtalocyanine encapsulated in dextrin
activated soluble polymer.
Photo- Sulfonated alumino phtalocyanine encapsulated in
activated dextrin soluble polymer.
Oxygenase Phenyl alanine monooxygenase sold by Sigma under
No. P6268 with 6-methyltetrahydroptarine sold by Sigma
under the No. M4758 and DL-dithiothreitol sold by Sigma
under the No. D0632, as cofactors - with a weight ratio of
pure enzyme to cofactor between 1:2 and 1:5.
Ox AmR described in WO94/18314, WO96/05295 sold
by Genencor; Termamyl ®, Fungamyl ® and Duramyl ®,
Brightener 2 Disodium 4,4′-bis(4-anilino-6-morpholino-1,3,5-triazin-2-
antifoam oxyalkylene copolymer as dispersing agent with a ratio of
Suppressor granular form.
QEA bis((C2H5O)(C2H4O)n)(CH3)—N+—C6H13—N+—(CH3)
Silica Precipitated silica identified as Zeodent 119 offered by
dental J. M. Huber.
Carboxy- Carbopol offered by B. F. Goodrich Chemical Company.
Carrageenan Iota Carrageenan offered by Hercules Chemical
Silicone anti- 0.5 0.5 0.5 — 0.3 0.3
Density in g/ 850 850 850 850 850 850
STPP 19.7 — — — —
NaSKS-6/ — 10.6 — 10.6 — —
Silicone 0.5 2.4 0.3 0.5 0.3 2.0
Density in 750 750 750 750 750 750
Na-SKS-6 10.0  — — —
Misc (Water — 2.0 2.0 2.0 — 2.0
Miscellaneous and Up to 100%
Brightener 1/2 0.05 0.02 0.08 0.1
Dodecenyl/tetradecenyl succinic 12.0 10.0 — —
PB1 15.0 15.0
Ca Carbonate 27.5 39.0 35.0 — — 40.0 — 40.0
Bentonite clay — 10.0 — — 5.0 — — —
STPP — — 54.3 51.4 51.4 — — 50.9
Citrate 35.0 17.0 — — — 46.1 40.2 —
Carbonate — 17.5 14.0 14.0 14.0 — 8.0 32.1
Bicarbonate — — — — — 25.4 — —
Silicate 32.0 14.8 14.8 10.0 10.0 1.0 25.0 3.1
Percarbonate — — — — — 6.7 11.8 4.8
HEDP — 1.0 — — — — — —
DETPMP — 0.6 — — — — — —
PMC — — 0.008 0.01 0.007 — — —
Paraffin 0.5 0.5 0.5 0.5 0.5 0.6 — —
Sulphate 7.0 20.0 5.0 2.2 0.8 12.0 4.6 —
pH 10.8 11.0 10.8 11.3 11.3 9.6 10.8 10.9
STPP 30.0 30.0 33.0 34.2 29.6 31.1 26.6 17.6
Carbonate 30.5 30.5 31.0 30.0 23.0 39.4 4.2 45.0
Silicate 7.4 7.4 7.5 7.2 13.3 3.4 43.7 12.4
Metasilicate — — 4.5 5.1 — — — —
Percarbonate — — — — — 4.0 — —
PB1 4.4 4.2 4.5 4.5 — — — —
PAAC — 0.004 0.004 0.004 — — — —
Sulphate 23.4 25.0 22.0 18.5 30.1 19.3 23.1 23.6
pH 10.8 10.8 11.3 11.3 10.7 11.5 12.7 10.9
Weight of 25 g 25 g 20 g 30 g 18 g 20 g
C12 glucose amide — — 6.0 — —
Polyhydroxy fatty — — — 6.5 6.5
Sodium diethylene — — 0.03 — —
Alkyl diphenyl — — — — 2.3
C12(E)S 0.5 0.5 0.5
C16-18 fatty alcohol/50EO 80.0 — —
C14-15 linear alcohol 7EO 2.0 10.0
The following single layer effervescent denture cleansing tablets were prepared according to the present invention:
Oxygenase 0.1 0.08
Protease 0.05 2.0
Sodium bicarbonate 39.0 39.0
Malic acid 14.0 14.0
Sulphamic acid 3.0 3.0
TAED 2.0 2.0
Dye/Flavor 2.0 2.0
PB1 16.0 16.0
EDTA 3.0 3.0
PEG 10,000 6.0 6.0
K monopersulfate 13.0 13.0
Na carbonate 1.0 1.0
LAS 1.0 1.0
Pyrogenic silica 2.0 2.0
The following dentifrice compositions were prepared according to the present invention:
Sorbitol (70% aqueous solution) 35.0 35.0 35.0 35.0
PEG-6 1.0 1.0 1.0 1.0
Silica dental abrasive 20.0 20.0 20.0 20.0
Sodium fluoride 0.2 0.2 0.2 0.2
Oxygenase 0.05 0.08 0.1 0.2
Protease 0.05 0.1 0.9 2.0
Sodum alkyl sulfate (27.9% 4.0 4.0 4.0 4.0
Carboxyvinyl polymer 0.3 0.3 0.3 0.3
Carrageenan 0.8 0.8 0.8 0.8
The following mouthwash compositions were prepared according to the present invention:
SDA 40 Alcohol 8.0 8.0 8.0 8.0
Flavor 0.08 0.08 0.08 0.08
Emulsifier 0.08 0.08 0.08 0.08
Sodium fluoride 0.05 0.05 0.05 0.05
Glycerin 10.0 10.0 10.0 10.0
Sweetener 0.02 0.02 0.02 0.02
Protease 0.01 0.09 0.2 2.0
Benzoic acid 0.05 0.05 0.05 0.05
Sodium hydroxide 0.2 0.2 0.2 0.2
Dye 0.04 0.04 0.04 0.04
1. A cleaning composition comprising a proteinic substrate based oxygenase and a cofactor.
2. A cleaning composition according to claim 1 wherein said proteinic substrate based oxygenase is further characterised by being an iron sulphur or iron heme oxygenase and/or a heavy metal dependant oxygenase.
3. A cleaning composition according to claim 1 wherein said proteinic substrate based oxygenase is present at a level of from about 0.0001% to about 2% pure enzyme by weight of total composition.
4. A cleaning composition according to claim 3 wherein said proteinic substrate based oxygenase is present at a level of from about 0.001% to about 0.5% pure enzyme by weight of total composition.
5. A cleaning composition according to claim 4 wherein said proteinic substrate based oxygenase is present at a level of from about 0.002% to about 0.1% pure enzyme by weight of total composition.
6. A cleaning composition according to claim 1 wherein said proteinic substrate based oxygenase is alkaline.
7. A cleaning composition according to claim 1 wherein the cofactor is comprised at a weight ratio of pure proteinic substrate based oxygenase to cofacor between about 10:1 to about 1:10.
8. A cleaning composition according to claim 7 wherein the cofactor is comprised at a weight ratio of pure proteinic substrate based oxygenase to cofactor between about 5:1 to about 1:8.
9. A cleaning composition according to claim 8 wherein the cofactor is comprised at a weight ratio of pure proteinic substrate based oxygenase to cofactor between about 1:2 to about 1:5.
10. A cleaning composition according to claim 1 further comprising a detergent enzyme.
11. A cleaning composition according to claim 10 wherein the detergent enzyme is selected from the group consisting of cellulase, lipase, protease, amylase and mixtures thereof.
12. A cleaning composition according to claim 11 wherein said enzyme is a serine protease.
13. A cleaning composition according to claim 12 wherein said protease is obtained from Bacillus.
14. A cleaning composition according to claim 13 wherein said protease is obtained from Bacillus subtilis and/or Bacillus licheniformis.
15. A cleaning composition according to claim 1 further comprising a conventional activated bleach system.
16. A cleaning composition according to claim 15 wherein the bleaching agent is selected from the group consisting of perborate, percarbonate and/or mixtures thereof and the activator is selected from the group consisting of tetraacetylethylenediamine, nonanoyloxybenzenesulfonate, 3,5,-trimethyl-hexanoloxy-benzenesulfonate and mixtures thereof.
17. A cleaning composition according to claim 1 further comprising another enzymatic bleach system.
18. A cleaning composition according to claim 1 further comprising a metallo catalyst based bleach system.
19. A cleaning composition according to claim 18 wherein said metallo catalyst is a transition metal complex of a macropolycyclic rigid ligand.
20. A cleaning composition according to claim 18 wherein said metallo catalyst is manganese.
21. A cleaning composition according to claim 1 which is in the form of an additive.
22. A fabric softening composition comprising proteinic based oxygenase and a cationic surfactant comprising two C12-C18 chain lengths.
23. A method of cleaning comprising the step of contacting a fabric with a cleaning and/or softening composition comprising a proteinic substrate based oxygenase, for fabric cleaning and/or fabric stain removal and/or fabric whiteness maintenance and/or fabric softening and/or fabric colour appearance and/or fabric dye transfer inhibition.
24. A method of cleaning comprising the step of contacting a hard surface with a cleaning composition according to claim 1.
25. A method according to claim 24 wherein the hard surface is dishware.
26. A method of cleaning teeth and/or mouth comprising the administration of a cleaning composition comprising a proteinic substrate based oxygenase.
27. A method of sanitisation comprising the step of contacting a fabric, or a hard surface with a cleaning composition according to claim 1 additionally comprising a polyphenol.
28. A method of sanitisation of teeth and/or mouth comprising the administration of a cleaning composition comprising a polyphenol and/or heterocyclic substrate based oxygenase.
US09462560 1997-07-09 1997-07-09 Cleaning compositions comprising a specific oxygenase Expired - Lifetime US6204234B1 (en)
US09462560 US6204234B1 (en) 1997-07-09 1997-07-09 Cleaning compositions comprising a specific oxygenase
PCT/US1997/012280 WO1999002632A1 (en) 1997-07-09 1997-07-09 Cleaning compositions comprising a specific oxygenase
US6204234B1 true US6204234B1 (en) 2001-03-20
ID=23836876
US09462560 Expired - Lifetime US6204234B1 (en) 1997-07-09 1997-07-09 Cleaning compositions comprising a specific oxygenase
US (1) US6204234B1 (en)
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US3944470A (en) * 1973-06-29 1976-03-16 The Procter & Gamble Company Stabilization and enhancement of enzymatic activity
US5795855A (en) * 1993-06-29 1998-08-18 Novo Nordisk A/S Enhancement of laccase reactions
US5912405A (en) * 1994-09-27 1999-06-15 Novo Nordisk A/S Enhancers such as acetosyringone
US5885304A (en) * 1993-06-29 1999-03-23 Novo Nordisk A/S Enhancement of laccase reactions
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