AU8317487A - Water insoluble encapsulated enzymes protected against deactivation by halogen bleaches - Google Patents

Abstract

A composition capable of releasing active enzyme into an aqueous, active chlorine containing media which in a first aspect comprises an enzyme core encapsulated with an initial coating of a time-release substance, a first coating of a bleach-neutralizing substance and a second coating of a time-release substance. In a second aspect, the composition comprises an enzyme encapsulated in a time-release substance designed to delay release of the enzyme in dissolution for a first-time delay, and a bleach-neutralizing substance, present as either a core material and/or a first coating on a diluent core, which is 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. In a third aspect, the composition comprises an enzyme core encapsulated with a time-release substance, a diluent core encapsulated with a first coating of a bleachneutralizing substance and a second coating of a time-release substance, and a bleach-neutralizing substance core encapsulated with a time-release substance. The invention further includes a cleaning composition which is particularly effective in warewashing which comprises one of the encapsulated enzyme-containing compositions described above, chlorine bleach, and at least one additional detergent component.

Description

(11) AU-A--83174/87

encapsulated diluent, whih comnprises: a diluenit co re; a t irs t. encapsulIati rig coat. ilrig of al i r bI each-nuut. ral i zinrg substance; anid a second encapsulating coating of it 1illlf

release substance.

AUSTRALIA

PATENTS ACT 1952 Form COMPLETE SPECIFICATION

(ORIGINAL) FOR OFFICE USE

Short Title: Int. Cl:

Application Number: Lodged:

Complete Specification-Lodged: Accepted: Lapsed: Published:

Priority:

Related Art:

TO BE COMPLETED BY APPLICANT

Name of Applicant: ECOLAB INC.

Address of Applicant: ECOLAB CENTER ST. PAUL MINNESOTA 55102 U.S.A.

Actual Inventor:

Address for Service: CLEMENT HACK CO., 601 St. Kilda Road, Melbourne, Victoria 3004, Australia.

Complete Specification for the invention entitled: WATER INSOLUBLE ENCAPSULATED ENZYMES 2ROTECTED AGAINST DEACTIVATION BY HALOGEN BLP'CHES

The followir7 statement is a full description of this invention including the best method of performing it known to me:-

163.508-US-01 Patent

WATER INSOLUBLE ENCAPSULATED ENZYMES SPROTEC'ED AGAINST DEACTIVATION BY HALOGEN BLEACHES

Field of the Invention The invention relates 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. o Background of the Invention Enzymes are proteins synthesized by L-'ing organisms which can catalyze specific biochemical reactions such as the conversion of starch to sugar (amylase), the hydrolysis of fa s 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 .an be difficult to remove from substrates such as dishes, flatware and fabrics as such biological materials are substantially insoluble in traditional cleaning meuia. To increase the solubility and thereby effect removal of such biological materials, it is known toemploy an enzyme in a cleaning media to catalytically assist in breaking down such materials into insoluble monomeric and/or oligomeric molecules. Certain t'/nes of enzymes such as amylase, lipase, and protease are known to be particularly useful for such purposes as they can effectiveiv remove such materials from substrates wi'thout significantly degrading tha substrate being cleaned. Halogen bleaches are a well known group uf 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 ir.to smaller colorless molecules. The cleaning actions of enzymes and haloger bleaches are complementary, each affecting different aspects of the soil, typically found on dishes, flatware, and fabrics. Accordingly, a super.or cleaning composition couli be formed by employing both an enzyme and a halogen bleach in a single cleaning composition. However, while simple in theory such a co.mbination has proven to be difficult to implement as 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. Early attempts to combine a halogen bleach and an enzyme into a stable cleaning composition included the incorporation of a stabilizing amount of a polysaccharide into the cleaning composition, the incorporation of a stabilizing amount of a nonionic polymer into the cleaning composition, and coupling of the enzyme to an insoluble support. All of these early I attempts met with limited success, ancouragino research into other methods. A slightly more successful attempt at combining a halogen bleach and an enzyme into a stable cleaning composition comprised encapsulation of the bleach in a time release coating. 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. Unfort.unately, this attempt also met with limited success as it proved virtually

4L I~C I

S3 impossible to economically prevent premature release of an enzyme deactivating amount of the bleach. A still slightly more successful attempt at combining a halogen bleach and an enzyme into a stable cleaning composition is disclosed in U.S. Pat. No. 4,421,664, which teaches that enzyme activity may be maintained in the presence of a halogen bleach by encapsulating the bleach in a time release coating and incorporating an amount of a reducing agent into the composition sufficient to substantially instantaneously reduce all prematurely released bleach. While this method has proven much more successful than earlier attempts, it has been discovered that in order for this method to work effectively it is necessary to employ an encapsulated bleach having an extremely high encapsulation efficiency which results in a prohibitively expensive composition. Accordingly, a substantial need exists for an inexpensive and stable cleaning composition containing both an enzyme and a bleach wherein both the enzyme and the bleach may perform their desired cleaning fur ction. Summary of the Invention In a first aspect of my invention I have discovered a composition capable of releasing active enzyme into an aqueous, chlorine bleach-containing media, the composition 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. In a second aspect of my invention I have discovered a composition capable of releasing ,.ctive enzyme into an aqueous, chlorine bleach-containing media, the ccnposition

L 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 bleach- neutralizing 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. Further, the enzyme may be encapsulated with an inner coating of bleach-neutralizing substance between the enzyme and the time-release substance. In a third aspect of my invention I have discovered a composition capable of releasing active enzyme into an aqueous, chlorine bleach-containing media, the composition 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-netutralizing ,"ubstance 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. Still further, 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. In a fourth aspect of my invention I have discovered 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. Commercially available enzymes typically contain a significant portion of an inert filler such' as sodium sulfate, sodium chloride, or the like. As utilized herein, unless otherwise indicated, "wt-% enzyme" refers to the active enzyme and any inert filler employed in combination with the enzyme. For example, the 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 sub- stance results in an -ncapsulated enzyme composition 1 comprising 80 wt-% enzyme core. "l i' As utilized herein, "bleach" refers to any chemical agent capable of removing the color from a substrate by oxidation. As utilized herein, "active halogen" or "active chlorine" refers to the halogen or chlorine actually pres-nt Sin the compound having a valence of greater than -1. For a detailed analysis of the meaning of "bleach", "active chlorine", and "available chlorine" see White, George, Handbook of Chlorination, 1972, pp. 188-190, which is S herein incorporated by reference. Detailed Descripti.on of the Invention Including a Best Mode

ENCAPSULATED ENZYME

In a first aspect of my invention I have discoverd a composition capable of releasing active enzyme into an aqueous, chlorine bleach containing media, the compo:;it ion comorising 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 bleact-neutralizing substance to ensure that all chlorine bleach has been neutralized by the bleach-neutralizing substance before the enzyme is released. Enzymes Any enzyme capable of facilitating the removal of biological soil from a substrate without substantially damagin1 the substrate may be usefully employed in thet 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. While commercially available enzymes typically contain a significant portion of an inert filler such as sodium sulfate, sodium chloride, or the like, I have found that the presence of such fillers does not affect the present invention. Proteases (including peptidases) are those enzymes which attack and break down proteinaceous soils such meat es residue, gravy, end blood. Proteases are classified in EC class 3, subclass 3,4. I have found the EC class 3.4. peptide peptido-hydrolases such as subtilopeptidase A (EC 3.4.4.16) to be particularly effectiv.e 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 3oils such as cooking oil, grease, and ice creamn. Lipases also belong to EC class 3, but are placed in subclitss 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 and alpha-l, 4-glucan malto- hydrolase (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 Ter- mamyl®. An in depth and detailed discussion of suitable enzymes can be found in U.S. Patent No. 4,421,664, column 4, line 16 through column 6, line 24, which disclosure is herein incor- porated uy reference. The encapsulated enzyme can comprise from a trace up to about 95 based upon the total capsule, enzyme core. However, to allow sufficient bleach-neutralizing substance to be introduced into solution and to achieve economical balance between encapsulation efficiency and amount of coating substance employed, the capsule preferably comprises about 50 to 80 wt-% enzyme. Bleach-Neutralizing Substance In the first aspect of my invention, surrounding and protectively encapsulating the enzyLne core is an inner coating of a bleach-neutralizing substance which, wnen 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 bAach- neutralizing substance should not damage the substrate be cleaned. Any composition capable of reducing active chlorine to a form which will not deactivate an enzyme and which meets the criteria set forth above, can be usefully employed in the present invention. 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. For reasons of low cost, high perform- ance, and ease of availability, the alkali metal and ammonium salts of sulf-oxy acids, such as ammonium silfite ((NH 4 2 S0 3 sodium bi sulfite (Na 2 SO 3 sodium thiosultite (Na2 S 2 03), sodium metabisulfite (Na2 S 203), potassium metabi- sulfite (K2 S 2 0 5 lithium hydrosulfite (Li2 S20 4 And the like are preferred. Sulf-oxy acids are readily available from a number of suppliers including Allied Corporation under the mark Sulftech®. Because of their odorless and noncorrosive nature, the preferred cnlorine bleach-neutralizing substances are those compounds capable of producing hydrogen peroxide when placed in solution. Such compounds include perbo:ates, percarbon- ates, perphosphates, persulfates, and the like. These compounds are readily available from a number of suppliers including Interox Peroxid-Chemie GmbH and Dupont. For reasons of cost and ease of availability, 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. However, to achieve an economical balance between encapsulation efficiency and amount of coating substance employed and provide sufficient bleach-neutralizing ;sutbstance to ensu e complete neutralization of all active chlorine present in solution, the capsule preferably compris a.bout to 60 vit-%, based upon the total capsule, bleach- neutralizing substance. Time-Release Silbstance In the first aspect of my invention, surrounding and pcotectively encapsulating the enzyme core and the first coating of bleach-neutralizing substance is an outer coating of a timre-release substance. The time-release substance delays release of the bleach-neutralizing subsftlnce and the enzyme so that a bleach, used in combination with the cap- sule, can perform its cleansing function before it is deac- tivated 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. Pur ther, the time-release substance ohould 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 minute, preferably about 2 to 6 miniutes may be empl)y(L in t he present invention. Generally, the time-release sub stance will comprise a high molecular weight semisolid or solid fat, an inorganic solid, a natural or synthetic polymer, or the like. For reasons of excellent film formation, the preferred time- release substances are the natural and synthet. ic polymers Suitable time-release polymers are well known in the art. and include: cellulose derivatives such as sodium carboxymet hyl cellulose, sodium hydroxyethyl cellulose, ethyl cellulo-e hydroxypropyl cellulose, hydrcx, propyl methyl cellul ose, nitro cellulose, cellulose acet:ate phthalate, and hydroxypro- pyl methyl cellulose phthalate; gelatin; starch; protein; fatty acids; waxes (including paraffin and mi ,rocryst allinte waxes); polyacrylamide; polyacrylic acid; polyvinyl a Iciol polyethylene glycol, etc. The use of these and other s!;imilar time-release substances includinq seleLction of lan airop i ate compound for a particular use, is well within the skill of one of ordinary skill in the art. Because of its ability to suspend soils in solution in addition to its time-release characteristics, the preferred time-release substance is carboxymethyl cellulos.e and salts thereof. Suitable sodium carboxymethyl cellulose is avail- able from a number of suppliers, including Hercules, Inc., under the marl' CMC-CLT'. The encapsulated enzyme can compric;e about l1-50 wt-Y, based upon the total capsule, time-relea(se substance. The preferred wt-2 depends upon the particular substance employed and how long the bleach i to be allowed to function before it is deactivated by the bleach-neutral i z in j sub;stance. For use in ware and fabric washing, I have found that about 1-20 based upon the total capsule, time-release substance is typically satisfactory. Initial TimeRelIpe __sbrtan e

Optionally, the encapsulated enzyme can comprie an initial coating of a t ime-release substance betwfeen the enzyme core and the bleach-neutralizing substance to ens.ure that all of the active chlorine in solution has been neutral- ized by the bleach-neutralizing substance before the enzyme is released. While I have found that excellent results may be ob-- tained in the absence of this initial coating, it may be useful in some cases s ch as when an unstab enzyme is employed, a slow reacting reducing agent is emptloyEd or a small amount of reducing agent is employed. The initial coating of time-release subsr;tance can comprI:., any of the time-release substances previously described. The amount of initial coating required to (ensure that all1 active chlorine has hFbeenlde activatte'i beforfe tii c nzyme i., released depends upon th amounts and Lype of hlaci-nut rd i z ing substance and initial coating material em11piyed. However, I have found that about 0.1) to wt- 1, isad upon the total capsule, initial coating material is t yp icalIlIy s ifficient to prevent premature release.

COM13INATION 01-1 ENCAPSEJLATE'l ENZYME AND) ENCAPSULATED BLEACHI-NEUTRAL I NG SUBSTANCE

In a sectond( apect of my invention I have tli sn~ve red A compos iion which c:ompri ses an enzyme e ncapsuir teoill a1 time- release substance des ig:ned to duelay r elease 4~ tlihe enzyme into solution for a first-time de lay, anl a b leach- neu tral1i zi ng substance encapsulated in a i me-re Iow; s ubs t an1ce d e s ig ned to delay re 1eav o of the 1' 1 au't neutralizing substance into solution fo)r a second-t im deilt! the first-t.: ime delay being longer than the second- timno dei,,y so that the bleach-neutralizing substLance wil1b e reoleased and completely neutral izo all act.ivye chlobr ine present. ii thle solut. ion before thf. nzyme is r e Ieas e Je hi ea chI neut ra lizinug subs t:',nce may be present e ither as a coru mate rial1 or as a first coating on a diluen n ncoe. Fur therf the enzyme may be encap~sulated with an inner cta.i ny of a lbleach--rieut ra liz i g substance between the enzyme and the t line-release subs tai;e S1t ill further the enzyme may be initiall y encapsulated with a time-release sulbstance. D)1 luent. A diluent core may be employed as,, a car rier for hbleach- neutralizing substance wherein the bleach neutralizing substance is coated onto the diluent. This is part icultarlIy usefuII when the bleach-n1 Itral izingo subst ance does ho(t reooily form substantially uni form granulIes. Th" use Vt a diluient core allows both enzyme and di luent to be simultaneously coate I withi1ldhnut a n substance, thereby s impli fyinrg manu factu re. S;u i t ablI e d i lu e 1t~s in11cluIIde soJd i u111 :;rI fa t e ';Ct i 1111 chiot' ri, etc. T A he enzymes?, cl(ion~e h al-in a1'ii~sl;t~rc~ 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 suostance employed to coat the enzyme and the bleach-neutral- izing substance may be the same or different. For ease of manufacturing, they are preferably u'e same. This composition is particularly useful when the ratio of chlorine bleach-reutraliziig substance to enzyme is so large that there simply is not sufficient enzyme particles upon which to attach sufficient chlorine bleach-neutralizing substance. Generally, 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 addi- tional .5-2 minutes after release of the chlori..e bleach- neutralizing substance. In this aspect the encapsulated enzyme particle can comprise from a trace up to about 95 preferably about 30-80 wt-% enzyme, about 0 to 10 preferably about 0 to wt-% initial coating of time-release substance, about 0 to preferably about 10 to 60 bleach-neutralizing substance, and about 1-50 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 preferably 50 to 80 wt-% diluent core, from a trace up to about 95 preferably about 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-% time-release substance.

YIZLI~ i L L IY

13

ibed COMBINATION OF ENCAPSULATED ENZYME, largo th; ally ENCAPSULATED BLEACH-NEUTRALIZING SUBSTANCE to attaci ease AND ENCAPSULATED DILUENT HAVING A COATING OF Gene ral- BLEACH-NEUTRALIZING SUBSTANCE neutrali: 2 of 5 of the b: In a third aspect of my invention I have discovered a should b atio composition which comprises an enzyme core encapsulated with substanc Sso a time-Lelease substance, a diluent core encapsulated with an 6 minute cles inner coating of a bleach-neutralizing substance and an outer for an a zing 10 coating of a time-release substance, and a bleach- bleach-n neutralizing substance core encapsulated with a time-release In d to substance. Further, the enzyme and the bleachi-neutralizing comprise r at substance cores may be encapsulated with an inner coating of 30-80 wt and a bleach-neutralizing substance Latween the core and the wt-% i ddi- 15 ti-m-release substance. Still further, the time-release 15 to ach- coating on the enzyme core may be designed to delay release neutrali of the enzyme into solution for a first time delay, and the 1-20 wt can time-release coating on the diluent core and the bleac:,- encapsul bout neutralizing substance core designed to dilay release of the comprise 0 to 20 diluent and the bleach-neutralizing substance into solution 20 substanc 0 to for a second time delay wherein the first time delay is substanc zing longer than the second time delay such that the bleach- wt-% tin wt-% neutralizing substance core and coatings will be released and comprise ated completely neutralize all active chlorine present in he bleach-r )m a 25 solution before the enzyme is released. 25 about 1- uent The enzymes, chlorine bleach-neutralizing substances, I time-release substances, and chlorine bleaches described making d as previously with respect to the first aspect are all equally which a zinq well suited for use in this aspect. The time-release compris: 30 substance and bleach-neutralizing substance employed to coat 30 neutral; the enzyme, the b -ich-neutralizing substance and the diluent the sam may be the same or different. For ease of manufacturing, enzyme, they are preferably the same. with a This composition is particularly useful when the ratio once-co; of chlorine bleach-neutralizing substance to enzyme is so

I

14 largo that there is insufficient enzyme particles upon which to attach sufficient chlorine bleach-neutralizing substance. Generally, when encapsulating the enzyme, bleach- neutralizing substance and diluent to achieve early release of the bleach-neutralizing substance, the time-relea. e 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 enzyie should be protectively encapsula'(ed for an additional 0.5-2 minutes after release of all of the bleach-neutralizing substance into solution. In this aspect the encapsulated enzyme particle can comprise from a trace up to about 95 preferably about 30-80 wt-% enzyme, about 0 to 10 preferably about 0 to wt-% initial coating of the time-release substance, about 0 to 95 preferably about 10 to 60 bleach- neutralizing substance, and about 1-50 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-niutrali ing substance core, about 0-40 chlorine bleach-neutralizing substance coating, and about 1-50 preferably about 1-20 wt-% time-release substance; ana the encapsulated diluent can comprise about 30-80 wt-% diluent core, 10-60 wt-% chlorine bleach-neutralizing substance and about 1-50 prefterably about 1-20 time-release substance. I have found a particularly easy and effective method of making encapsulated enzyme and bleach-neutralizing substance which achieves the desired order of release, tlh mt hodl comprising the steps of obtaining a diluent and a :leach-- neutralizing substance having a granular size substantially the same as the enzyme granules, simultaneously coatinq the enzyme, diluent and bleach-neutraliz ing substance qrinul ;es with a bleach-neutralizing substance, and then cat inq the once-coated granules with a time-release substance.

CLEANING COMPOSITION

In a fourth aspect of my invention, the compositions of the first, second and/or third aspects are combined with a chlorine bleach and at least one add -tional detercent 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 i; 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 compoundts

capable of rel.easing active chlorine (Cl. 2) 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 tri- chloride, [(mono-tri-chloro)-tetra-(mono-potassLum dichloro)- ]penta-isocyanurate, 1,3-dichloro-5,5--dimethyl hydantoin, paratolene sulfondi-chloroamiide, trichlomelamine, N-chloro- melamine, N-chlorosuccinimide, N,N'-dichloroazodicarbonamide, N-chloro acetyl urea, N,N'-dichlorobiuret, chlorinated

dicyandiamide, trichlorocyanuric acid, dichlorogly- coluril, and the like. For reasons of excellent bleaching perform- ance, the preferred bleaches are hydra ted and anhydroui,; sodium dichlorisocyanurate and chlorinated tr iod ium

phosphate. These bleaches are available from a number of commercial sources including Olin Corporation undo r the mark Clearon CDB-56 dichloroisocyanurate (sodium dihydrate) and Monsanto Industrial Chemical Co. under the mark ACI-56. While the cleaning composition can comprise only chilo-- rine bleach and encapsulated enzyme, for reasons lf increa;ed cleanin. ability it: preferably further compris!es at lea5s,;t onW additional detergent component such as a ,ur factant, 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 sodium or potassium salts) of facty 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 diethanolamides; and block copolymers of ethylene oxide and propylene oxide. Suitable detergent fillers, builders, sequestrants, and chelating agents include any of these well-recognized compon- ents whose functions include maintaining an alkaline pH, suspending particulate matter in solution, preventing redepo- sition of particulate matter, etc. A nonexhaustive list of such detergent fillers, builders, sequestrants and chelating agents condensed includes phosphates such ar sodium tripolyphosphate, alkalis such as sodium carbonate, sodium metasilicate, and sodium hydroxide, filler; 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 compoc'tion ca- comprise: about 0.1--1.5 preferably about 0.5 tc 1 wt-% available chlorine, about 0.3 to 20 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 preferably about 55 to wt-% additional detergent components. Preferably the cleaning composition contains up to 10 wt-% surfactant as an additional detergent component. The amount of chlorine bleach-neutr;lizing substance I employed must be sufficient to reduce all active chlorine present in the solution. Preferably 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. Method of Preparation Preparation of the encapsulated enzyme and the encapsu- lated bleach-neutralizing substance can be accomplished in a:y of the several known encapsulating processes such as pan coating, roller coating, spray-congealing, etc. The prefer- red process is a fluidized bed process encapsulation. Basically, encapsulation in a fluidized bed comprises the steps of liquefying the coating materials by either melting the material or dissolving the material in a suitable solvent (preferably water); (ii) fluidizing the particles to be encapsulated by placing the particles in a chamber and passing an oil flow therethrough; (iii) coating the particles with the coating material by spraying the liquefied coating material onto the fluidized particles; and (iv) a lowing the coated particles to cool and/or dry. The cleaning composition may be prepared by simply blending all components together, being sure to minimize the possibility of damaging the capsules. Example Into a 32 liter container was placed 1.25 ibs. KLUICEL E, a hydroxypropyl cellulose purchased from Hercules, Inc., and

39.41 Ibs. of soft water. The KLUCEL E and soft water were mixed until the KLUCEL E was completely dissolved. Into a fluidized bed was placed 23.75 lbs. TERMAMYL 60T, a powdered bacterial amylase purchased from Novo Industri a/s. The TERMAMYL 6)T was flu:.dized in the bed at an air pressure of psi, and the bed heated to 105 0 F. The entire amount of KLUCEL E solution was sprayed onto the fluidized TERMAMYL granules through a Gustav Schlick Nozzle, Model 941. The 0 fluidized bed was heated to 125 F, and the encapsulated TERMAMYL 60T dried therein for 1 minLte. The capsules were cooled to 100 0 F. and removed from utie bed. 24.5 lbs. of encapsulated TERMAMYL 60T was obtained. Into the fluidized bed used above was placed 2.45 lbs. of the encapsulated TERMAMYL 60T and 27.86 lbs. granular sodium sulfate. Into the 32 liter container was placed 5.68 lbs. sodium perborate monohydrate purchased from Interox Peroxid-Chemie GmbH and 113 lbs. of soft water. The sodium perborate monohydrate and water were agitated until the sodium perborate monohydrate was completely dissolved. The encapsulated TERMAMYL 60T and sodium sulfate were fluidized in the fluidized bed at an air pressure of 60 psi and the 0 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 0 to 150 and the encapsulated granulkes allowed to dry. Into the 32 liter container was placetd lbs. KLUCEL E and 60 lbs. of soft water. The KLUCELI, E ind soft water were agitated until the KILUCIL E was complkte:ly dissolved. After the coating of sodium perborate monohydrat dried, the KLUCEL E solution was sprayed onto the once c(,ated granules forming capsules with a first coat: ing t ;;iiiiu perborate monohydrate and a second coat ing ,o KiIAir'cL, 1E. ThIr fluidized bed was heated 0 to 170 andt tie enicaps';i ated granules dried therein for 2 minut:ies. TheI ip;ul e: we cooled to 100 0 F. and removed from the bed.' Capsules retain- ing 90.4% of the original enzyme activity were obtained. ExapleII Into a chlorine bleach solution of known concentration was placed an amount of the composition formed in Example I1 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 mono hydrate, and the initial coat of KLtJCEI E to the solution was tested and found to contaln 27.0% off the initial enzyme activity. E.xamp)I e__I I-1 Into a chlorine bleach solution of known concent-rat-ion was placed an amount of the composition formed in Exampii, 1 sufficient to create a 20%0 stoichiometric blcach-neutralizirg exccqss of sodium perborate monohydrate. After allowing thf. oiter coat of KIJUCEIJ E, the coat off sodium perborate rtonohy- drate, and the initial coat of KLUCEL E to dissolve the, solution was tested and fouri,, to conitain 54.6% off the- ini nial enzyme activity. E'xamplIe-- I-V Into a 32 liter contai ner was, placed 1 .5 lbS!. S~ r sulfate and 15 lbs. off soft water. The sodium sulf-ate aind soft water were mixed until he sodium sulfate was comot.letf p1y dissolved. Into a fluidized bed was placed 18 lbs. ES3PEl{AI 41.0T,a powdered bacterial protease purchased ffrom Novo Ind u.str Ia/ The, ESPEPASE 4. OT was fluidi zed in the fflui dized bed ait a atomization pressure of 40 psi and the bed heated t 12!50"P The, entire amount of sodium sulfate solution wras eae to 120 0 F. and sprayed onto the flui dized ES-PERASE through a Gustav Schlick Nozzle, Model 941. In to the 32 liter conta iner wa;; p1 aced 4 67 lbu. r perborate monohydrate purchased f romn Irterox arui 9J3 .48 1 os; 31 sof t water The sod iura per borate- [nonioyd rate- anri w.itf- r were agitated until the sodium perborate monohydrate was completely dissolved. The fluidized bed was heated to 0 130 the sodium perborate monohydrate solution maintained 0 at less than 115 F, and the entire amount of sodium perborate monohydrate solution sprayed onto the once coated fluidized granules. Into the 32 liter container was placed lbs. CMC-CLT, a sodium carboxymethyl cellulose purchased from Hercules, Inc., and 49.5 Ibs. of soft water. The CMC-CLT and soft water were mixed until the CMC-CLT was completely dissolved. Finally, the CMC-CLT solution was maintained at 0 less than 130 F. and the entire criount thereof sprayed onto the twice coated fluidized granules. The fluidized bed was then heated to 1300 F. and the thrice encapsulated granules dried therein for 1 minute, then cooled to 1000 F. and removed from the bed. Example V 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 result- ant solution was found to have an enzyme activity of 2.28 knp units per gram of encapsulated enzyme representing a ret en- tion of 80% of the theoretical activity. -Example VI Into a 2 liter container was placed 470.5 grams sodium sulfate and 1.600 grams soft water. The sodium sulfat.e and soft water were mixed until the sodium sulfate was completely dissolved. Into a separate 1 liter container was placed 70.5 gramI; of a 3000 molecular weight polyacrylic acid and 2:~1.5 granms soft water. The polya:rylic acid and soft water werie mixed until the polyacrylic acid was completely dissolved. Into a fli'idized bud was placed 352.9 grams EI'Pi:RA;I

I

21- a powdered bacterial protease purchased from Novi Industri a/s. The ESPERASE 4.0M was fluidized in the bed and the bed heated to 800 F. The entire amount of sodium sulfate 0 solution was heated to 84 F. and sprayed onto the fluidized ESPERASE 4.0M granules. The fluidized bed was heated to 110 0 F. and the entire amount of the polvacrylic acid solution heated to 900F. and sprayed onto the once coated granules. The fluidized bed was heated to 1200 F. and the twice-coated granules dried therein, and then cooled to 100°F. and removed from the bed. Example VII 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 0 to 140 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 indic ited enzyme activity. The specification and Examples above are presented to aid in the complete nonlimiting understanding of the inven- tion. Since many variations and embodiments of the invention can be made without departing from the spirit and scope of the invention, the invention resides in the claims herein- after appended.

THE CLAIMS DEF INING T111' INVENTION ARE AS3 F<OLLOWS:

1 An encaps~ulated enzyme composition capable of delivering active enzyme into a solution containing anl active chlorine which comprfises: an enzyme core; a firs;t encapsulating coating of a Phlorine bleach-neu tra1.1z in ri Wub;Lance; anl a s;ecoml encaps1ulat ing coatinq otit t tinitk- release substance. 2. The corwnposiit ion oft claim 1 further compr is~irq anl init ial encapstila t-inq coatinug of: a t ime-re iease substAnce, between the enzyme core and the chllorine1)ac-net lzit; subs tance f irs t: c_,oait nqig 3 The compos it ion of claim I fur ther comprisinguc), ill combination with the encapsulatful enzyme, a s epaira te I1k7 encapsulated chlorine bleach-neutra lizi ng stustance which comprises: a)a h 1tin~iUtf1Kich-neut ral inzinUjSq t tubsane cc a e and a1n e licatIclr1t: in uLq of a t in lei ci ast substance. 4. Trhe mc;i iS of, cia im 1 fur ther cc cpr isi no, in combina tio 10 wi tii thle ;!lcaopIilat~ted e'lizyifl aI sep'i raI t e I Y ericaprsu Iat ed (Ii I ie it wh i ch cu(mp r i ses: a) a dii Iucift Core; ab first encapsau 1at ing (Int Nno 'talitL ci iec 1)1 ach- neult raI I i 'zi m;q suhlst ance ',nId a ~'t(Iflt encapi511t ininq ''JIj )t I i lli release substanne. The~j conlps it itni "f v1aim I or 4 WPeM ni thli' ezzytc 1s a proteads;c 1a iipaise '111 amry 1ase or a mii xt ill? t lhe ec) 6 TPhe cc i I t.X~ i f I a j it I oc r I I I ei I I t it, ohi Lor No 1) i ch-nt'ut raI liz i rig subst aiice is I .i 111 fc 'wi d a _11It' t her et 7 I'he cio ii~~c t jcdl of ci V a iin wh WIPI it 11 1;o 1 W7 a ;id or salt thereof is a thiosultate, metabis;lf i tI,, bisulfite, or salt thereof. 8. The composition of claim 1 or 4 wherein tOe chlorine bleach neutralizing rsubv '.ance is; a perborate, persulfate, perphotsphate, or porcarbonate 9. The composi;ition of clair I or 4 where in the L ine- releas;e subst; ance 1is a cel lu 1ose de r ivaLi ye. A Cleanl nq compos;i t ion com~pr .1i.I q: (it) an eficapsulcled enwymoi Which enrIre (i)anl enzyme core; (ii) f irs~ t eicaps~u I'l inq ('oat!in (it; f a chlorine l~e~~etrli' I( iLne;arid (iii.) at second enea-,p,;Iiat i Iq n;0. ofi a t. imo I'e Iea4I e t'ih~ ance; 1 a chlorine bleachr; aund at- 1.easit-: one add it~ i )na I det-er qeuf upnet, ,el ectAed froin ,iurf ac~t~ el deeqmt (10 fi II dt erqeilt buildIer,; sequet-rantn ad( (hP 1 .iiiq cqetilt

I1I A cleaninq C,-oIIIIonit iOn v -Ali fn(%ip,;ulat~od enziymat. Wich cf'i ')III)I P

1411entzymfe

or it-e hDeicl-neut: tIa I i z' 111, j ('11i)1 ;uIbh!-t .iire illd(

c i.i ei i e ld (iIie t i iCiqI fIU t illj (f

t IIr .I diiw sub,;L e' nl (ii onca .41 rlt-ot. enriiutit W1 iii C)Ifcpt L'

t'lk 1 Ii w 1)I1ieaeii--rIir cI i jil i m j ai~ ecn ec api,nI I at, I I111 I-f.,t i 11e J w e re1e.;e ;hLie Ic hllor inte hi t--c-i ti11i

(di) a,i I ea.,t (ne add(i t I ('1a I ulet ferfqenf CIAIuP. fl0't

i (e1 't ed f ru(Iti ,;Il-f arIt .iitr d t orqiit I iI I tl ldet fq qenIt lil i 1Ie -'equerlanitns, and (11t1 ,t i nq op-lit 12. A elclinq~l~U~ t i 101 I~:m i.,i q:

ahbeut (13 2 wt I1~ iI i' 1e comnposi tion, encapsulated enzyme which compr is~es: i) about 1 to 95 bas~ed ulponj thilk encapsulated enzyme, enzyme core; GOi about 1-95i wqt-%, bas ed( upon th OnCaPS-Ilated enzyme, fi r t eicap~;u lat inq co)at ir:q oft a chlorine bleach-neutrali z i n "Mb~tanCe; and (iii) about 1-5 0 wt-T based upon the encaps;uiated enzyme, s;econdi enupu atimri coat inig of a t ime*-releaso substance; A. b) aout 0 .1-40 wt-% chlor ine hi each; arid c) about 55-9 wt- 6, ha u ed upon the clIeanin g corlipot i t l oil, of at Ia-,t: ()Ile add i t' i olh 'Let erjerit component s;elected t he fIrum group consis~t intig ()I de t c rkent f ille rs, detergent- bii lde rt Si t act ant S'

1 eqtiestrants and chelating aqeritii 13. A cleaning comnpos i tion xipr.iirg a )about 0.3-'20 wt- ha-,ed uponl tile c I caningk COMpO.sIt ion, en[capSulated enzyme which about w t-7p k~e t hie 201 tlncapsu la ted enzyme enZYMe COI"; (ii) about I wt 1;ke( upon t he~ encapsu'Ilated envz yre ,t t. e ncai u at i nq c 'at ink rog a chlorine bleachneut r~ I is-i rig ;htac and i ii) abou t V wt 1, based upon t he 21) t icpiI~at~(l enizymie, seconid enxxnpsu I at i Aq civt ig of! a t ire--re Lea- substan-e; at lePast a1 siit f i cut 111 ni ricti t -a I Ii

ani1ount, (t ail erzCaPSu tidi Mernt whiichi ctipt isvs: i) about I W 'AUae r~Po t ile P1eiuxidpsu bat6ed" (ii ucrit d; Illerit c'ol e; (ii) about. IAC wt based upon~l t he encapsu lat ed di I uvnt !iArit Pntcapsu at Uh tg ht't ig oA a ch lor i ne hieachneut rA z r. Ig sut nice; ari i ii) about 1 W 1. ism! UDi. he rlIap.suIlated di Iveiit iel.'i(1 ent-apiu lat igl ocat

(it a t ime- re Iease itiit .inc'e c) lint G. 1 40 wt A bwa;d uponl t he c I c, 11c

Claims (1)

1. composition, chlorine bleach; and about 55-95 based upon the cleaning composition, adaitional detergent components selected from the group consisting of detergent fillers, detergent builders, surfactants, sequestrants, and chelating agents. 14. The cleaning composition of claim 10 or 11 wherein the enzyme is a protease, lipase, amylases, or mixture thereof. 15. Th- cleaning compoition of claims 10 or 11 wherein the chlorine bleach-neutralizing substance is a sulf-oxy acid or salt thereof. 16. The cleaning composition of claims 10 or 11 wherein the chlorine bleach-neutralizing substance is a perborate, persulfate, perphosphate, or percarbonate. 17. The cleaning composition of claim 10 or 11 wherein the time-release substance is a cellulose derivative.

   DATED THIS 31S"' DAY OF DCEMBER 1987 ECOLAB INC. By Its Patent Attorneys: CLEMENT HACK CO, Fellows Institute of Patent Attorneys of Australia

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