US3746621A - Preparation of enzyme containing microcapsule - Google Patents
Preparation of enzyme containing microcapsule Download PDFInfo
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- US3746621A US3746621A US00836066A US3746621DA US3746621A US 3746621 A US3746621 A US 3746621A US 00836066 A US00836066 A US 00836066A US 3746621D A US3746621D A US 3746621DA US 3746621 A US3746621 A US 3746621A
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- binder
- enzyme
- solvent
- dispersion
- swellable
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- 102000004190 Enzymes Human genes 0.000 title abstract description 38
- 108090000790 Enzymes Proteins 0.000 title abstract description 38
- 239000003094 microcapsule Substances 0.000 title abstract description 13
- 238000002360 preparation method Methods 0.000 title description 3
- 239000006185 dispersion Substances 0.000 abstract description 18
- 239000002904 solvent Substances 0.000 abstract description 18
- 239000007787 solid Substances 0.000 abstract description 13
- 238000000034 method Methods 0.000 abstract description 11
- 238000004925 denaturation Methods 0.000 abstract description 5
- 230000036425 denaturation Effects 0.000 abstract description 5
- 238000001694 spray drying Methods 0.000 abstract description 4
- 239000011230 binding agent Substances 0.000 description 37
- 229940088598 enzyme Drugs 0.000 description 36
- 239000000243 solution Substances 0.000 description 16
- 239000002245 particle Substances 0.000 description 12
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 11
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 11
- 108010010803 Gelatin Proteins 0.000 description 10
- 102000004882 Lipase Human genes 0.000 description 10
- 108090001060 Lipase Proteins 0.000 description 10
- 239000004367 Lipase Substances 0.000 description 10
- 229920000159 gelatin Polymers 0.000 description 10
- 239000008273 gelatin Substances 0.000 description 10
- 235000019322 gelatine Nutrition 0.000 description 10
- 235000011852 gelatine desserts Nutrition 0.000 description 10
- 235000019421 lipase Nutrition 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 239000002775 capsule Substances 0.000 description 8
- 229920001577 copolymer Polymers 0.000 description 8
- 229920002307 Dextran Polymers 0.000 description 7
- 239000004375 Dextrin Substances 0.000 description 7
- 229920001353 Dextrin Polymers 0.000 description 7
- 239000005018 casein Substances 0.000 description 7
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 7
- 235000021240 caseins Nutrition 0.000 description 7
- 235000019425 dextrin Nutrition 0.000 description 7
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 239000007864 aqueous solution Substances 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- 239000000377 silicon dioxide Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 229920000084 Gum arabic Polymers 0.000 description 4
- 239000004372 Polyvinyl alcohol Substances 0.000 description 4
- 241000978776 Senegalia senegal Species 0.000 description 4
- 229920002472 Starch Polymers 0.000 description 4
- 235000010489 acacia gum Nutrition 0.000 description 4
- 239000000205 acacia gum Substances 0.000 description 4
- 239000003960 organic solvent Substances 0.000 description 4
- 229920002451 polyvinyl alcohol Polymers 0.000 description 4
- 235000019422 polyvinyl alcohol Nutrition 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 3
- 241000206672 Gelidium Species 0.000 description 3
- 235000010419 agar Nutrition 0.000 description 3
- 239000001913 cellulose Substances 0.000 description 3
- 229920002678 cellulose Polymers 0.000 description 3
- 239000004927 clay Substances 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 238000001035 drying Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 235000010413 sodium alginate Nutrition 0.000 description 3
- 239000000661 sodium alginate Substances 0.000 description 3
- 229940005550 sodium alginate Drugs 0.000 description 3
- 239000007921 spray Substances 0.000 description 3
- QCZAWDGAVJMPTA-RNFRBKRXSA-N ClC1=CC=CC(=N1)C1=NC(=NC(=N1)N[C@@H](C(F)(F)F)C)N[C@@H](C(F)(F)F)C Chemical compound ClC1=CC=CC(=N1)C1=NC(=NC(=N1)N[C@@H](C(F)(F)F)C)N[C@@H](C(F)(F)F)C QCZAWDGAVJMPTA-RNFRBKRXSA-N 0.000 description 2
- 238000005054 agglomeration Methods 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 108010058314 rennet Proteins 0.000 description 2
- 239000002195 soluble material Substances 0.000 description 2
- 238000005507 spraying Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 108700023418 Amidases Proteins 0.000 description 1
- 102000004867 Hydro-Lyases Human genes 0.000 description 1
- 108090001042 Hydro-Lyases Proteins 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 235000010724 Wisteria floribunda Nutrition 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000001112 coagulating effect Effects 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- NIQQIJXGUZVEBB-UHFFFAOYSA-N methanol;propan-2-one Chemical compound OC.CC(C)=O NIQQIJXGUZVEBB-UHFFFAOYSA-N 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 229940108461 rennet Drugs 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- -1 vinyl methyl Chemical group 0.000 description 1
Images
Classifications
-
- 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/04—Enzymes or microbial cells immobilised on or in an organic carrier entrapped within the carrier, e.g. gel or hollow fibres
Definitions
- ABSTRACT OF THE DISCLOSURE A method for making enzyme-containing microcapsules and the resulting product including forming a dispersion of an enzyme, a binder, a solvent for the binder, and a swellable solid which is insoluble in said solvent, and spray drying the dispersion at a temperature below that which the enzyme undergoes denaturation.
- powdery enzymes in most cases, are fairly quickly deactivated by the presence of moisture or contact by other substances. For instance, powdered lipase, when mixed with a detergent for cleaning use, often loses its activity due to the influence of the coexisting detergent. Furthermore, certain powdered enzymes agglomerate through absorption of moisture in air or partially agglomerate when put in water to form aqueous solutions. This makes it difficult to rapidly prepare an aqueous solution of the enzyme.
- the enzyme-containing microcapsules of the present invention overcome such drawbacks immediately. That is to say, by micro-encapsulation, the enzyme is protected from moisture in the air as well as from contact with other substances, and the microcapsules do not agglomerate in air since they are in the form of spherical solid particles. When put in water, the microcapsule is expanded and broken down by the action of the swellable particles, contained therein, to form an aqueous enzyme solution without agglomeration.
- the enzyme-containing capsules of the present invention are produced by forming a dispersion of an enzyme, a binder material, a solvent for said binder,
- the binder may be either Water or organic compound soluble.
- the enzyme is dissolved or dispersed in a solution of the binder and solvent.
- the swellable particles are then dispersed in the mixture and the resulting dispersion is dried.
- the enzyme and/or the swellable agent may be dispersed in a solvent prior to mixing in the binder solution.
- the solvent utilized under these circumstances may be the same or different from the binder solvent but must be one which will not deleteriously aifect the resulting dispersion and drying steps.
- microcapsules that are the product of the present invention vary in size according to the scale and type of spraying apparatus utilized. In general, the product size varies from a few to several thousand microns. The present invention, however, preferably contemplates atomizing so as to obtain particles of from about 10 to 2000 microns.
- FIG. 1 is a diagrammatic cross-sectional view of an enzyme-containing microcapsule in accordance with the present invention, wherein tightly packed particles 1 of powdered enzyme and swellable particles 2 are enclosed by a binder substance 3.
- a binder solution used in the practice of the present invention there are included solutions of methanol, acetone, or like organic solvents, of a waterand organic solvent-soluble material, such as ethylene-maleic anhyhydride copolymers, vinyl methyl ether-maleic anhydride copolymers or the like.
- aqueous solutions of a water-soluble material such as gelatin casein, dextrin, dextran, gum arabic, cellulose derivatives, polyvinyl alcohol (PVA), agar-agar, sodium alginate or the like, may be utilized.
- the conncentration of the solution may be varied from about 0.1% to about 20%, preferably 1 to 20% by weight depending on the viscosity.
- the binder termined by experimentation.
- the binder should be used in as small an amount as possible, as debe such that it is unaffected by the enzyme incorporated therein.
- the binders which are preferred in the practice of the present invention must keep the enzyme active, and include those which exhibit excellent affinity for water, and dissolve in organic solvents having low boiling points.
- Exemplary of such binders are vinyl methyl ethermaleic acid or anhydride copolymers (PVM/MA) gum arabic and dextrin.
- the swellable particles are finely divided solids that do not react with the binder, do not deactivate the enzyme, are insoluble in the solvent for the binder, and undergo such physical changes as solution, swelling and breakdown upon contact with water.
- Examples are silica, clay, starch, powdered dextran, gelatin, cured gelatin, casein, and the like. Among these, silica and starch are easily obtainable and function well in the present invention.
- the swellable powder is preferably present in an amount of from 0.5 to 30 times the amount of binder present by weight.
- Methanolacetone PVM/MA PVA Starch S102 For spray drying there may be employed any of the commercially available spray dryers, for example, both centrifugal atomizer-type and spray nozzle-type dryers may be used. Since most enzymes undergo denaturation at temperatures above 60 C. the drying is advantageously carried out at room temperature or at a somewhat elevated temperature at which the inside of the capsule is maintained at a temperature that does not cause denaturation of enzyme. Exemplary drying temperatures are: organic solvent, inlet 80 C., outlet 60 C., and water, inlet 150 C., outlet 100 C.
- the swellable powder utilized in the present invention is necessary in order to allow the capsule to dissolve quickly.
- gelatin When gelatin is utilized as the swellable material, it is usually dispersed into a PVM/MA-acetone solution.
- dextrin when used as a binder, an aqueous solution is formed, but when used as the swellable agent, the dextrin is dispersed in an organic solvent, Also, since casein is an alkali soluble, it may be used as a binder in weak alkali solutions, but in other cases operates as the swellable powder.
- EXAMPLE I A binder solution prepared by dissolving 20 g. of an ethylene-maleic anhydride copolymer in 100 m1. of a 1:1 mixture of methanol and acetone was mixed with a liquid dispersion prepared by dispersing 100 g. of powdered lipase and 80 g. of powdered dextran in '800 ml. of acetone to form a spraying liquid dispersion. The dispersion was sprayed through a nozzle having a diameter of 1.3 mm. under a pressure of 1 kg./cm. gauge into a dryer chamber of a diameter of 1 m. and a depth of 2 m. while passing therethrough 1.3 cubic meters per minute of hot air.
- the air temperature at inlet was 70 C. and at outlet was 40 C.
- the lipase-containing capsule exhibited a rate of solution substantially equal to that of the powdered lipase before encapsulization.
- the capsule was stored in mixture with a commercially available granulated detergent for 3 months without any decrease in the activity of lipase being observed.
- Example II The procedure of Example I was used but the milk coagulating enzyme rennet was used in place of lipase. The rennet-containing capsule thus obtained quickly dissolved in water or milk without any agglomeration.
- EXAMPLE III An aqueous binder solution prepared by dissolving 20 g. of dextrin in 300 ml. of water was mixed with a liquid dispersion prepared by dispersing 200 g. of fine silica and 20 g. of lipase in 350 ml. of acetone. The liquid dispersion, thus formed, was subjected to microencapsulation by means of a Minor Unit Spray Dryer. The dryer was operated at a speed of 20,000 r.p.m., a
- An enzyme-containing microcapsule comprising an enzyme and particles of a finely divided swellable solid encapsulated in a binder substance, which is unafiected by the enzyme said swellable solid being inert with respect to the binder substance, and said swellable solid being present in an amount of from 0.5 to 30 times the amount of binder present by weight.
- said binder is a member selected from the group consisting of ethylene-maleic anhydride copolymers, vinylmethyl ether maleic anhydride copolymers, gelatin, casein, dextrin, dextran, gum arabic, cellulose derivatives, polyvinyl alcohol, agar-agar, and sodium alginate.
- swellable solid is a member selected from the group consisting of silica, clay, starch, powdered dextran, gelatin, cured gelatin and casein.
- a method of producing enzyme-containing microcapsules comprising forming a liquid dispersion of an enzyme, a binder, a solvent for said binder, and a finely divided swellable solid, inert with respect to said binder, which is insoluble in said solvent, and spray drying said dispersion at a temperature below that which the enzyme undergoes denaturation, said binder being present in an amount of from 0.1 to 20.0% by weight based on the dispersion, said binder being unaffected by the enzyme.
- said binder is a member selected from the group consisting of ethylenemaleic anhydride copolymers, vinylmethyl ether maleic anhydride copolymers, gelatin, casein, dextrin, dextran, gum arabic, cellulose derivatives, polyvinyl alcohol, agaragar, and sodium alginate.
- said swellable solid is a member selected from the group consisting of silica, clay, starch, powdered dextran, gelatin, cured gelatin, and casein.
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- Engineering & Computer Science (AREA)
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- Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Dispersion Chemistry (AREA)
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Abstract
A METHOD FOR MAKING ENZYME-CONTAINING MICROCAPSULES AND THE RESULTING PRODUCT INCLUDING FORMING A DISPERSION OF AN ANZYME, A BINDER, A SOLVENT FOR THE BINDER, AND A SWELLABLE SOLID WHICH IS INSOLUBLE IN SAID SOLVENT, AND SPRAY DRYING THE DISPERSION AT A TEMPERATURE BELOW THAT WHICH THE ENZYME UNDERGOES DENATURATION.
Description
July 17, 1973 ASAJII KONDQ ETAL 3,746,621
PREPARATION OF ENZYME-CONTAINING Mxcnocmsum;
Filed June 24, 1969 United States Patent 3,746,621 PREPARATION OF ENZYME-CONTAINING MICROCAPSULE Asaji Kondo, Masao Kitajima, and Shizuo Miyano, Asakishi, Japan, assignors to Fuji Photo Film Co., Ltd., Kanagawa, Japan Filed June 24, 1969, Ser. No. 836,066 Claims priority, application Japan, June 25, 1968, 43/ 44,099 Int. Cl. C07g 7/02 US. Cl. 195-63 11 Claims ABSTRACT OF THE DISCLOSURE A method for making enzyme-containing microcapsules and the resulting product including forming a dispersion of an enzyme, a binder, a solvent for the binder, and a swellable solid which is insoluble in said solvent, and spray drying the dispersion at a temperature below that which the enzyme undergoes denaturation.
BACKGROUND OF THE INVENTION (1) Field of the invention (2) Description of the prior art There are a variety of commercially available enzymes, such as protease, lipase, carbohydrease and the like, that act on high molecular weight substrates, also enzymes, such as peroxidase, hydrase, amidase and the like, that act on low molecular weight substrates are available. These enzymes, and others are generally commercially available in the form of a dried powder. They are prepared, usually, from aqueous solutions of crude enzymes by addition of acetone, alcohols or the like as a precipitant.
The powdery enzymes, in most cases, are fairly quickly deactivated by the presence of moisture or contact by other substances. For instance, powdered lipase, when mixed with a detergent for cleaning use, often loses its activity due to the influence of the coexisting detergent. Furthermore, certain powdered enzymes agglomerate through absorption of moisture in air or partially agglomerate when put in water to form aqueous solutions. This makes it difficult to rapidly prepare an aqueous solution of the enzyme.
The enzyme-containing microcapsules of the present invention overcome such drawbacks immediately. That is to say, by micro-encapsulation, the enzyme is protected from moisture in the air as well as from contact with other substances, and the microcapsules do not agglomerate in air since they are in the form of spherical solid particles. When put in water, the microcapsule is expanded and broken down by the action of the swellable particles, contained therein, to form an aqueous enzyme solution without agglomeration.
ice
BRIEF DESCRIPTION OF THE INVENTION In general, the enzyme-containing capsules of the present invention are produced by forming a dispersion of an enzyme, a binder material, a solvent for said binder,
and swellable particles which are insoluble in the solvent.
The binder may be either Water or organic compound soluble.
In one embodiment of the present invention the enzyme is dissolved or dispersed in a solution of the binder and solvent. The swellable particles are then dispersed in the mixture and the resulting dispersion is dried. However, when the enzyme and/or the swellable agent are hard to dissolve or disperse in the binder solution, they may be dispersed in a solvent prior to mixing in the binder solution. The solvent utilized under these circumstances may be the same or different from the binder solvent but must be one which will not deleteriously aifect the resulting dispersion and drying steps.
The microcapsules that are the product of the present invention vary in size according to the scale and type of spraying apparatus utilized. In general, the product size varies from a few to several thousand microns. The present invention, however, preferably contemplates atomizing so as to obtain particles of from about 10 to 2000 microns.
In the accompanying drawing, the figure is a diagrammatic cross-sectional view of an enzyme-containing microcapsule in accordance with the present invention, wherein tightly packed particles 1 of powdered enzyme and swellable particles 2 are enclosed by a binder substance 3.
As a binder solution used in the practice of the present invention, there are included solutions of methanol, acetone, or like organic solvents, of a waterand organic solvent-soluble material, such as ethylene-maleic anhyhydride copolymers, vinyl methyl ether-maleic anhydride copolymers or the like. Also, aqueous solutions of a water-soluble material, such as gelatin casein, dextrin, dextran, gum arabic, cellulose derivatives, polyvinyl alcohol (PVA), agar-agar, sodium alginate or the like, may be utilized. The conncentration of the solution may be varied from about 0.1% to about 20%, preferably 1 to 20% by weight depending on the viscosity. However, in order to attain quick breakdown in water, the binder termined by experimentation. Of course, the binder should should be used in as small an amount as possible, as debe such that it is unaffected by the enzyme incorporated therein. The binders which are preferred in the practice of the present invention, must keep the enzyme active, and include those which exhibit excellent affinity for water, and dissolve in organic solvents having low boiling points. Exemplary of such binders are vinyl methyl ethermaleic acid or anhydride copolymers (PVM/MA) gum arabic and dextrin.
The swellable particles are finely divided solids that do not react with the binder, do not deactivate the enzyme, are insoluble in the solvent for the binder, and undergo such physical changes as solution, swelling and breakdown upon contact with water. Examples are silica, clay, starch, powdered dextran, gelatin, cured gelatin, casein, and the like. Among these, silica and starch are easily obtainable and function well in the present invention. The swellable powder is preferably present in an amount of from 0.5 to 30 times the amount of binder present by weight.
Methanolacetone PVM/MA PVA Starch S102 For spray drying there may be employed any of the commercially available spray dryers, for example, both centrifugal atomizer-type and spray nozzle-type dryers may be used. Since most enzymes undergo denaturation at temperatures above 60 C. the drying is advantageously carried out at room temperature or at a somewhat elevated temperature at which the inside of the capsule is maintained at a temperature that does not cause denaturation of enzyme. Exemplary drying temperatures are: organic solvent, inlet 80 C., outlet 60 C., and water, inlet 150 C., outlet 100 C.
The swellable powder utilized in the present invention is necessary in order to allow the capsule to dissolve quickly. When gelatin is utilized as the swellable material, it is usually dispersed into a PVM/MA-acetone solution. However, when dextrin is used as a binder, an aqueous solution is formed, but when used as the swellable agent, the dextrin is dispersed in an organic solvent, Also, since casein is an alkali soluble, it may be used as a binder in weak alkali solutions, but in other cases operates as the swellable powder.
EXAMPLE I A binder solution prepared by dissolving 20 g. of an ethylene-maleic anhydride copolymer in 100 m1. of a 1:1 mixture of methanol and acetone was mixed with a liquid dispersion prepared by dispersing 100 g. of powdered lipase and 80 g. of powdered dextran in '800 ml. of acetone to form a spraying liquid dispersion. The dispersion was sprayed through a nozzle having a diameter of 1.3 mm. under a pressure of 1 kg./cm. gauge into a dryer chamber of a diameter of 1 m. and a depth of 2 m. while passing therethrough 1.3 cubic meters per minute of hot air. The air temperature at inlet was 70 C. and at outlet was 40 C. Thus, there was obtained 130 g. of lipase-containing capsules of particle sizes of from 20 microns to 100 microns. The lipase-containing capsule exhibited a rate of solution substantially equal to that of the powdered lipase before encapsulization. The capsule was stored in mixture with a commercially available granulated detergent for 3 months without any decrease in the activity of lipase being observed.
EXAMPLE II The procedure of Example I was used but the milk coagulating enzyme rennet was used in place of lipase. The rennet-containing capsule thus obtained quickly dissolved in water or milk without any agglomeration.
EXAMPLE III An aqueous binder solution prepared by dissolving 20 g. of dextrin in 300 ml. of water was mixed with a liquid dispersion prepared by dispersing 200 g. of fine silica and 20 g. of lipase in 350 ml. of acetone. The liquid dispersion, thus formed, was subjected to microencapsulation by means of a Minor Unit Spray Dryer. The dryer was operated at a speed of 20,000 r.p.m., a
temperature, at inlet of C., temperature, at outlet, of 60 C., and with an air stream of 1 cubic meter per minute. The dropping rate of the dispersion was 500 ml./ hr. Thus, there were obtained 100 g. of lipase-containing capsules having particle sizes of from 20 microns to 50 microns.
We claim:
' 1. An enzyme-containing microcapsule comprising an enzyme and particles of a finely divided swellable solid encapsulated in a binder substance, which is unafiected by the enzyme said swellable solid being inert with respect to the binder substance, and said swellable solid being present in an amount of from 0.5 to 30 times the amount of binder present by weight.
2. The enzyme-containing microcapsule of claim 1, wherein said binder is a member selected from the group consisting of ethylene-maleic anhydride copolymers, vinylmethyl ether maleic anhydride copolymers, gelatin, casein, dextrin, dextran, gum arabic, cellulose derivatives, polyvinyl alcohol, agar-agar, and sodium alginate.
3. The enzyme-containing microcapsule of claim 1, wherein said swellable solid is a member selected from the group consisting of silica, clay, starch, powdered dextran, gelatin, cured gelatin and casein.
4. A method of producing enzyme-containing microcapsules comprising forming a liquid dispersion of an enzyme, a binder, a solvent for said binder, and a finely divided swellable solid, inert with respect to said binder, which is insoluble in said solvent, and spray drying said dispersion at a temperature below that which the enzyme undergoes denaturation, said binder being present in an amount of from 0.1 to 20.0% by weight based on the dispersion, said binder being unaffected by the enzyme.
5. The method of claim 4, wherein said binder is a member selected from the group consisting of ethylenemaleic anhydride copolymers, vinylmethyl ether maleic anhydride copolymers, gelatin, casein, dextrin, dextran, gum arabic, cellulose derivatives, polyvinyl alcohol, agaragar, and sodium alginate.
6. The method of claim 4, wherein said swellable solid is a member selected from the group consisting of silica, clay, starch, powdered dextran, gelatin, cured gelatin, and casein.
7. The method of claim 4, wherein said binder is present in an amount of from 1.0 to 20.0% by weight.
8. The method of claim 4, wherein said swellable solid is present in an amount of from 0.5 to 30 times the amount of binder present by weight.
9. The method of claim 4, wherein said dispersion is formed by dissolving or dispersing said enzyme in a solution of said binder and said solvent, and dispersing therein particles of said swellable solid.
10. The method of claim 4, wherein said enzyme is dissolved in a portion of said solvent prior to being dispersed or dissolved in a solution of said binder and solvent.
11. The method of claim 4, wherein said enzyme and said swellable solid are dissolved in a solvent therefor prior to forming the dispersion with a solution of said binder and solvent.
References Cited UNITED STATES PATENTS 2,642,376 6/195'3 Gale et al. -63 3,091,567 5/1963 Wurzburg et a1. 424-35 3,181,998 5/1965 Kanig 195--63 X 3,455,838 7/1969 Marotta et a1 252-316 A. LOUIS MONACE'LL, Primary Examiner D. M. NA'FF, Assistant Examiner US. Cl. X.R. 195-68
Applications Claiming Priority (1)
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JP4409968 | 1968-06-25 |
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Cited By (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3849253A (en) * | 1972-10-10 | 1974-11-19 | Penick & Ford Ltd | Process of immobilizing enzymes |
US4063017A (en) * | 1976-04-22 | 1977-12-13 | Purdue Research Foundation | Porous cellulose beads and the immobilization of enzymes therewith |
EP0060052A1 (en) * | 1981-02-27 | 1982-09-15 | Research Association For Petroleum Alternative Development | Method of immobilizing live microorganisms |
US4617272A (en) * | 1984-04-25 | 1986-10-14 | Economics Laboratory, Inc. | Enzyme drying process |
US4678594A (en) * | 1985-07-19 | 1987-07-07 | Colgate-Palmolive Company | Method of encapsulating a bleach and activator therefor in a binder |
US5100668A (en) * | 1988-06-14 | 1992-03-31 | Massachusetts Institute Of Technology | Controlled release systems containing heparin and growth factors |
US5468622A (en) * | 1990-04-03 | 1995-11-21 | Immunomatrix, Inc. | Salt stabilization of antibody-enzyme conjugates heat-dried into paper |
WO1996001048A1 (en) * | 1994-07-06 | 1996-01-18 | Zeneca Limited | Solid microspheres for agriculturally active compounds and process for their production |
WO2002023998A1 (en) * | 2000-09-19 | 2002-03-28 | Dsm N.V. | Targeting of active compounds to curd during cheese making |
US20100286019A1 (en) * | 2007-01-12 | 2010-11-11 | Scher Herbert B | Spray Drying Process |
US20120017947A1 (en) * | 2010-07-20 | 2012-01-26 | Susana Fernandez Prieto | Delivery particle |
EP2508598A1 (en) * | 2009-12-01 | 2012-10-10 | The Nisshin OilliO Group, Ltd. | Lipase powder preparation and use thereof |
-
1969
- 1969-06-24 US US00836066A patent/US3746621A/en not_active Expired - Lifetime
Cited By (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3849253A (en) * | 1972-10-10 | 1974-11-19 | Penick & Ford Ltd | Process of immobilizing enzymes |
US4063017A (en) * | 1976-04-22 | 1977-12-13 | Purdue Research Foundation | Porous cellulose beads and the immobilization of enzymes therewith |
US4090022A (en) * | 1976-04-22 | 1978-05-16 | Purdue Research Foundation | Porous cellulose beads |
EP0060052A1 (en) * | 1981-02-27 | 1982-09-15 | Research Association For Petroleum Alternative Development | Method of immobilizing live microorganisms |
US4617272A (en) * | 1984-04-25 | 1986-10-14 | Economics Laboratory, Inc. | Enzyme drying process |
US4678594A (en) * | 1985-07-19 | 1987-07-07 | Colgate-Palmolive Company | Method of encapsulating a bleach and activator therefor in a binder |
US5100668A (en) * | 1988-06-14 | 1992-03-31 | Massachusetts Institute Of Technology | Controlled release systems containing heparin and growth factors |
US5637468A (en) * | 1990-04-03 | 1997-06-10 | Immunomatrix, Inc. | Salt stabilization of antibody-enzyme conjugates heat-dried into paper |
US5468622A (en) * | 1990-04-03 | 1995-11-21 | Immunomatrix, Inc. | Salt stabilization of antibody-enzyme conjugates heat-dried into paper |
WO1996001048A1 (en) * | 1994-07-06 | 1996-01-18 | Zeneca Limited | Solid microspheres for agriculturally active compounds and process for their production |
US5639710A (en) * | 1994-07-06 | 1997-06-17 | Zeneca Limited | Solid microspheres for agriculturally active compounds and process for their production |
WO2002023998A1 (en) * | 2000-09-19 | 2002-03-28 | Dsm N.V. | Targeting of active compounds to curd during cheese making |
US20030185938A1 (en) * | 2000-09-19 | 2003-10-02 | De Haan Ben Rudolf | Targeting of active compounds to curd during cheese making |
US20100286019A1 (en) * | 2007-01-12 | 2010-11-11 | Scher Herbert B | Spray Drying Process |
EP2508598A1 (en) * | 2009-12-01 | 2012-10-10 | The Nisshin OilliO Group, Ltd. | Lipase powder preparation and use thereof |
EP2508598A4 (en) * | 2009-12-01 | 2013-05-29 | Nisshin Oillio Group Ltd | Lipase powder preparation and use thereof |
US20120017947A1 (en) * | 2010-07-20 | 2012-01-26 | Susana Fernandez Prieto | Delivery particle |
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