Classifications

• • B—PERFORMING OPERATIONS; TRANSPORTING
  • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
  • B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
  • B01J31/00—Catalysts comprising hydrides, coordination complexes or organic compounds
  • B01J31/003—Catalysts comprising hydrides, coordination complexes or organic compounds containing enzymes
• • C—CHEMISTRY; METALLURGY
  • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
  • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
  • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
  • C11D3/16—Organic compounds
  • C11D3/38—Products with no well-defined composition, e.g. natural products
  • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
  • C11D3/38618—Protease or amylase in liquid compositions only
• • C—CHEMISTRY; METALLURGY
  • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
  • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
  • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
  • C11D3/16—Organic compounds
  • C11D3/38—Products with no well-defined composition, e.g. natural products
  • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
  • C11D3/38663—Stabilised liquid enzyme compositions
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
  • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
  • C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates

Definitions

• ABSTRACT Aqueous amylolytic enzyme-containing compositions comprising water, amylolytic enzyme, a water-soluble calcium salt, an organic co-stabilizing agent selected from aliphatic glycols and 1,3-propanediol and, optionally, a nonionic or zwitterionic detergent are disclosed.
• the compositions, useful as starch-degrading compositions, are stabilized substantially against loss of amylolytic enzyme activity during storage.
• amylolytic enzymes in the alteration and- /or degradation of starchy materials is known.
• US. Pat. No. 2,607,359 (Aug. 19,1962) describes compositions containing an amylolytic enzyme useful in facilitating the removal of porous materials such as wallpapers, labels and casein type pastes from surfaces to which the porous materials are held by a starch-containing adhesive.
• Jaag in Seifen, Ole, Fette, Wachse 88, No. 24, pp. 789-793, (Nov. 1962) describes the use of amylolytic enzymes in laundry formulations. These enzymes aid in the laundry process by attacking starchy soils and stains found on soiled fabrics and decomposing and/or altering them so as to render them more removable during laundering.
• Enzymatic materials are expensive and powerful materials which must be judiciously formulated and used. These enzymes when employed in aqueous compositions are unstable and suffer appreciable destruction during long periods of storage as evidenced by substantial loss in starch-degrading and/or soiland stainremoving efficacy. The loss in amylolytic activity is particularly severe under conditions of high temperature. Furthermore, aqueous laundering solutions containing amylolytic enzymes often contain additional components desirable in the laundering process but which have an adverse effect on the amylolytic enzyme. Proteolytic enzymes, for example, while useful in providing proteinaceous soiland stain-removing properties in laundering compositions, often tend to have such an adverse degrading effect on amylolytic enzymes.
• lt is another object of this invention to provide aqueous amylolytic enzyme-containing compositions stabilized substantially against loss of activity by the presence of minor amounts of enzyme-stabilizing compounds.
• aqueous amylolytic enzyme-containing compositions containing minor amounts of calcium ion and certain organic costabilizing agents.
• the aqueous compositions of the present invention can additionally contain nonionic or zwitterionic detergent components to enhance the stability of the amylolytic enzymes in the aqueous compositions of this invention and to enhance the detergent properties of these compositions.
• the present invention is based in part on the discovery that extended periods of stabilization can be achieved by introducing into aqueous enzyme-containing compositions a source of calcium ion and an organic compound selected from the group consisting of aliphatic glycols and 1,3- propane diol.
• the stabilized aqueous enzyme-containing compositions of this invention comprise 1. from about to about 97 percent water;
• amylolytic enzymes which can be stabilized in aqueous solution by the action of the hereinbefore described combination of calcium ion and organic compound are known materials and can be of fungal, plant, animal or bacterial-origin.
• Suitable amylolytic enzymes include the a-amylases which are particularly well suited for breaking down starch molecules as they attack the a -glycosidic linkages in starch. The degraded short chains are easily removed from their environment with water or aqueous solutions of detergents.
• amylolytic enzymes include the a-amylases of mold origin including those derived from Aspergillus oryzae, Aspergillus niger, Aspergillus alliaceus, Aspergillus wentii, and Pencillium glaucum.
• a-amylases of mold origin including those derived from Aspergillus oryzae, Aspergillus niger, Aspergillus alliaceus, Aspergillus wentii, and Pencillium glaucum.
• a-amylases derived from cereal grains, pancreatic sources and such bacteria as Bacillus subtilis Bacillus macerans, Bacillus mesentericus and Bacillus thermophilus are also useful herein. These enzymes are active in the pH range of from about 4.5 to about 10 and at temperatures from about 60F. to about F. Optimum activity of these a-amylases is generally exhibited in the pH range of from about 5.5 to about 7.5.
• Preferred amylolytic enzymes herein are the a-amylases derived from the bacterial organism Bacillus subtilis. These amylases provide excellent desizing and starch digestive properties and are especially useful in the laundering of textile materials containing soils and stains of a starchy nature.
• amylolytic enzymes useful herein can be employed in a pure state. Generally they are employed in the form of a powdered commercially available preparation wherein the amylolytic enzyme is present in an amount of from about 2 to about 80 percent of the preparation. The remaining portion, i.e. about to about 98 percent, comprises inert vehicle such as sodium sulfate, calcium sulfate, sodium chloride, clay or the like. In preparing the stabilized aqueous starchdegrading compositions of this invention, such commercial enzyme preparations are admixed with water and the remaining components of the compositions.
• the active enzyme content of these commercial enzyme compositions is the result of manufacturing methods employed and is not critical herein so long as the finished compositions of this invention have the hereinafter specified enzyme content.
• Insoluble inert materiby methods known in the art so long as the stabilized compositions of the invention provide an amount of amylolytic enzyme activity sufficient to provide desirable levels of starch degrading properties.
• amylolytic activity refers to the tendency of an amylolytic enzyme to perform the desired function of catalytic alteration and/or degradation of starchy materials
• Stability refersto the tendency of an amylolytic enzyme to retain its enzymatic activity.
• the activity level of amylolytic enzyme suitable herein can be determined by-numerous methals are generally removed from the compositions of this invention to provide aqueous compositions which are clear and substantially free of precipitated deposits.
• Specific examples of commercial enzyme preparations suitable for use herein and the manufacturers thereof include: Diasmen c r-amylase (Daiwa Kasei K. K.
• Rapidase a-amylase' THC- (Rapidase, Seclin, France); Novo Bacterial a-amylase (Novo Industri, Copenhagen, Denmark); Wallerstein a-amylase (Wallerstein Company, Staten Island, New York); Rhozyme-33 and Rhozyme H-39 (Rohm & Haas, Philadelphia, Pennsylvania).
• Preferred herein is a powdered enzyme preparation containing a-amylase and amixture of alkaline and neutral proteases available as CRD-Protease (or Monsanto DA-lO) from Monsanto Company, St. Louis, Missouri.
• This composition contains about 3 a-amylase and is useful herein to provide the compositions of the invention with amylolytic and proteolytic enzyme activity.
• Mixtures of proteases and 'a-amylases are preferred herein and include the enzyme preparations described in US. Pat. No, 3,031,380 to Minagawa et al. (Apr. 24, 1962).
• amylolytic enzyme employed'in the compositions of this invention can vary depending.
• the stabilized aqueous compositions of this invention When employed as spot removers, they should contain an amount of amylolytic enzyme sufficient to remove the starchy soils and stains normally encountered in a laundering situation.
• the compositions of this invention are prepared to contain from about 0.001 to about l-percent enzyme by weight of the aqueous composition on a pure enzyme basis.
• the compositions preferably contain from about 0.01 to about 0.5 percent amylolytic enzyme.
• compositions of this invention contain from about 0.1 to about 4.0 percent of the powdered amylo lytic enzyme-containing preparation as it is available in commercial form e.g., containing from' about 2 to about 80 percent active enzyme. It will be appreciated that when such preparations are employed herein, the amount of the preparation required to provide aqueous compositions having desirable levels of amylolytic activity will depend on the activity level of the enzymecontaining preparation employed. The precise amounts of such materials employed can be readily determined ods. Asuitable method is the 3,5-dinitrosalicylate assay method.
• a sample of amylase is allowed to catalyze the hydrolysis of the 1,4- a-glycosidic bonds of starch and glycogens for five minutes at a temperature of 37C. at a pH of 6.0.
• the reaction is terminated by the addition of buffered sodium 3,5-dinitrosalicylate, the color is developed and the amount of maltose determined by spectrophotometric response and comparison with solutions of analytical grade maltose hydrate.
• the amylase has one activity unit for each 0.4 mg. of maltose hydrate produced during hydrolysis under the specified conditions.
• the amylase activity method is well known and is described with particularly in P. Bemfeld, Methods in Enzymol. Vol I. p. 149 (1955).
• the present invention is based in'part upon the surprising discovery that extended periodsof enzyme stabilization can be achieved by incorporating in'toaqueous enzyme solutions acombination of water-soluble calcium salt and organic co- 7 stabilizing compound hereinbefore described.
• the water-soluble salts of calcium include, for example, calcium chloride, calcium acetate, calcium citrate, calcium glycerol phosphate, calcium gluconate, calcium glucoheptanate, calcium lactate, calcium levulinate, calcium lactobionate, calcium malate, calcium lactophosphate, calcium succinate, calcium maleate, and calcium sulfate.
• the stabilized compositions of the invention are-prepared to contain from about 0.001 to about l percent of the stabilized composition with respect to the calcium ion. Preferably from about 0.005 to about 0.05 percent with respect to the calcium ion,
• certain of the commercially available enzyme I preparations suitable herein contain, in addition to active enzyme, certain inert materialsincluding for example, calcium chloride or calcium sulfate. When such an enzyme preparation is employed as the source of amy-' lolytic enzyme, an amount of calcium ion is also incorporated thereby.v Additional calcium ion is conveniently provided by the addition of one or more of the calcium salts hereinbefore described so as to provide a level of calcium ion within'the hereinbefore described range.
• Preferred calcium salts include calcium acetate,
• the organic co-stabilizers which in concert with cal cium ion provide enhanced amylolytic enzyme activity include the aliphatic glycols and l,3-propanediol.
• the aliphatic glycols employed herein have the formula norcn cn o' a wherein x-is from 1 to about 200, and include ethylene glycol and the polyethylene glycols.
• the polyethylene glycols useful herein are those wherein'x in the hereinbefore described formula ranges from 2 to about 200 andv include diethylene glycol, triethylene glycol and the corresponding polymers of ethylene oxide wherein the average number of oxyethylene groups ranges upward from 4 (tetraethylene glycol) to about 200.
• the aliphatic glycols useful herein range in consistency from light liquids to white waxy solids and dissolve in water to form clear solutions.
• Preferred aliphatic glycols herein include diethylene glycol and triethylene glycol.
• These polyethylene glycols have average molecular weights of about 200 to about 3500 and are commercially available under the trade designation Carbowax with numerical designation referring to average molecular weight, e.g. 200, 400, 600, 1000, or the like.
• the upward numerical gradation corresponds to increasing molecular weight, increasing melting point and decreasing water-solubility.
• Mixtures of aliphatic glycols of the invention can be employed herein.
• 1,3-propanediol also provides an amylolytic enzyme-stabilizing effect as hereinbefore described.
• This compound is a preferred co-s'tabilizing agent herein and provides excellent stabilizing effects.
• organic amylolytic enzyme co-stabilizing compounds of this invention are employed in minor but effective' amounts ranging from about 2 to about 27 percent by weight of the composition.
• the stabilized compositions are prepared to contain from about 5 to about percent by weight of the co-stabilizing agent. The latter range is preferred from the standpoint of optimum stabilizing effects, particularly over long storage periods at high temperatures.
• Nonionic and zwitterionic detergents can be employed, as optional ingredients, in the compositions of this invention. These detergents enhance considerably the storage stability of the amylolytic en- 1 zymes employed herein and significantly improve the detergent characteristics of the composition. Because of these useful characteristics it is preferred to include nonionic and zwitterionic detergents in the aqueous en zyme compositions of the invention.
• the nonionics and zwitterionics can be utilizedherein in amounts ranging from 0 to about 15 percent, and preferably from 4 to 10 percent, by weight of the enzyme-containing composition.
• Suitable nonionics for use herein include:
• the polyethylene oxide condensates of alkyl phenols, e.g., the condensation products of alkyl phenols having an alkyl group containing from about six to 12 carbon atoms in either a straight chain or branched chain configuration with ethylene oxide, the said ethylene oxide being present in amounts equal to 5 to moles of ethylene oxide per mole of alkyl phenol.
• the alkyl substituent in such compounds may be derived from polymerized propylene, diisobutylene, octene or nonene, for example. 2.
• Those nonionic synthetic detergents derived from the condensation of ethylene oxide with the product resulting from the reaction of propylene oxideand ethylene diamine.
• acyl moieties are normally derived from naturally occurring glycerides (e.g., coconut oil, palm oil, soybean oil and tallow), but can be derived synthetically (e.g., by the oxidation'of petroleum, or by hydrogenation of carbon monoxide by the Fischer-Tropsch process).
• glycerides e.g., coconut oil, palm oil, soybean oil and tallow
• RRIRIIP V Long chain tertiary amine oxides corresponding to the following general formula RRIRIIP V,
• R is an, alkyl, alkenyl or monohydroxyalkyl radical ranging from 10 to 22 carbon atoms in chain length and R and R" are each alkyl .or monohydroxyalkyl groups containing from one to three carbon atoms.
• the arrow in the formula is a conventional representation of a semi-polar bond.
• suitable phosphine oxides are found in US. Pat. No. 3,304,263 which issued Feb. 14, 1967, and include: dimethyldodecylphosphine oxide and bis-( 2-hydroxyethyl)- dodecylphosphine oxide.
• R is an alkyl radical containing from about 10 to about 22 carbon atoms, from 0 to about 5 ether linkages and from 0 to about 2 hydroxyl substituents, at least one moiety of R being uninterrupted by ether linkages and containing from about 10 to about 18 car- 7 straight chain or branched, and wherein one of the aliphatic substituents contains from about eight to 22 carbon atoms and one contains an anionic water solubilizing-group, e.g., carboxy, sulfo, sulfato, phosphate or phosphono.
• Examples of compounds falling within this definition are 3-( N,N-dimethyl-N-hexadecylammonio) propane-l-sulfonate and 3-(N,N-dimethyl-N- hexadecylammonio )-2-hydroxypropanel-sulfonate.
• zwitterionic synthetic detergents see Diehl and Smith, Laundering Fabrics in Cold Water Containing a Synthetic Detergent Composition, Canadian Patent No. 708,147 issued Apr. 20, 1965 at page 6, lines 1 22. This disclosure is specifically incorporated herein by reference.
• Nonionic detergents or mixtures of nonionic detergents and zwitterionic detergents can be employed.
• Preferred herein are the condensation products of 1 mole of aliphatic alcohol having eight to 22 carbon atoms with from 5 to 40 moles of ethylene oxide, e.g. tallow alcohol ethoxylated with 11 or 30 moles of ethylene oxide and coconut alcohol ethoxylated with 6 moles of ethylene oxide.
• Also preferred are the 3-(N,N-dimethyl-N-alkylammonio)-2- hydroxypropane-l-sulfonates wherein the alkyl has from eight to 22 carbon atoms, e.g.
• compositions of the present invention are prepared to contain from about 65 to about 97 percent by weight of water. Preferably from about 72 to about 95 percent is employed. Demineralized water is preferred, although not mandatory for use herein.
• the various components of the enzyme compositions of this invention can be mixed together in any order. However, it is preferred that a stabilizer-water mixture be prepared first and the enzymes added thereto to prevent any degradation or deactivation which might occur by adding the enzyme to water which does not contain the enzyme-stabilizing combination of the invention.
• the optional detergent components can be added at any time.
• the pH of the stabilized aqueous enzyme compositions of this invention generally ranges from about 5.0 to 10.0 and preferably ranges from about 6.5 to about 8.5. Maximum stabilizing affects are obtained in the preferred pH range.
• the pH can be raised with a base, e.g., sodium or potassium hydroxide, or lowered with an acid, e.g., hydrochloric acid.
• a preservative be added to the compositions to prevent bacterial and fungal growth.
• Phenyl mercuric acetate which is generally utilized herein in amounts ranging from about 10 to about 40 parts per million of the compositions is an effective preservative. Any preservative compatible with the components of the compositions can be utilized herein.
• the stabilized aqueous compositions of this invention can also contain any of the usual detergent adjuvents, diluents and additives so long as they do not substantially interfere with the activity of the enzymatic components.
• perfumes, anti-tamishing agents, inert salts such as sodium sulfate, anti-redeposition agents, bacten'ostatic agents, dyes, fluorescers, suds builders, suds depressors, and the like can be utilized herein without detracting from the advantageous prop erties of'these compositions. It is preferred that the compositions of the present invention contain in addition certain proteolytic enzymes.
• proteolytic enzymes include the alkaline proteases, neutral proteases, and acid proteases which aid materially the removal of proteinaceous soils and stains from laundered textiles.
• the employment of proteolytic enzymes in combination with the amylolytic enzymes of the present invention is preferred from the standpoint of facilitating the removal of a broad spectrum of varied soils and stains.
• the preferred proteolytic enzymes are the subtilisins, obtained from the bacterial organism, Bacillus subtilis.
• proteolytic enzymes are included in the compositions of the present invention, it is desirable to include any of the known proteolytic enzyme-stabilizing materials known in the art to thereby enhance proteolytic enzyme activity upon storage. Suitable proteolytic enzyme stabilizing materials are described for example in Ser. No. 683,196, entitled Stabilized Aqueous Enzyme Preparation filed Nov. 15, 1967 by Charles Bruce McCarty.
• compositions of this invention can be employed as spot removers, detergent additives'or as detergent cleaning compositions per se. Thesecompositions can EXAMPLES
• the following examples merely serve to illustrate the invention in specific detail and when read in conjunction with the foregoing description will aid in determining the full scope of the present invention. The examples are merely illustrative and are not intended to restrict this invention. All parts, percentages and ratios set forth herein are by weight unless otherwise indicated.
• compositions were prepared and stored in closed glass bottles for the lengths of time indicated in Table I.
• Each composition containined 10 percent by weight of the organic co-stabilizing agent; 1 percent Monsanto CRD-Protease (a commercially available mixture of proteases and amylases derived from Bacillus subtilis); and 89 percent of an aqueous stock solution containing 0.01 percent calcium acetate monohydrate and 0.29 percent sodium chloride.
• the amylolytic activity of each composition was measured at the stated intervals by the assay method hereinbefore described.
• Control samples stored under identical conditions were also evaluated for retention of enzymatic activity.
• no organic co-stabilizing agent was employed in the case of Control-1.
• no organic costabilizing agent was present in the case of Control-2, no organic costabilizing agent was present and thestock solution was replaced with distilled water, i.e., no calcium acetate monohydrate or sodium chloride was present. The results are tabulated as follows:
• ionic or zwitterionic was added and the enzyme was added last.
• the enzymes employed were Alcalase (a proteolytic enzyme preparation havinga crystalline enzyme content of about 6 percent and derived from Bacillus subtilis); and/or Monsanto CRD-Protease (a mixture of proteolytic and amylolytic enzymes derivedv from Bacillus subtilis). Ethanol, where present, was employed as a stabilizer for the proteolytic enzyme.
• an aqueous stock solution, hereinbefore described was employed in an amount to bring the balance of the composition to 100 percent.
• the composi- 'tions were stored for the periods of time indicated in Table II at a temperature of 100F.
• compositions of Examples 4 to 29 perform well as spot removers, as additives to detergent compositions and as'laundry detergents per se.
• EXAMPLE 30 A stabilized aqueous enzyme composition is formu-v lated according to this invention from the following components:
• Thiscomposition can be employed without dilution V as a soiland stain-removing composition to remove or facilitate removal of starchy and proteinaceous matter from textile materials.
• the soiland stain-removing efficacy is demonstrated even after extended periods of storage (8 weeks) at elevated temperature (120F.).
• composition of this example can be employed as an additive to commercial detergent formulations. When about 1.2 ml. of the composition is added per gallon of washing solution, excellent soiland stain-- removing properties are demonstrated.
• a stabilized aqueous enzyme composition consisting essentially of by weight of the composition:
• composition of claim I wherein the costabilizing compound is an aliphatic alcohol having the formula wherein is from about 2 to about 200; and wherein the amylolytic enzyme is an a-amylase characterized by amylolytic activity in the pH range of from about 4.5 to about'l0 and at a temperature of from about costabilizing compound is selected from the group consisting of diethylene glycol; triethylene glycol; and glycols of the formula wherein the average value of x is from 4 to about 80.
• the costabilizing compound is an aliphatic alcohol having the formula wherein is from about 2 to about 200; and wherein the amylolytic enzyme is an a-amylase characterized by amylolytic activity in the pH range of from about 4.5 to about'l0 and at a temperature of from about costabilizing compound is selected from the group consisting of diethylene glycol; triethylene glycol; and glycols of the formula wherein the average value of x is from 4 to about 80.
• composition of claim 6 wherein from about 4 to about 10 percent of a nonionic or zwitterionic detergent is present.
• composition of claim 7 wherein the detergent is selected from the group consisting of condensation products of 1 mole of aliphatic alcohol having from eight to 22 carbon atoms with from 5 to 40 moles of ethylene oxide; 3-(N,N-dimethyl-N-alkylammonio) propanel-sulfonate wherein the alkyl has from eight to 22 carbon atoms; and 3-(N,N-dimethyl-N- r 13 alkylammonio )-2-hydroxypropane- 1 -sulfonate wherein the alkyl has from eight to 22 carbon atoms. 5
• composition of claim 8 wherein the detergent is 3-(N,N-dimethyl-N-coconutalkylammonio)-2- hydroxypropane-l-sulfonate and the organic costabilizing compound is triethylene glycol.
• composition of claim 8 wherein the calcium salt is selected from the group consisting of calcium acetate, calcium sulfate and calcium chloride.
• a stabilized aqueous enzyme composition consisting essentially of by weight of the composition:
• composition of claim 11 wherein the amylolytic enzyme is an a-amylase characterised by amylolytic activity in the pH range of from about 4.5 to about and at a temperature of from about 60F. to about 150F.
• composition of claim 12 wherein the a-amylase is derived from Bacillus subtilis.
• composition of claim 13 wherein the a-amylase is present in an amount of from about 0.01 to about 0.5 percent.
• composition of claim 15 wherein from about 4 to about 10 percent of a detergent selected from the group consisting of nonionic and zwitterionic detergents is present.
• composition of claim 16 wherein the detergent is selected from the group consisting of condensation products of 1 mole of aliphatic alcohol having from eight to 22 carbon atoms with from 5 to 40 moles of ethylene oxide; 3.-(N,N-dimethyl-N-alkylammonio) propanel-sulfonate wherein the alkyl has from eight to 22 carbon atoms; and 3-( N,N-dimethyl-N- alkylammonio)-2-hydroxypropanel-sulfonate wherein the alkyl has from eight to 22 carbon atoms.
• composition of claim 17 wherein the detergent is 3-(N,N-dimethyl-N-coconutalkylammonio)-2- hydroxypropanel -sulfonate.
• composition of claim 17 wherein the calcium salt is selected from the group consisting of calcium acetate, calcium sulfate and calcium choride'.

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Cited By (43)

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Citations (18)

• 1969
  • 1969-12-10 CA CA069,490A patent/CA940070A/en not_active Expired
  • 1969-12-19 FR FR6944221A patent/FR2026896A1/fr not_active Withdrawn
  • 1969-12-22 AT AT1195869A patent/AT305936B/de not_active IP Right Cessation
  • 1969-12-22 BE BE743505D patent/BE743505A/xx unknown
  • 1969-12-22 DE DE1964088A patent/DE1964088C3/de not_active Expired
  • 1969-12-22 NL NL6919220A patent/NL6919220A/xx not_active Application Discontinuation
  • 1969-12-22 GB GB62221/69A patent/GB1277479A/en not_active Expired
  • 1969-12-22 CH CH1902769A patent/CH522034A/de not_active IP Right Cessation
• 1972
  • 1972-03-06 US US00232300A patent/US3819528A/en not_active Expired - Lifetime

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