Classifications

• • 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
• • 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
  • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
  • C11D17/0039—Coated compositions or coated components in the compositions, (micro)capsules
• • 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
  • C11D3/38672—Granulated or coated enzymes

Definitions

• the invention related broadly to encapsulated enzymes and particularly to water soluble encapsulated enzymes which may be combined with a halogen bleach to form an effective bleach/enzyme cleaning composition.
• Enzymes are proteins synthesized by living organisms which can catalyze specific biochemical reactions such as the conversion of starch to sugar (amylase), the hydrolysis of fats to glycerol and fatty acids (lypase) and the hydrolytic breakdown of proteins (protease). It is commonly believed that enzymes are capable of catalyzing reactions only at a limited number of specific sites commonly referred to as "active sites”.
• Certain biological materials such as proteins, lipids and polysaccharides can be difficult to remove from substrates such as dishes, flatware and fabrics as such biological materials are substantially insoluble in traditional cleaning media.
• an enzyme in a cleaning media to catalytically assist in breaking down such materials into insoluble monomeric and/or oligomeric molecules.
• Certain types of enzymes such as amylase, lipase, and protease are known to be particularly useful for such purposes as they can effectively remove such materials from substrates without significantly degrading the substrate being cleaned.
• Halogen bleaches are a well known group of chemical compounds having the ability to remove stains such as those caused by coffee and tea from a substrate. Halogen bleaches eliminate such stains by breaking down the large colored organic molecules which form such stains into smaller colorless molecules.
• halogen bleaches The cleaning actions of enzymes and halogen bleaches are complementary, each affecting different aspects of the soils typically found on dishes, flatware, and fabrics. Accordingly, a superior cleaning composition could be formed by employing both an enzyme and a halogen bleach in a single cleaning composition.
• halogen bleaches tend to instantly deactivate enzymes at concentrations as low as 1 part active halogen per one million parts cleaning media. While such deactivation of enzymes is not fully understood, it is believed that the halogen bleach affects either a change in the structure of the enzyme's active site or a change in the shape of the enzyme such that the enzyme's active site is no longer available as a reactor site.
• the time release coating delayed the release of the enzyme deactivating bleach for a time period sufficient to allow the enzyme to perform its cleaning function before it was deactivated.
• this attempt also met with limited success as it proved virtually impossible to economically prevent premature release of an enzyme deactivating amount of the bleach.
• compositions capable of releasing active enzyme into an aqueous, chlorine bleach-containing media comprising an enzyme core encapsulated with an inner coating of a bleach-neutralizing substance and an outer coating of a time-release substance.
• the encapsulated enzyme may further comprise an initial coating of a time-release substance between the enzyme and the bleach-neutralizing substance to ensure that all chlorine bleach present in the solution has been neutralized by the bleach-neutralizing substance before the enzyme is released.
• a composition capable of releasing active enzyme into an aqueous, chlorine bleach-containing media comprising an enzyme core encapsulated with a time-release substance designed to delay release of the enzyme into solution for a first-time delay, and a bleach-neutralizing substance encapsulated with a time-release substance designed to delay release of the bleach-neutralizing substance into solution for a second-time delay; the first-time delay being longer than the second- time delay so that the bleach­neutralizing substance will be released and completely neutralize all chlorine bleach present in the solution before the enzyme is released.
• the bleach-neutralizing substance may be present either as a core material or as an inner coating material on a diluent core.
• the enzyme may be encapsulated with an inner coating of bleach-neutralizing substance between the enzyme and the time-release substance.
• compositions capable of releasing active enzyme into an aqueous, chlorine bleach-containing media comprising an enzyme core encapsulated with a time-release substance, a diluent core encapsulated with an inner coating of a bleach-neutralizing substance and an outer coating of a time-release substance, and a bleach-neutralizing substance core encapsulated with a time-release substance.
• the enzyme core and the bleach-neutralizing substance core may be further encapsulated with an initial coating of a bleach-­neutralizing substance between the core and the time-release substance.
• the enzyme core may be coated with the time-release substance so as to delay release of enzyme into solution for a first time delay, and the cores of diluent and bleach-neutralizing substance coated with the time-release substance so as to delay release of diluent and bleach-neutralizing substance into solution for a second time delay; the first time delay being longer than the second time delay so that all bleach-neutralizing substance present as either a core material or a coating material on a diluent core will be released and completely neutralize all chlorine bleach present in the solution before the enzyme is released.
• a cleaning composition particularly effective in warewashing which comprises at least one of the encapsulated enzyme containing compositions described above, a chlorine bleach, and at least one additional detergent component.
• enzymes typically contain a significant portion of an inert filler such as sodium sulfate, sodium chloride, or the like.
• wt-% enzyme refers to the active enzyme and any inert filler employed in combination with the enzyme.
• encapsulation of a mixture of 20 mg enzyme and 60 mg inert filler with an inner coating of 10 mg bleach-neutralizing substance and an outer coating of 10 mg time-release sub­stance results in an encapsulated enzyme composition comprising 80 wt-% enzyme core.
• bleach refers to any chemical agent capable of removing the color from a substrate by oxidation.
• active halogen or “active chlorine” refers to the halogen or chlorine actually present in the compound having a valence of greater than -1.
• compositions capable of releasing active enzyme into an aqueous, chlorine bleach containing media comprising an enzyme core encapsulated with an inner coating of a bleach-neutralizing substance and an outer coating of a time-release substance.
• the encapsulated enzyme may further comprise an initial coating of a time-release substance between the enzyme and the bleach-neutralizing substance to ensure that all chlorine bleach has been neutralized by the bleach-neutralizing substance before the enzyme is released.
• Any enzyme capable of facilitating the removal of biological soil from a substrate without substantially damaging the substrate may be usefully employed in the present invention.
• Such enzymes includes proteases, lipases, amylases, and the like.
• the preferred enzyme or combination of enzymes depends upon the substrate to be cleaned and the types of soil to be removed. For reasons of ease of handling and ease of encapsulation, the enzyme is preferably powdered in form.
• Proteases are those enzymes which attack and break down proteinaceous soils such as meat residue, gravy, and blood. Proteases are classified in EC class 3, subclass 3.4. I have found the EC class 3.4.4 peptide peptido-hydrolases such as subtilopeptidase A (EC 3.4.4.16) to be particularly effective in the cleaning composition of this invention.
• a suitable protease can be purchased from Novo Industries under the mark Esperase®.
• Lipases are those enzymes which attack and break down fatty soils such as cooking oil, grease, and ice cream. Lipases also belong to EC class 3, but are placed in subclass 3.1. I have found the EC class 3.1.1 enzymes such as the glycerol ester hydrolases (EC 3.1.1.3) to be particularly effective in the cleaning composition of this invention.
• a suitable lipase can be purchased from Enzyme Development under the mark Lipase 30,000.
• Amylases are those enzymes which can attack and break down starch, polysaccharide, and cellulosic soils such as potatoes, rice, oatmeal, and grass. Amylases also belong to EC class 3, but are placed in subclass 3.2. I have found the EC 3.2.1 glycoses hydrolases such as alpha-1, 4-glucan-4-­glucanohydrolase (EC 3.2.1.1), and alpha-1, 4-glucan malto­hydrolase (EC 3.2.1.2) to be particularly effective in the cleaning composition of this invention.
• a suitable amylase can be purchased from Novo Industries under the mark Ter­mamyl®.
• the encapsulated enzyme can comprise from a trace up to about 95 wt-%, based upon the total capsule, enzyme core.
• the capsule preferably comprises about 50 to 80 wt-% enzyme.
• surrounding and protectively encapsulating the enzyme core is an inner coating of a bleach-neutralizing substance which, when released into solution, reduces all active chlorine present in the solution to a form which will not deactivate the enzyme.
• the bleach-neutralizing substance should, of course, be a stable solid at room temperature and be compatible with the enzyme and all other components intended to be combined with the encapsulated enzyme. Further, the bleach-­neutralizing substance should not damage the substrate to be cleaned.
• Suitable bleach-neutralizing substances include sulf-oxy acids and salts thereof, hydrogen peroxide producing compounds, sugars, and the like.
• Sulf-oxy acids and the salts thereof are a well-known group of compounds which possess the ability to neutralize chlorine bleaches.
• the alkali metal and ammonium salts of sulf-oxy acids such as ammonium sulfite ((NH4)2SO3), sodium bisulfite (Na2SO3), sodium thiosulfite (Na2S2O3) sodium metabisulfite (Na2S2O3), potassium metabi­sulfite (K2S2O5), lithium hydrosulfite (Li2S2O4), and the like are preferred.
• Sulf-oxy acids are readily available from a number of suppliers including Allied Corporation under the mark Sulftech®.
• the. preferred chlorine bleach-neutralizing substances are those compounds capable of producing hydrogen peroxide when placed in solution.
• Such compounds include perborates, percarbon­ates, perphosphates, persulfates, and the like. These compounds are readily available from a number of suppliers including Interox Peroxid-Chemie GmbH and Dupont.
• the preferred hydrogen peroxide producing source is sodium perborate monohydrate available from Interox Peroxid-Chemie GmbH.
• the encapsulated enzyme can comprise about 1 to 95 wt-%, based upon the total capsule, bleach-neutralizing substance.
• the capsule preferably comprises about 10 to 60 wt-%, based upon the total capsule, bleach­neutralizing substance.
• surrounding and protectively encapsulating the enzyme core and the first coating of bleach-neutralizing substance is an outer coating of a time-release substance.
• the time-release substance delays release of the bleach-neutralizing substance and the enzyme so that a bleach, used in combination with the cap­sule, can perform its cleansing function before it is deac­tivated by the bleach-neutralizing substance.
• the time-­release substance should, of course, be compatible with the enzyme, the bleach-neutralizing substance, and all other components intended to be combined therewith. Further, the time-release substance should not damage the substance to be cleaned. Any material meeting these two criteria and capable of delaying the release of substantial amounts of the bleach-neutralizing substance for about 1 to 20 minutes, preferably about 2 to 6 minutes may be employed in the present invention.
• the time-release substance will comprise a high molecular weight semisolid or solid fat, an inorganic solid, a natural or synthetic polymer, or the like.
• the preferred time­release substances are the natural and synthetic polymers.
• Suitable time-release polymers include: cellulose derivatives such as sodium carboxymethyl cellulose, sodium hydroxyethyl cellulose, ethyl cellulose, hydroxypropyl cellulose, hydroxypropyl methyl cellulose, nitro cellulose, cellulose acetate phthalate, and hydroxypro­pyl methyl cellulose phthalate; gelatin; starch; proteins; fatty acids; waxes (including paraffin and microcrystalline waxes); polyacrylamide; polyacrylic acid; polyvinyl alcohol; polyethylene glycol, etc.
• the use of these and other similar time-release substances including selection of an appropri­ ate compound for a particular use, is well within the skill of one of ordinary skill in the art.
• the preferred time-release substance is carboxymethyl cellulose and salts thereof.
• Suitable sodium carboxymethyl cellulose is avail­able from a number of suppliers, including Hercules, Inc., under the mark CMC-CLT®.
• the encapsulated enzyme can comprise about 1-50 wt-%, based upon the total capsule, time-release substance.
• the preferred wt-% depends upon the particular substance employed and how long the bleach is to be allowed to function before it is deactivated by the bleach-neutralizing substance. For use in ware and fabric washing, I have found that about 1-20 wt-%, based upon the total capsule, time-release substance is typically satisfactory.
• the encapsulated enzyme can comprise an initial coating of a time-release substance between the enzyme core and the bleach-neutralizing substance to ensure that all of the active chlorine in solution has been neutral­ized by the bleach-neutralizing substance before the enzyme is released.
• time-release substance can comprise any of the time-release substances previously described.
• initial coating required to ensure that all active chlorine has been deactivated before the enzyme is released depends upon the amounts and type of bleach-neutral­izing substance and initial coating material employed. However, I have found that about 0.5 to 5 wt-%, based upon the total capsule, initial coating material is typically sufficient to prevent premature release.
• composition which comprises an enzyme encapsulated in a time-release substance designed to delay release of the enzyme into solution for a first-time delay, and a bleach-­neutralizing substance encapsulated in a time-release substance designed to delay release of the bleach-­neutralizing substance into solution for a second-time delay; the first-time delay being longer than the second- time delay so that the bleach-neutralizing substance will be released and completely neutralize all active chlorine present in the solution before the enzyme is released.
• the bleach-­neutralizing substance may be present either as a core material or as a first coating on a diluent core.
• the enzyme may be encapsulated with an inner coating of a bleach-neutralizing substance between the enzyme and the time-release substance. Still further, the enzyme may be initially encapsulated with a time-release substance.
• a diluent core may be employed as a carrier for bleach-­neutralizing substance wherein the bleach-neutralizing substance is coated onto the diluent. This is particularly useful when the bleach-neutralizing substance does not readily form substantially uniform granules.
• the use of a diluent core allows both enzyme and diluent to be simultaneously coated with bleach-neutralizing substance, thereby simplifying manufacture.
• Suitable diluents include sodium sulfate, sodium chloride, etc.
• the enzymes, chlorine bleach-neutralizing substances, time-release substances, and chlorine bleaches described previously with respect to the first aspect are all equally well suited for use in this aspect.
• the time-release substance employed to coat the enzyme and the bleach-neutral­izing substance may be the same or different. For ease of manufacturing, they are preferably the same.
• This composition is particularly useful when the ratio of chlorine bleach-neutralizing substance to enzyme is so large that there simply is not sufficient enzyme particles upon which to attach sufficient chlorine bleach-neutralizing substance.
• the time-release layers should be designed to prevent release of the bleach-neutralizing substance for at least about 1 minute, preferably about 2 to 6 minutes, and the enzyme should be protectively encapsulated for an addi­tional .5-2 minutes after release of the chlorine bleach­neutralizing substance.
• the encapsulated enzyme particle can comprise from a trace up to about 95 wt-%, preferably about 30-80 wt-% enzyme, about 0 to 10 wt-%, preferably about 0 to 5 wt-% initial coating of time-release substance, about 0 to 95 wt-%, preferably about 10 to 60 wt-%, bleach-neutralizing substance, and about 1-50 wt-%, preferably about 1-20 wt-% outer coating of time-release substance; and the encapsulated chlorine bleach-neutralizing substance can comprise from a trace up to about 95 wt-%, preferably 50 to 80 wt-% diluent core, from a trace up to about 95 wt-%, preferably about 50-­80 wt-% chlorine bleach-neutralizing substance if employed as the core or about 15-40 wt-% chlorine bleach-neutralizing substance if employed as the first coat, and about 1-50 wt-%, preferably about 1-20 wt-% enzyme
• composition which comprises an enzyme core encapsulated with a time-release substance, a diluent core encapsulated with an inner coating of a bleach-neutralizing substance and an outer coating of a time-release substance, and a bleach-­neutralizing substance core encapsulated with a time-release substance.
• the enzyme and the bleach-neutralizing substance cores may be encapsulated with an inner coating of a bleach-neutralizing substance between the core and the time-release substance.
• the time-release coating on the enzyme core may be designed to delay release of the enzyme into solution for a first time delay, and the time-release coating on the diluent core and the bleach-­neutralizing substance core designed to delay release of the diluent and the bleach-neutralizing substance into solution for a second time delay wherein the first time delay is longer than the second time delay such that the bleach-­neutralizing substance core and coatings will be released and completely neutralize all active chlorine present in the solution before the enzyme is released.
• the enzymes, chlorine bleach-neutralizing substances, time-release substances, and chlorine bleaches described previously with respect to the first aspect are all equally well suited for use in this aspect.
• the time-release substance and bleach-neutralizing substance employed to coat the enzyme, the bleach-neutralizing substance and the diluent may be the same or different. For ease of manufacturing, they are preferably the same.
• This composition is particularly useful when the ratio of chlorine bleach-neutralizing substance to enzyme is so large that there is insufficient enzyme particles upon which to attach sufficient chlorine bleach-neutralizing substance.
• the time-release layers should be designed to prevent release of bleach-neutralizing substance for at least about 1 minute, preferably about 2 to 6 minutes, and the enzyme should be protectively encapsulated for an additional 0.5-2 minutes after release of all of the bleach-neutralizing substance into solution.
• the encapsulated enzyme particle can comprise from a trace up to about 95 wt-%, preferably about 30-80 wt-% enzyme, about 0 to 10 wt-%, preferably about 0 to 5 wt-% initial coating of the time-release substance, about 0 to 95 wt-%, preferably about 10 to 60 wt-%, bleach-­neutralizing substance, and about 1-50 wt-%, preferably about 1-20 wt-% outer coating of time-release substance;
• the encapsulated chlorine bleach-neutralizing substance can comprise about 50-80 wt-% chlorine bleach-neutralizing substance core, about 0-40 wt-% chlorine bleach-neutralizing substance coating, and about 1-50 wt-%, preferably about 1-20 wt-% time-release substance; and the encapsulated diluent can comprise about 30-80 wt-% diluent core, 10-60 wt-% chlorine bleach-neutralizing substance and about 1-50 wt-%
• compositions of the first, second and/or third aspects are combined with a chlorine bleach and at least one additional detergent component to form an effective cleaning composition.
• the chlorine bleach should be able to dissolve rapidly so that it may perform its cleaning function before the chlorine bleach-neutralizing substance is released. Many of the well-known chlorine bleaches are rapidly soluble and would be suitable for use in the invention.
• Chlorine bleaches are a well-known group of compounds capable of releasing active chlorine (Cl2) or hypochlorite (OCL-) ions into solution.
• Suitable chlorine bleaches include alkali metal dichloroiso- cyanurates, chlorinated trisodium phosphate, alkali metal and alkaline earth metal hypochlorites, monochloramine, dichloramine, nitrogen tri­chloride, [(mono-tri-chloro)-tetra-(mono-potassium dichloro)­]penta-isocyanurate, 1,3-dichloro-5,5-dimethyl hydantoin, paratoluene sulfondi-chloroamide, trichlomelamine, N-chloro­melamine, N-chlorosuccinimide, N,N ⁇ -dichloroazodicarbonamide, N-chloro acetyl urea, N,N ⁇ -dichlorobiuret, chlor
• the preferred bleaches are hydrated and anhydrous sodium dichlorisocyanurate and chlorinated trisodium phosphate. These bleaches are available from a number of commercial sources including Olin Corporation under the mark Clearon CDB-56 (sodium dichloroisocyanurate dihydrate) and Monsanto Industrial Chemical Co. under the mark ACL-56.
• the cleaning composition can comprise only chlo­rine bleach and encapsulated enzyme, for reasons of increased cleaning ability it preferably further comprises at least one additional detergent component such as a surfactant, a detergent filler, a detergent builder, a sequestrant, a chelating agent, etc.
• additional detergent component such as a surfactant, a detergent filler, a detergent builder, a sequestrant, a chelating agent, etc.
• Suitable organic surfactants include anionic, nonionic, amphalytic, zwitterionic, and mixtures thereof. While any compatible surfactant may be employed, surfactant types which are most widely used in detergent compositions include soaps (i.e., sodium or potassium salts) of fatty acids, rosin acids, and tall oil; alkylarenesulfonates; alkyl sulfates, including surfactants with both branched-chain and straight-­chain hydrophobes, as well as primary and secondary sulfate groups; sulfates and sulfonates containing an intermediate linkage between the hydrophobic and hydrophilic groups, such as the fatty acylated methyl taurides and the sulfated fatty monoglycerides; long-chain acid esters of polyethylene glycol, particularly the tall oil ester; polyethylene glycol ethers of alkyl phenols; polyethylene glycol ethers of long-­chain alcohols and mercaptans; fatty acyl diethanol
• Suitable detergent fillers, builders, sequestrants, and chelating agents include any of these well-recognized compon­ents whose functions include maintaining an alkaline pH, suspending particulate matter in solution, preventing redepo­sition of particulate matter, etc.
• a nonexhaustive list of such detergent fillers, builders, sequestrants and chelating agents includes condensed phosphates such as sodium tripolyphosphate, alkalis such as sodium carbonate, sodium metasilicate, and sodium hydroxide, fillers such as sodium sulfate, sodium bicarbonate and sodium chloride, soil suspending agents such as carboxymethylcellulose, and chelators such as ethylene diamine tetraacetic acid and polyacrylic acid.
• the cleaning composition can comprise: about 0.1-1.5 wt-%, preferably about 0.5 to 1 wt-% available chlorine, about 0.3 to 20 wt-%, preferably about 1.5 to 15 wt-% encapsulated enzyme; an excess stoichiometric amount of an encapsulated bleach-neutralizing substance for the active chlorine, and about 0 to 99 wt-%, preferably about 55 to 95 wt-% additional detergent components.
• the cleaning composition contains up to 10 wt-% surfactant as an additional detergent component.
• the amount of chlorine bleach-neutralizing substance employed must be sufficient to reduce all active chlorine present in the solution.
• the stoichiometric ratio of bleach-neutralizing substance to active chlorine is about 1:1 to 1.5:1 to ensure immediate deactivation of the active chlorine.
• Preparation of the encapsulated enzyme and the encapsu­lated bleach-neutralizing substance can be accomplished in any of the several known encapsulating processes such as pan coating, roller coating, spray-congealing, etc.
• the prefer­red process is a fluidized bed process encapsulation.
• encapsulation in a fluidized bed comprises the steps of
• the cleaning composition may be prepared by simply blending all components together, being sure to minimize the possibility of damaging the capsules.
• KLUCEL E a hydroxypropyl cellulose purchased from Hercules, Inc.
• soft water 39.41 lbs.
• the KLUCEL E and soft water were mixed until the KLUCEL E was completely dissolved.
• TERMAMYL 60T a powdered bacterial amylase purchased from Novo Industri a/s.
• the TERMAMYL 60T was fluidized in the bed at an air pressure of 40 psi, and the bed heated to 105°F.
• the entire amount of KLUCEL E solution was sprayed onto the fluidized TERMAMYL 60T granules through a Gustav Schlick Nozzle, Model 941.
• the fluidized bed was heated to 125°F. and the encapsulated TERMAMYL 60T dried therein for 1 minute.
• the capsules were cooled to 100°F. and removed from the bed. 24.5 lbs. of encapsulated TERMAMYL 60T was obtained.
• the encapsulated TERMAMYL 60T and sodium sulfate were fluidized in the fluidized bed at an air pressure of 60 psi and the bed heated to between 140 to 168°F. The entire amount of sodium perborate monohydrate solution was sprayed onto the fluidized TERMAMYL 60T and sodium sulfate granules. The temperature of the fluidized bed was then adjusted to remain between 142 to 150°F., and the encapsulated granules allowed to dry.
• Into the 32 liter container was placed 2 lbs. KLUCEL E and 60 lbs. of soft water. The KLUCEL E and soft water were agitated until the KLUCEL E was completely dissolved.
• the KLUCEL E solution was sprayed onto the once coated granules forming capsules with a first coating of sodium perborate monohydrate and a second coating of KLUCEL E.
• the fluidized bed was heated to 170°F. and the encapsulated granules dried therein for 2 minutes.
• the capsules were cooled to 100°F. and removed from the bed. Capsules retain­ing 90.4% of the original enzyme activity were obtained.
• Example II Into a chlorine bleach solution of known concentration was placed an amount of the composition formed in Example I sufficient to create a 2% stoichiometric bleach-neutralizing excess of sodium perborate monohydrate. After allowing the outer coat of KLUCEL E, the coat of sodium perborate mono­hydrate, and the initial coat of KLUCEL E to dissolve, the solution was tested and found to contain 27.0% of the initial enzyme activity.
• Example II Into a chlorine bleach solution of known concentration was placed an amount of the composition formed in Example I sufficient to create a 20% stoichiometric bleach-neutralizing excess of sodium perborate monohydrate. After allowing the outer coat of KLUCEL E, the coat of sodium perborate monohy­drate, and the initial coat of KLUCEL E to dissolve, the solution was tested and found to contain 54.6% of the initial enzyme activity.
• ESPERASE 4.0T a powdered bacterial protease purchased from Novo Industri a/s.
• the ESPERASE 4.0T was fluidized in the fluidized bed at an atomization pressure of 40 psi and the bed heated to 125° F.
• the entire amount of sodium sulfate solution was heated to 120°F. and sprayed onto the fluidized ESPERASE 4.0T granules through a Gustav Schlick Nozzle, Model 941.
• the fluidized bed was then heated to 130° F. and the thrice encapsulated granules dried therein for 1 minute, then cooled to 100° F. and removed from the bed.
• Example IV Into a beaker equipped with a laboratory stir bar and plate was placed 0.10 grams sodium dichloroisocyanurate dihydrate, 100.6 grams deionized water, and 0.34 grams encapsulated enzyme formed in Example IV. The mixture was vigorously agitated and complete neutralization of active chlorine found to take approximately 3 minutes. The result­ant solution was found to have an enzyme activity of 2.28 knp units per gram of encapsulated enzyme representing a reten­tion of 80% of the theoretical activity.
• ESPERASE 4.0M a powdered bacterial protease purchased from Novi Industri a/s.
• the ESPERASE 4.0M was fluidized in the bed and the bed heated to 80°F.
• the entire amount of sodium sulfate solution was heated to 84°F. and sprayed onto the fluidized ESPERASE 4.0M granules.
• the fluidized bed was heated to 110°F. and the entire amount of the polyacrylic acid solution heated to 90°F. and sprayed onto the once coated granules.
• the fluidized bed was heated to 120° F. and the twice-coated granules dried therein, and then cooled to 100°F. and removed from the bed.
• Example VI Into a beaker equipped with a laboratory stir plate, was placed 0.4 grams sodium dichloroisocyanurate dihydrate purchased from the FMC Corp. and 150 grams soft water heated to 140°F., and 1.0 gram of the encapsulated enzyme formed in Example VI. The mixture was vigorously agitated and found to effect complete neutralization of active chlorine. An EMPA 116 test cloth was placed in the solution and indicated enzyme activity.

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• 1987
  • 1987-12-31 AU AU83174/87A patent/AU8317487A/en not_active Abandoned
• 1988
  • 1988-01-05 AT AT88100045T patent/ATE109822T1/de not_active IP Right Cessation
  • 1988-01-05 ES ES88100045T patent/ES2060609T3/es not_active Expired - Lifetime
  • 1988-01-05 DE DE3850991T patent/DE3850991T2/de not_active Expired - Fee Related
  • 1988-01-05 EP EP88100045A patent/EP0286773B1/fr not_active Expired - Lifetime
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  • 1988-01-28 NO NO880372A patent/NO880372L/no unknown
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  • 1988-04-15 BR BR8801839A patent/BR8801839A/pt not_active Application Discontinuation
  • 1988-04-16 KR KR1019880004349A patent/KR970001229B1/ko not_active IP Right Cessation

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