Source: https://patents.google.com/patent/US5932532A/en
Timestamp: 2018-11-19 07:52:49
Document Index: 421509607

Matched Legal Cases: ['Application No. 2', 'application no. 08', 'application no. 08', 'application no. 08', 'application no. 08', 'application no. 08', 'application no. 08', 'application no. 08', 'application no. 08', 'application no. 08']

US5932532A - Bleach compositions comprising protease enzyme - Google Patents
Bleach compositions comprising protease enzyme Download PDF
US5932532A
US5932532A US08931684 US93168497A US5932532A US 5932532 A US5932532 A US 5932532A US 08931684 US08931684 US 08931684 US 93168497 A US93168497 A US 93168497A US 5932532 A US5932532 A US 5932532A
US08931684
Catherine Michelle Quinn
Bleaching and cleaning compositions comprising a bleaching compound, one or more bleach activators, and protease enzymes are provided. Thus, laundry detergent compositions which comprise protease, perborate or percarbonate and activators such as benzoyl caprolactain exhibit improved dingy clean-up performance.
This application is a continuation-in-part of U.S. patent application Ser. No. 08/322,677, filed Oct. 13, 1994, now U.S. Pat. No. 5,677,272 which is a continuation-in-part of U.S. application Ser. No. 08/136,626, filed Oct. 14, 1993, now abandoned, and U.S. application Ser. No. 08/237,938, filed May 2, 1994, now abandoned.
The present invention relates to cleaning and bleaching compositions which employ protease enzymes to boost performance especially on dingy stains and soil. Bleaching, fabric laundering, automatic dishwashing and sanitizing compositions with improved bleach activity are provided.
It has been found that certain levels of bleach activators and peroxygen bleaching compounds can be used with certain levels of protease enzymes in bleaching compositions to obtain surprisingly effective dingy soil clean-up. The combined effect of the bleach activators, peroxygen bleaching compound and the proteases, which hydrolyzes protein based stains, is greater in this bleaching composition than expected, especially in light of the fact that bleach is known to oxidize enzymes. Without meaning to be limited by theory, it is believed that at these levels, there is a synergy between the bleach activator/peroxygen bleaching compound and the protease so that the combined cleaning effect of the two is greater than the additive effect of each one separately.
Accordingly, it is an object of the present invention to provide improved cleaning and bleaching compositions using bleaching compounds and protease enzymes. It is another object herein to provide a means for removing dingy soils and stains from fabrics using the bleaching systems and protease enzymes of this invention. These and other objects are secured herein, as will be seen from the following disclosures.
The use of amido-derived bleach activators in laundry detergents is described in U.S. Pat. No. 4,634,551. Lactam activators are described in copending applications Serial Nos. 08/064,624; 08/064,562; 08/196,322; and 08/082,270.
Protease enzymes are described in EP 90915958:4; U.S. Pat. No. 5,185,250; U.S. Pat. No. 5,204,015; copending application U.S. Ser. No.08/136,797; and copending application U.S. Ser. No. 08/136,626.
The present invention encompasses bleach compositions which provide dingy clean-up comprising protease enzymes, a bleach compound capable of yielding hydrogen peroxide in an aqueous liquor, and one or more bleach activators, such that the combined performance of the bleach activator/bleaching compound and the protease enzyme as measured by the Hunter Whiteness Value is more than additive; and wherein further such compositions do not comprise nonanoyloxybenzenesulfonate (NOBS) as the sole bleach activator.
Modified protease bacterial serine protease enzymes obtained from Bacillus subtilis, Bacillus lentus or Bacillus licheniformis are preferred. Said enzymes comprise at least about 0.001%, preferably from about 0.001% to about 5%, of the detergent compositions.
Preferred bleaching agents are members selected from the group consisting of H2 O2, perborate, percarbonate, persulfate and mixtures thereof. Particularly preferred bleaching agents comprise percarbonate or perborate bleach, or mixtures thereof. Preferred bleach activators are selected from acyl lactam-type activators, amido-derived activators, alkanoyloxybenzenesulfonates, and mixtures thereof.
Particularly preferred activators which are employed in the present invention include benzoyl caprolactam, nonanoyl caprolactam, benzoyl valerolactam, nonanoyl valerolactam, 3,5,5-trimethylhexanoyl caprolactam, 3,5,5-trimethylhexanoyl valerolactam, octanoyl caprolactam, octanoyl valerolactam, decanoyl caprolactam, decanoyl valerolactam, undecenoyl caprolactam, undecenoyl valerolactam, (6-octanamidocaproyl)oxybenzenesulfonate, (6-nonanamidocaproyl)-oxybenzenesulfonate, (6-decanamidocaproyl)oxybenzenesulfonate, benzoyloxybenzenesulfonate, and mixtures thereof. Examples of highly preferred substituted benzoyl lactams include methylbenzoyl caprolactam, methylbenzoyl valerolactam, ethylbenzoyl caprolactam, ethylbenzoyl valerolactam, propylbenzoyl caprolactam, propylbenzoyl valerolactam, isopropylbenzoyl caprolactam, isopropylbenzoyl valerolactam, butylbenzoyl caprolactam, butylbenzoyl valerolactam, tert-butylbenzoyl caprolactam, tert-butylbenzoyl valerolactam, pentylbenzoyl caprolactam, pentylbenzoyl valerolactam, hexylbenzoyl caprolactam, hexylbenzoyl valerolactam, ethoxybenzoyl caprolactam, ethoxybenzoyl valerolactam, propoxybenzoyl caprolactam, propoxy-benzoyl valerolactam, isopropoxybenzoyl caprolactam, isopropoxybenzoyl valero-lactam, butoxybenzoyl caprolactam, butoxybenzoyl valerolactam, tert-butoxy-benzoyl caprolactam, tert-butoxybenzoyl valerolactam, pentoxybenzoyl capro-lactam, pentoxybenzoyl valerolactam, hexoxybenzoyl caprolactam, hexoxybenzoyl valerolactam, 2,4,6-trichlorobenzoyl caprolactam, 2,4,6-trichlorobenzoyl valerolactam, pentafluorobenzoyl caprolactam, pentafluorobenzoyl valerolactam, dichlorobenzoyl caprolactam, dimethoxybenzoyl caprolactam, 4-chlorobenzoyl caprolactam, 2,4-dichlororbenzoyl caprolactam, terephthaloyl dicaprolactam, pentafluorobenzoyl caprolactam, pentafluorobenzoyl valerolactam, dichlorobenzoyl valerolactam, dimethoxybenzoyl valerolactam, 4-chlorobenzoyl valerolactam, 2,4-dichlorobenzoyl valerolactam, terephthaloyl divalerolactam, 4-nitrobenzoyl caprolactam, 4-nitrobenzoyl valerolactam, dinitro-benzoyl caprolactam, dinitrobenzoyl valerolactam, and mixtures thereof. The compositions herein may also comprise NOBS, but not as the sole bleach activator present in the bleaching composition.
Particularly preferred are bleach activators selected from the group consisting of benzoyl caprolactam, benzoyl valerolactam, nonanoyl caprolactam, nonanoyl valerolactam, 4-nitrobenzoyl caprolactam, 4-nitrobenzoyl valerolactam, octanoyl caprolactam, octanoyl valerolactam, decanoyl caprolactam, decanoyl valerolactam, undecanoyl caprolactam, undecanoyl valerolactam, 3,5,5-trimethylhexanoyl caprolactam, 3,5,5-trimethylhexanoyl valerolactam, dinitrobenzoyl caprolactam, dinitrobenzoyl valerolactam, terephthaloyl dicaprolactam, terephthaloyl divalerolactam, (6-octanamidocaproyl)oxybenzenesulfonate, (6-nonanamido-caproyl)oxybenzenesulfonate, (6-decanamidocaproyl)oxybenzenesulfonate, benzoyloxybenzenesulfonate, and mixtures thereof.
Preferably, the molar ratio of hydrogen peroxide yielded by the peroxygen bleaching compound to bleach activator is greater than about 1.0. Most preferably, the molar ratio of hydrogen peroxide to bleach activator is at least about 1.5.
The invention also encompasses detergent compositions, especially laundry detergents, comprising otherwise conventional surfactants and other detersive ingredients.
Without limitation by theory, it is believed that dingy soils and stains are the result of combinations of fatty soils and particulate soils. Fatty soils comprise lipids, proteins, and pigments that are deposited on fabrics from contact with human or animal skin. The majority of lipids are secreted from the sebecous gland as sebum. Proteins and pigments from skin fragments are liberated by the breakdown of skin cells. Particulate soils comprise mostly airborne soil and floor/ground dust. It is believed that sebum is the major soil present on laundry, and its removal is important because unremoved fat acts as a matrix to hold particulate soils. Further it is believed that compounds present in the sebum oxidize to contribute to yellowing of fabrics. Particulate soils include topsoil and products produced during the incomplete combustion of petroleum products.
The performance on dingy clean-up can be measured in terms of the Hunter Whiteness Values (W), which is calculated according to the following equation:
W=(7L.sup.2 -40 Lb)/700
wherein L,a,b are determined from a tristimulus meter reading and represent a three axis opponent color scale system based on the theory that color is perceived by black-white (L), red-green (a), and yellow-blue (b) sensations. The higher the value for W, the better the whiteness performance and dingy clean-up. See R. S. Hunter and R. W. Harold, The Measurement of Appearance, Second Ed., John Wiley & Sons, New York, 1987 and ASTM Standards on Color and Appearance Measurement, Third Ed., ASTM, Philadelphia, Pa., 1991.
Compositions of the present invention comprise protease enzyme and bleach activator/bleach compounds at levels such that the Hunter Whiteness Value for the composition is more than additive, i.e., the W for the composition is greater than the sum of the W's for compositions without protease plus the W's for compositions without the bleach activator/bleach compound as determined by a statistically significant number of tests.
Protease enzymes Protease enzymes are usually present in such commercial preparations at levels sufficient to provide at least about 0.005 Anson units (AU) of activity per gram of composition. Therefore, said enzymes comprise at least about 0.001%, preferably from about 0.001% to about 5%, of the detergent compositions.
Suitable examples of proteases are the subtilisins which are obtained from particular strains of B.subtilis, B.lentus and B.licheniforms. Another suitable protease is a modified bacterial serine protease enzyme obtained from Bacillus subtilis or Bacillus licheniformis, having maximum activity throughout the pH range of 8-12, developed and sold by Novo Industries A/S under the registered trade name ESPERASE. The preparation of this enzyme and analogous enzymes is described in British Patent Specification No. 1,243,784 of Novo. Proteolytic enzymes suitable for removing protein-based stains that are commercially available include those sold under the tradenames ALCALASE and SAVINASE by Novo Industries A/S (Denmark) and MAXATASE by International Bio-Synthetics, Inc. (The Netherlands). Other proteases include Protease A (see European Patent Application 130,756, published Jan. 9, 1985) and Protease B (see European Patent Application Serial No. 87303761.8, filed Apr. 28, 1987, and European Patent Application 130,756, Bott et al, published Jan. 9, 1985). Most preferred is what is called herein "Protease C", which is a variant of an alkaline serine protease from Bacillus, particularly Bacillus lentus, in which arginine replaced lysine 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; U.S. Pat. No. 5,185,250, and U.S. Pat. No. 5,204,015. Also preferred are protease which are described in copending application U.S. Ser. No.08/136,797, entitled Protease-Containing Cleaning Compositions and copending application U.S. Ser. No. 08/136,626, entitled Bleaching Compositions Comprising Protease Enzymes, which are incorporated herein by reference. Genetically modified variants, particularly of Protease C, are also included herein.
Bleaching Compounds--Bleaching compositions herein contain bleaching mixtures containing a bleaching agent and one or more bleach activators, in an amount sufficient to provide bleaching of the stain or stains of interest. Bleaching agents will typically be at levels of from about 1% to about 80%, more typically from about 5% to about 20%, of the detergent composition, especially for fabric laundering. Bleach and pre-soak compositions may comprise from 5% to 99% of the bleaching agent. The amount of bleach activators will typically be from about 0.1% to about 60%, more typically from about 0.5% to about 40% of the bleaching mixture comprising the bleaching agent-plus-bleach activator.
The compositions of the present invention may also comprise mixtures of bleaching activators.
Peroxygen bleaching agents, the perborates, the percarbonates, etc., are preferably combined with bleach activators, which lead to the in situ production in aqueous solution (i.e., during the washing process) of the peroxy acid corresponding to the bleach activator.
Alkanoyloxybenzenesulfonates--Suitable alkanoyloxybenzenesulfonate bleach activators which can be employed in the present invention are of the formula: ##STR1## wherein R1 --C(O)-- contains from about 8 to about 12 carbon atoms (provided that when R1 is nonanoyl the compositions herein comprise at least one other bleach activator) and M is a suitable cation, such as an alkali metal, ammonium, or substituted ammonium cation, with sodium and potassium being most preferred.
Highly preferred hydrophobic alkanoyloxybenzenesulfonates are selected from the group consisting of 3,5,5-trimethylhexanoyloxybenzenesulfonate, 2-ethylhexanoyloxybenzenesulfonate, octanoyloxybenzenesulfonate, decanoyloxybenzenesulfonate, dodecanoyloxybenzenesulfonate, and mixtures thereof.
Amido Derived Bleach Activators--The amido derived bleach activators which can be employed in the present invention are amide substituted compounds of the general formulas: ##STR2## or mixtures thereof, wherein R1, R2 and R5 are as defined above and L can be essentially any suitable leaving group. A leaving group is any group that is displaced from the bleaching activator as a consequence of the nucleophilic attack on the bleach activator by the perhydroxide anion. This, the perhydrolysis reaction, results in the formation of the peroxycarboxylic acid. Generally, for a group to be a suitable leaving group it must exert an electron attracting effect. It should also form a stable entity so that the rate of the back reaction is negligible. This facilitates the nucleophilic attack by the perhydroxide anion.
Preferred bleach activators are those of the above general formula wherein R1, R2 and R5 are as defined for the peroxyacid and L is selected from the group consisting of: ##STR3## and mixtures thereof, wherein R1 is an alkyl, aryl, or alkaryl group containing from about 1 to about 14 carbon atoms, R3 is an alkyl chain containing from 1 to about 8 carbon atoms, R4 is H or R3, and Y is H or a solubilizing group.
The preferred solubilizing groups are --SO3 - M+, --CO2 - M+, --SO4 - M+, --N+ (R3)4 X- and O←N(R3)3 and most preferably --SO3 - M+ and --CO2 -M + wherein R3 is an alkyl chain containing from about 1 to about 4 carbon atoms, M is a cation which provides solubility to the bleach activator and X is an anion which provides solubility to the bleach activator. Preferably, M is an alkali metal, ammonium or substituted ammonium cation, with sodium and potassium being most preferred, and X is a halide, hydroxide, methylsulfate or acetate anion. It should be noted that bleach activators with a leaving group that does not contain a solubilizing groups should be well dispersed in the bleaching solution in order to assist in their dissolution.
Preferred bleach activators are those of the above general formula wherein L is selected from the group consisting of: ##STR4## wherein R3 is as defined above and Y is --SO3 - M+ or --CO2 - M+ wherein M is as defined above.
Another important class of bleach activators provide organic peracids as described herein by ring-opening as a consequence of the nucleophilic attack on the carbonyl carbon of the cyclic ring by the perhydroxide anion. For instance, this ring-opening reaction in lactam activators involves attack at the lactam ring carbonyl by hydrogen peroxide or its anion. Since attack of an acyl lactam by hydrogen peroxide or its anion occurs preferably at the exocyclic carbonyl, obtaining a significant fraction of ring-opening may require a catalyst.
Still another class of preferred bleach activators includes the acyl lactam activators, especially acyl caprolactams and acyl valerolactams of the formulae: ##STR5## wherein R6 is H, an alkyl, aryl, alkoxyaryl, or alkaryl group containing from 1 to bout 12 carbon atoms, or a substituted phenyl group containing from about 6 to about 18 carbons. See copending U.S. applications Ser. No. 08/064,562 and 08/082,270, which disclose substituted benzoyl lactams. See also U.S. Pat. No. 4,545,784, issued to Sanderson, October 8, 1985, incorporated herein by reference, which discloses acyl caprolactams, including benzoyl caprolactam, adsorbed into sodium perborate.
Various nonlimiting examples of activators which may also comprise the bleach compositions disclosed herein include those in U.S. Pat. No. 4,915,854, issued Apr. 10, 1990 to Mao et al, and U.S. Pat. No. 4,412,934. See also U.S. Pat. No. 4,634,551 for other typical bleaches and activators useful herein.
Detersive Surfactants--Nonlimiting examples of surfactants useful in detergent compositions herein typically at levels from about 1% to about 55%, by weight, include the conventional C11 -C18 alkyl benzene sulfonates ("LAS") and primary, branched-chain and random C10 -C20 alkyl sulfates ("AS"), the C10 -C18 secondary (2,3) alkyl sulfates of the formula CH3 (CH2)x(CHOSO3 - M+) CH3 and CH3 (CH2)y(CHOSO3 - M+) CH2 CH3 where x and (y+1) are integers of at least about 7, preferably at least about 9, and M is a water-solubilizing cation, especially sodium, unsaturated sulfates such as oleyl sulfate, the C10 -C18 alkyl alkoxy sulfates ("AEx S"; especially EO 1-7 ethoxy sulfates), C10 -C18 alkyl alkoxy carboxylates (especially the EO 1-5 ethoxycarboxylates), the C10-18 glycerol ethers, the C10 -C18 alkyl polyglycosides and their corresponding sulfated polyglycosides, and C12 -C18 alpha-sulfonated fatty acid esters. If desired, the conventional nonionic and amphoteric surfactants such as the C12 -C18 alkyl ethoxylates ("AE") including the so-called narrow peaked alkyl ethoxylates and C6 -C12 alkyl phenol alkoxylates (especially ethoxylates and mixed ethoxy/propoxy), C12 -C18 betaines and sulfobetaines ("sultaines"), C10 -C18 amine oxides, and the like, can also be included in the overall compositions. The C10 -C18 N-alkyl polyhydroxy fatty acid amides can also be used. Typical examples include the C12 -C18 N-methylglucamides. See WO 9,206,154. Other sugar-derived surfactants include the N-alkoxy polyhydroxy fatty acid amides, such as C10 -C18 N-(3-methoxypropyl) glucamide. The N-propyl through N-hexyl C12 -C18 glucamides can be used for low sudsing. C10 -C20 conventional soaps may also be used. If high sudsing is desired, the branched-chain C10 -C16 soaps may be used. Mixtures of anionic and nonionic surfactants are especially useful. Other conventional useful surfactants are listed in standard texts.
Examples of carbonate builders are the alkaline earth and alkali metal carbonates as disclosed in German Pat. Application No. 2,321,001 published on Nov. 15, 1973.
M.sub.z (zAlO.sub.2)y!·xH.sub.2 O
Na.sub.12  (AlO.sub.2).sub.12 (SiO.sub.2).sub.12 !·xH.sub.2 O
Enzymes--Optional enzymes can be included in the formulations herein for a wide variety of fabric laundering purposes, including removal of protein-based, carbohydrate-based, or triglyceride-based stains, for example, and for the prevention of refugee dye transfer, and for fabric restoration. The enzymes to be incorporated include amylases, lipases, cellulases, and peroxidases, as well as mixtures thereof Other types of enzymes may also be included. They may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. However, their choice is governed by several factors such as pH-activity and/or stability optima, thermostability, stability versus active detergents, builders and so on. In this respect bacterial or fungal enzymes are preferred, such as bacterial amylases and fungal cellulases.
Enzymes are normally incorporated at levels sufficient to provide up to about 5 mg by weight, more typically about 0.01 mg to about 3 mg, of active enzyme per gram of the composition. Stated otherwise, the compositions herein will typically comprise from about 0.001% to about 5%, preferably 0.01%-1% by weight of a commercial enzyme preparation.
The most preferred soil release and anti-redeposition agent is ethoxylated tetraethylenepentamine. Exemplary ethoxylated amines are further described in U.S. Pat. No. 4,597,898, VanderMeer, issued Jul. 1, 1986. Another group of preferred clay soil removal-antiredeposition agents are the cationic compounds disclosed in European Pat. Application 111,965, Oh and Gosselink, published Jun. 27, 1984. Other clay soil removal/antiredeposition agents which can be used include the ethoxylated amine polymers disclosed in European Pat. Application 111,984, 25 Gosselink, published Jun. 27, 1984; the zwitterionic polymers disclosed in European Patent Application 112,592, Gosselink, published Jul. 4, 1984; and the amine oxides disclosed in U.S. Pat. No. 4,548,744, Connor, issued Oct. 22, 1985. Other clay soil removal and/or anti redeposition agents known in the art can also be utilized in the compositions herein. Another type of preferred antiredeposition agent includes the carboxy methyl cellulose (CMC) materials. These materials are well known in the art.
Specific examples of optical brighteners which are useful in the present compositions are those identified in U.S. Pat. No. 4,790,856, issued to Wixon on Dec. 13, 1988. These brighteners include the PHORWHITE series of brighteners from Verona. Other brighteners disclosed in this reference include: Tinopal UNPA, Tinopal CBS and Tinopal 5BM; available from Ciba-Geigy; Artic White CC and Artic White CWD, available from Hilton-Davis, located in Italy, the 2-(4-stryl-phenyl)-2H-napthol 1,2-d!triazoles; 4,4'-bis- (1,2,3-triazol-2-yl)-stil- benes; 4,4'-bis(stryl)bisphenyls; and the aminocoumarins. Specific examples of these brighteners include 4-methyl-7-diethyl- amino coumarin; 1,2-bis(-venzimidazol-2-yl)ethylene; 1,3-diphenyl-phrazolines; 2,5-bis(benzoxazol-2-yl)thiophene; 2-stryl-napth- 1,2-d!oxazole; and 2-(stilbene-4-yl)-2H-naphtho- 1,2-d!triazole. See also U.S. Pat. No. 3,646,015, issued Feb. 29, 1972 to Hamilton. Anionic brighteners are preferred herein.
The detergent compositions herein may also contain non-surfactant suds suppressors. These include, for example: high molecular weight hydrocarbons such as paraffin, fatty acid esters (e.g., fatty acid triglycerides), fatty acid esters of monovalent alcohols, aliphatic C18 -C40 ketones (e.g., stearone), etc. Other suds inhibitors include N-alkylated amino triazines such as tri- to hexa-alkylmelamines or di- to tetra-alkyldiamine chlortriazines formed as products of cyanuric chloride with two or three moles of a primary or secondary amine containing 1 to 24 carbon atoms, propylene oxide, and monostearyl phosphates such as monostearyl alcohol phosphate ester and monostearyl di-alkali metal (e.g., K, Na, and Li) phosphates and phosphate esters. The hydrocarbons such as paraffin and haloparaffin can be utilized in liquid form. The liquid hydrocarbons will be liquid at room temperature and atmospheric pressure, and will have a pour point in the range of about -40° C. and about 50° C., and a minimum boiling point not less than about 110° C. (atmospheric pressure). It is also known to utilize waxy hydrocarbons, preferably having a melting point below about 100° C. The hydrocarbons constitute a preferred category of suds suppressor for detergent compositions. Hydrocarbon suds suppressors are described, for example, in U.S. Pat. No. 4,265,779, issued May 5, 1981 to Gandolfo et al. The hydrocarbons, thus, include aliphatic, alicyclic, aromatic, and heterocyclic saturated or unsaturated hydrocarbons having from about 12 to about 70 carbon atoms. The term "paraffin" as used in this suds suppressor discussion, is intended to include mixtures of true paraffins and cyclic hydrocarbons.
Other Ingredients--A wide variety of other ingredients usefull in detergent compositions can be included in the compositions herein, including other active ingredients, carriers, hydrotropes, processing aids, dyes or pigments, solvents for liquid formulations, solid fillers for bar compositions, etc. If high sudsing is desired, suds boosters such as the C10 -C16 alkanolamides can be incorporated into the compositions, typically at 1%-10% levels. The C10 -C14 monoethanol and diethanol amides illustrate a typical class of such suds boosters. Use of such suds boosters with high sudsing adjunct surfactants such as the amine oxides, betaines and sultaines noted above is also advantageous. If desired, soluble magnesium salts such as MgCl2, MgSO4, and the like, can be added at levels of, typically, 0.1%-2%, to provide additional suds and to enhance grease removal performance.
To illustrate this technique in more detail, a porous hydrophobic silica (trademark SIPERNAT D10, DeGussa) is admixed with a proteolytic enzyme solution containing 3%-5% of C13 -C15 ethoxylated alcohol (EO 7) nonionic surfactant. Typically, the enzyme/surfactant solution is 2.5 X the weight of silica. The resulting powder is dispersed with stirring in silicone oil (various silicone oil viscosities in the range of 500-12,500 can be used). The resulting silicone oil dispersion is emulsified or otherwise added to the final detergent matrix. By this means, ingredients such as the aforementioned enzymes, bleaches, bleach activators, bleach catalysts, photoactivators, dyes, fluorescers, fabric conditioners and hydrolyzable surfactants can be "protected" for use in detergents, including liquid laundry detergent compositions.
The N--O group can be represented by the following general structures: ##STR6## wherein R1, R2, R3 are aliphatic, aromatic, heterocyclic or alicyclic groups or combinations thereof, x, y and z are 0 or 1; and the nitrogen of the N--O group can be attached or form part of any of the aforementioned groups. The amine oxide unit of the polyamine N-oxides has a pKa<10, preferably pKa<7, more preferred pKa<6.
The hydrophilic optical brighteners useful in the present invention are those having the structural formula: ##STR7## wherein R1 is selected from anilino, N-2-bis-hydroxyethyl and NH-2-hydroxyethyl; R2 is selected from N-2-bis-hydroxyethyl, N-2-hydroxyethyl-N-methylamino, morphilino, chloro and amino; and M is a salt-forming cation such as sodium or potassium.
A bleach composition is as follows:
______________________________________Ingredient              % (Wt.)______________________________________Sodium Percarbonate     20.0(6-nonanamidocaproyl)oxybenzenesulfonate                   10.0Protease Enzyme*        1.0Water-soluble filler**  Balance______________________________________ *Protease C **Sodium carbonate, sodium silicate mixture (1:1).
The compositions of Example I can be used per se as a bleach, or can be added to a pre-soak or surfactant-containing detergent composition to impart a bleaching benefit thereto. Fabrics exposed to the compositions of Example I exhibit more performance benefits on dingy soils than the added single contributions of bleach and protease would predict.
1. A bleaching composition which provides dingy clean up, comprising
a) at least about 0.001% by weight of a protease enzyme selected from the group consisting of a protease enzyme having N76D/S103A/V104I subtilisin variant derived from Bacillus lentus subtilisin, a protease enzyme having K27R/V104I/N123S/
T274A subtilisin variant derived from Bacillus lentus subtilisin and mixtures thereof;
b) from about 1% to about 75% by weight of a bleaching compound capable of yielding hydrogen peroxide in a liquid; and
c) from about 0.1% to about 50% by weight of one or more bleach activators selected from the group consisting of:
i) alkanoyloxybenzenesulfonate bleach activators;
ii) an amido-derived bleach activator of the general formula: ##STR8## or mixtures thereof, wherein R1 is an alkyl, aryl or alkaryl group containing from about 1 to about 14 carbon atoms, R2 is an alkylene, arylene, or alkyarylene group containing from about 1 to about 14 carbon atoms, R5 is H or an alkyl, aryl or alkaryl group containing from about 1 to about 10 carbon atoms, and L is a leaving group;
iii) N-acyl lactam bleach activators of the formula: ##STR9## wherein n is from 0 to about 8 and R6 is H, an alkyl, alkoxyaryl or alkaryl group containing from 1 to 12 carbon atoms, or a substituted phenyl group containing from about 6 to about 18 carbon atoms;
iv) mixtures of i), ii) and iii); and.
2. A bleaching composition according to claim 1 wherein said bleaching compound is percarbonate or perborate or mixtures thereof, said bleach activator is selected from the group consisting of benzoyl caprolactam, benzoyl valerolactam, nonanoyl caprolactam, nonanoyl valerolactam, 4-nitrobenzoyl caprolactam, 4-nitrobenzoyl valerolactam, octanoyl caprolactam, octanoyl valerolactam, decanoyl caprolactam, decanoyl valerolactam, undecanoyl caprolactam, undecanoyl valerolactam, 3,5,5-trimethyl-hexanoyl caprolactam, 3,5,5-trimethyl-hexanoyl valerolactam, dinitrobenzoyl caprolactam, dinitrobenzoyl valerolactam, terephthaloyl dicaprolactam, terephthaloyl divalerolactam, (6-octanamidocaproyl)oxybenzenesulfonate, (6-nonanamido-caproyl)oxybenzenesulfonate, (6-decanamidcaproyl)oxybenzene sulfonate, benzoyloxybenzenesulfonate and mixtures thereof.
3. A bleaching composition which provides dingy clean up, comprising at least about 0.001% to about 5% by weight of a proteases enzyme selected from the group consisting of a protease enzyme having N76D/S103A/V104I subtilisin variant derived from Bacillus lentus subtilisin, a protease enzyme having K27R/V104I/N123S/T274A subtilisin variant derived from Bacillus lentus subtilisin and mixtures thereof, from about 1% to about 75% by weight of a bleaching compound capable of yielding hydrogen peroxide in a aqueous liquor and selected from the group consisting of perborates, percarbonates and mixtures thereof, and from about 0.1% to about 50% by weight one or more bleach activators selected from the group consisting of acyl caprolactams, acyl valerolactams, (6-octanamidocaproyl)oxybenzenesulfonate, (6-nonanamidocaproyl)oxybenzenesulfonate, (6-decanamidcaproyl)oxybenzene sulfonate and mixtures thereof.
4. A composition according to claim 3 wherein said composition further comprises an alkanoyloxybenzenesulfonate bleach activator.
5. A composition according to claim 3 wherein said composition further comprises a detersive surfactant.
US08931684 1993-10-14 1997-09-16 Bleach compositions comprising protease enzyme Expired - Fee Related US5932532A (en)
US08322677 US5677272A (en) 1993-10-14 1994-10-13 Bleaching compositions comprising protease enzymes
US08931684 US5932532A (en) 1993-10-14 1997-09-16 Bleach compositions comprising protease enzyme
US08322677 Continuation-In-Part US5677272A (en) 1993-10-14 1994-10-13 Bleaching compositions comprising protease enzymes
US5932532A true US5932532A (en) 1999-08-03
ID=27384899
US08931684 Expired - Fee Related US5932532A (en) 1993-10-14 1997-09-16 Bleach compositions comprising protease enzyme
US (1) US5932532A (en)
US6352562B1 (en) * 1993-05-20 2002-03-05 The Procter & Gamble Co. Method of cleaning fabrics using bleaching compounds comprising substituted benzoyl caprolactam bleach activators
US20060205626A1 (en) * 2005-03-11 2006-09-14 Gant Robert G Cleaning compound for a medical or dental office
US20070207940A1 (en) * 2006-02-10 2007-09-06 Gyorgyi Fenyvesi Detergent compositions comprising renewably-based, biodegradable 1,3-propanediol
WO2007118618A1 (en) * 2006-04-13 2007-10-25 Henkel Ag & Co. Kgaa Bleaching agents containing piperidones
WO2010039961A1 (en) * 2008-10-03 2010-04-08 E.I. Dupont De Nemours And Company Enzymatic peracid production using a cosolvent
US20150013075A1 (en) * 2013-07-10 2015-01-15 Whirlpool Corporation Method of sanitization in a laundry treating appliance
AU7228187A *
EP0247421A2 (en) * 1981-11-10 1987-12-02 THE PROCTER &amp; GAMBLE COMPANY Detergent compositions and washing liquors for use in textile laundering processes
US4770815A (en) * 1986-10-24 1988-09-13 The Procter & Gamble Company Detergent plus softener with imidazoline ingredient
US4861509A (en) * 1986-12-10 1989-08-29 Lever Brothers Company Enzymatic detergent and bleaching composition
EP0350096A2 (en) * 1988-07-04 1990-01-10 Unilever N.V. Bleaching detergent compositions
US4927558A (en) * 1986-11-25 1990-05-22 Novo Industri A/S Proteolytic detergent additive and compositions containing the same
EP0416967A1 (en) * 1989-08-11 1991-03-13 Mitsubishi Gas Chemical Company, Inc. Novel alkaline protease
US5002687A (en) * 1989-04-13 1991-03-26 Lever Brothers Company, Division Of Conopco, Inc. Fabric washing compositions
US5053333A (en) * 1988-01-27 1991-10-01 M & D Research Co., Ltd. Protease
US5215907A (en) * 1989-02-24 1993-06-01 Oklahoma Medical Research Foundation Thermostable acid protease from sulfolobus acidocaldarius
US5244791A (en) * 1984-05-29 1993-09-14 Genecor International, Inc. Methods of ester hydrolysis
US5837010A (en) * 1994-11-18 1998-11-17 Procter & Gamble Company Detergent compositions containing a lipase variant at low levels
"Protein Engineering as a Tool to Obtain Better Proteases for Use in Detergents", J.H. Van Ee, Chimicaoggi, Jul.-Aug. 1991.
Protein Engineering as a Tool to Obtain Better Proteases for Use in Detergents , J.H. Van Ee, Chimicaoggi, Jul. Aug. 1991. *
U.S. application no. 08/064,562, A. D. Willey, filed May 20, 1993. *
U.S. application no. 08/064,623, A. D. Willey et al, filed May 20, 1993. *
U.S. application no. 08/064,624, A. D. Willey et al, filed May 20, 1993. *
U.S. application no. 08/082,270, A. D. Willey et al, filed Jun. 24, 1993. *
U.S. application no. 08/136,518, D. N. DiGuilio et al, filed Oct. 14, 1993. *
U.S. application no. 08/136,626, M. E. Burns et al, filed Oct. 14, 1993. *
U.S. application no. 08/136,797, C. K. Ghosh et al, filed Oct. 14, 1993. *
U.S. application no. 08/151,085, M. E. Burns et al, filed Nov. 12, 1993. *
U.S. application no. 08/196,322, M. E. Burns et al, filed Feb. 15, 1994. *
USSN 07/938,666, Nicholson, Aug. 31, 1992. *
US9375390B2 (en) 2006-02-10 2016-06-28 Dupont Tate & Lyle Bio Products Company, Llc Agricultural compositions comprising renewably-based biodegradable 1,3-propanediol
US8802729B2 (en) 2006-02-10 2014-08-12 Dupont Tate & Lyle Bio Products Company, Llc Enzyme stabilized detergent compositions
US8436046B2 (en) 2006-02-10 2013-05-07 Dupont Tate & Lyle Bio Products Company, Llc Detergent composition containing bio-derived 1,3-propanediol and its conjugate esters