CN115322844A - Biological enzyme capsule and preparation method thereof - Google Patents
Biological enzyme capsule and preparation method thereof Download PDFInfo
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- CN115322844A CN115322844A CN202211024705.8A CN202211024705A CN115322844A CN 115322844 A CN115322844 A CN 115322844A CN 202211024705 A CN202211024705 A CN 202211024705A CN 115322844 A CN115322844 A CN 115322844A
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- capsule
- hydrogel
- enzyme
- biological enzyme
- biological
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- 239000002775 capsule Substances 0.000 title claims abstract description 116
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 82
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 82
- 238000002360 preparation method Methods 0.000 title claims abstract description 22
- 239000007788 liquid Substances 0.000 claims abstract description 38
- 239000000017 hydrogel Substances 0.000 claims abstract description 36
- 239000000463 material Substances 0.000 claims abstract description 31
- 239000000243 solution Substances 0.000 claims abstract description 24
- 239000011162 core material Substances 0.000 claims abstract description 19
- 238000000034 method Methods 0.000 claims abstract description 17
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 16
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 claims abstract description 12
- 239000001110 calcium chloride Substances 0.000 claims abstract description 12
- 229910001628 calcium chloride Inorganic materials 0.000 claims abstract description 12
- 239000007864 aqueous solution Substances 0.000 claims abstract description 11
- 150000005846 sugar alcohols Polymers 0.000 claims abstract description 10
- 238000001914 filtration Methods 0.000 claims abstract description 9
- 239000000499 gel Substances 0.000 claims abstract description 9
- 238000002156 mixing Methods 0.000 claims abstract description 8
- 230000018044 dehydration Effects 0.000 claims abstract description 5
- 238000006297 dehydration reaction Methods 0.000 claims abstract description 5
- 239000011258 core-shell material Substances 0.000 claims abstract description 3
- 229940088598 enzyme Drugs 0.000 claims description 80
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 claims description 33
- 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 claims description 13
- 229920001817 Agar Polymers 0.000 claims description 13
- 239000008272 agar Substances 0.000 claims description 13
- 235000010413 sodium alginate Nutrition 0.000 claims description 13
- 239000000661 sodium alginate Substances 0.000 claims description 13
- 229940005550 sodium alginate Drugs 0.000 claims description 13
- 108091005804 Peptidases Proteins 0.000 claims description 12
- 239000004372 Polyvinyl alcohol Substances 0.000 claims description 12
- 239000004365 Protease Substances 0.000 claims description 12
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 12
- 229920002451 polyvinyl alcohol Polymers 0.000 claims description 12
- 235000019419 proteases Nutrition 0.000 claims description 12
- 108010059892 Cellulase Proteins 0.000 claims description 11
- 229940106157 cellulase Drugs 0.000 claims description 11
- 235000013772 propylene glycol Nutrition 0.000 claims description 11
- 239000004382 Amylase Substances 0.000 claims description 10
- 102000013142 Amylases Human genes 0.000 claims description 10
- 108010065511 Amylases Proteins 0.000 claims description 10
- 235000019418 amylase Nutrition 0.000 claims description 10
- 102000004882 Lipase Human genes 0.000 claims description 9
- 239000004367 Lipase Substances 0.000 claims description 9
- 108090001060 Lipase Proteins 0.000 claims description 9
- 229940040461 lipase Drugs 0.000 claims description 9
- 235000019421 lipase Nutrition 0.000 claims description 9
- 238000001816 cooling Methods 0.000 claims description 8
- 102100032487 Beta-mannosidase Human genes 0.000 claims description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 claims description 6
- 108010059820 Polygalacturonase Proteins 0.000 claims description 6
- 108010055059 beta-Mannosidase Proteins 0.000 claims description 6
- 108010093305 exopolygalacturonase Proteins 0.000 claims description 6
- -1 carboxypropyl Chemical group 0.000 claims description 4
- 239000001913 cellulose Substances 0.000 claims description 4
- 229920002678 cellulose Polymers 0.000 claims description 4
- 229920002134 Carboxymethyl cellulose Polymers 0.000 claims description 3
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- 235000010948 carboxy methyl cellulose Nutrition 0.000 claims description 3
- 239000008112 carboxymethyl-cellulose Substances 0.000 claims description 3
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 claims description 2
- 241000220479 Acacia Species 0.000 claims description 2
- 241001116389 Aloe Species 0.000 claims description 2
- 229920001661 Chitosan Polymers 0.000 claims description 2
- 229920000858 Cyclodextrin Polymers 0.000 claims description 2
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 claims description 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 claims description 2
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 claims description 2
- 229920002307 Dextran Polymers 0.000 claims description 2
- 239000001856 Ethyl cellulose Substances 0.000 claims description 2
- ZZSNKZQZMQGXPY-UHFFFAOYSA-N Ethyl cellulose Chemical compound CCOCC1OC(OC)C(OCC)C(OCC)C1OC1C(O)C(O)C(OC)C(CO)O1 ZZSNKZQZMQGXPY-UHFFFAOYSA-N 0.000 claims description 2
- 235000010643 Leucaena leucocephala Nutrition 0.000 claims description 2
- 229930195725 Mannitol Natural products 0.000 claims description 2
- 108010014251 Muramidase Proteins 0.000 claims description 2
- 102000016943 Muramidase Human genes 0.000 claims description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 2
- 229940023476 agar Drugs 0.000 claims description 2
- 235000011399 aloe vera Nutrition 0.000 claims description 2
- 239000011324 bead Substances 0.000 claims description 2
- 229960002086 dextran Drugs 0.000 claims description 2
- 235000019325 ethyl cellulose Nutrition 0.000 claims description 2
- 229920001249 ethyl cellulose Polymers 0.000 claims description 2
- 235000011187 glycerol Nutrition 0.000 claims description 2
- 229920002674 hyaluronan Polymers 0.000 claims description 2
- 229960003160 hyaluronic acid Drugs 0.000 claims description 2
- 239000001866 hydroxypropyl methyl cellulose Substances 0.000 claims description 2
- 235000010979 hydroxypropyl methyl cellulose Nutrition 0.000 claims description 2
- 229920003088 hydroxypropyl methyl cellulose Polymers 0.000 claims description 2
- UFVKGYZPFZQRLF-UHFFFAOYSA-N hydroxypropyl methyl cellulose Chemical compound OC1C(O)C(OC)OC(CO)C1OC1C(O)C(O)C(OC2C(C(O)C(OC3C(C(O)C(O)C(CO)O3)O)C(CO)O2)O)C(CO)O1 UFVKGYZPFZQRLF-UHFFFAOYSA-N 0.000 claims description 2
- 239000004325 lysozyme Substances 0.000 claims description 2
- 229960000274 lysozyme Drugs 0.000 claims description 2
- 235000010335 lysozyme Nutrition 0.000 claims description 2
- 239000000845 maltitol Substances 0.000 claims description 2
- VQHSOMBJVWLPSR-WUJBLJFYSA-N maltitol Chemical compound OC[C@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O VQHSOMBJVWLPSR-WUJBLJFYSA-N 0.000 claims description 2
- 235000010449 maltitol Nutrition 0.000 claims description 2
- 229940035436 maltitol Drugs 0.000 claims description 2
- 239000000594 mannitol Substances 0.000 claims description 2
- 235000010355 mannitol Nutrition 0.000 claims description 2
- 229920000609 methyl cellulose Polymers 0.000 claims description 2
- 239000001923 methylcellulose Substances 0.000 claims description 2
- 235000010981 methylcellulose Nutrition 0.000 claims description 2
- 239000001267 polyvinylpyrrolidone Substances 0.000 claims description 2
- 229920000036 polyvinylpyrrolidone Polymers 0.000 claims description 2
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 claims description 2
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 claims description 2
- 235000010356 sorbitol Nutrition 0.000 claims description 2
- 239000000600 sorbitol Substances 0.000 claims description 2
- 229920005862 polyol Polymers 0.000 claims 1
- 150000003077 polyols Chemical class 0.000 claims 1
- 230000000694 effects Effects 0.000 abstract description 21
- 239000000126 substance Substances 0.000 abstract description 3
- 239000003599 detergent Substances 0.000 description 26
- 230000000052 comparative effect Effects 0.000 description 10
- 239000008187 granular material Substances 0.000 description 8
- 229920000642 polymer Polymers 0.000 description 5
- 239000003381 stabilizer Substances 0.000 description 5
- PTHCMJGKKRQCBF-UHFFFAOYSA-N Cellulose, microcrystalline Chemical compound OC1C(O)C(OC)OC(CO)C1OC1C(O)C(O)C(OC)C(CO)O1 PTHCMJGKKRQCBF-UHFFFAOYSA-N 0.000 description 4
- 229920002472 Starch Polymers 0.000 description 4
- 238000005520 cutting process Methods 0.000 description 4
- 108010025899 gelatin film Proteins 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- 239000004094 surface-active agent Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 239000004375 Dextrin Substances 0.000 description 3
- 229920001353 Dextrin Polymers 0.000 description 3
- 235000019425 dextrin Nutrition 0.000 description 3
- 238000007046 ethoxylation reaction Methods 0.000 description 3
- 230000014759 maintenance of location Effects 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 239000002102 nanobead Substances 0.000 description 3
- 229920001184 polypeptide Polymers 0.000 description 3
- 239000003755 preservative agent Substances 0.000 description 3
- 230000002335 preservative effect Effects 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 239000003945 anionic surfactant Substances 0.000 description 2
- DMSMPAJRVJJAGA-UHFFFAOYSA-N benzo[d]isothiazol-3-one Chemical compound C1=CC=C2C(=O)NSC2=C1 DMSMPAJRVJJAGA-UHFFFAOYSA-N 0.000 description 2
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical class 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 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 229940079919 digestives enzyme preparation Drugs 0.000 description 2
- 238000005538 encapsulation Methods 0.000 description 2
- 239000004744 fabric Substances 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 150000002191 fatty alcohols Chemical class 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000007908 nanoemulsion Substances 0.000 description 2
- 239000002736 nonionic surfactant Substances 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- XFRVVPUIAFSTFO-UHFFFAOYSA-N 1-Tridecanol Chemical compound CCCCCCCCCCCCCO XFRVVPUIAFSTFO-UHFFFAOYSA-N 0.000 description 1
- SMZOUWXMTYCWNB-UHFFFAOYSA-N 2-(2-methoxy-5-methylphenyl)ethanamine Chemical compound COC1=CC=C(C)C=C1CCN SMZOUWXMTYCWNB-UHFFFAOYSA-N 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N 2-Propenoic acid Natural products OC(=O)C=C NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- PUSPAPGHKSLKKH-UHFFFAOYSA-N 2-methyl-1,2-thiazolidin-3-one Chemical compound CN1SCCC1=O PUSPAPGHKSLKKH-UHFFFAOYSA-N 0.000 description 1
- QJRVOJKLQNSNDB-UHFFFAOYSA-N 4-dodecan-3-ylbenzenesulfonic acid Chemical compound CCCCCCCCCC(CC)C1=CC=C(S(O)(=O)=O)C=C1 QJRVOJKLQNSNDB-UHFFFAOYSA-N 0.000 description 1
- SEKMAUCMRCHQMC-UHFFFAOYSA-N 5-chloro-2-methyl-1,2-thiazolidin-3-one Chemical compound CN1SC(Cl)CC1=O SEKMAUCMRCHQMC-UHFFFAOYSA-N 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 229920001340 Microbial cellulose Polymers 0.000 description 1
- 229920006243 acrylic copolymer Polymers 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 125000002947 alkylene group Chemical group 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 229910021538 borax Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- DHNRXBZYEKSXIM-UHFFFAOYSA-N chloromethylisothiazolinone Chemical compound CN1SC(Cl)=CC1=O DHNRXBZYEKSXIM-UHFFFAOYSA-N 0.000 description 1
- 238000005202 decontamination Methods 0.000 description 1
- 230000003588 decontaminative effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 102000035118 modified proteins Human genes 0.000 description 1
- 108091005573 modified proteins Proteins 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 239000002077 nanosphere Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 235000010339 sodium tetraborate Nutrition 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 description 1
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
- C11D3/38672—Granulated or coated enzymes
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
- B01J13/02—Making microcapsules or microballoons
- B01J13/04—Making microcapsules or microballoons by physical processes, e.g. drying, spraying
- B01J13/046—Making microcapsules or microballoons by physical processes, e.g. drying, spraying combined with gelification or coagulation
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Dispersion Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The invention belongs to the technical field of daily chemical products, and discloses a biological enzyme capsule and a preparation method thereof. The biological enzyme capsule is a core-shell structure hydrogel capsule, the wall material of the hydrogel capsule comprises gel materials and water-soluble film-forming materials, and the capsule core material comprises a biological enzyme preparation and polyhydric alcohol. The preparation method comprises the following steps: fully dissolving the capsule wall material in water at 70-80 ℃, and uniformly mixing the biological enzyme of the capsule core material and the polyalcohol; preparing hydrogel capsules by using a dripping method, wherein a uniformly stirred capsule wall material solution flows out of a dripper, a capsule core material flows out of the dripper to form a sandwiched liquid column, then the liquid column is cut off by a cutter to form a series of liquid drops with a certain diameter, a calcium chloride aqueous solution is dripped into the liquid drops to be solidified into hydrogel, and the hydrogel capsules wrapping biological enzymes are obtained after filtration and dehydration. According to the invention, biological enzyme is embedded in the capsule core, so that good enzyme activity stability can be maintained.
Description
Technical Field
The invention belongs to the technical field of daily chemical products, and particularly relates to a biological enzyme capsule and a preparation method thereof.
Background
The biological enzyme is a high-activity biological catalyst, has high catalytic efficiency and strong specificity. Such as protease, which can rapidly decompose protein dirt; lipase, which can rapidly remove greasy dirt; amylase, which can remove starch dirt; the cellulase can remove the small hair bulbs of the fabric and smoothen clothes. Due to its highly effective decontamination, many enzyme preparations are widely used in washing products such as washing powders, laundry soaps, and laundry detergents.
In recent years, with the increasing sales of laundry detergents, the problem of enzyme activity stability in the laundry detergents is a difficult problem for engineers to research and improve. Because the laundry detergent is a water phase system, the biological enzyme is protein, except part of the biological enzyme can be subjected to self digestion in the water phase, and the stability of the biological enzyme is also influenced by factors such as a surfactant, a pH value and the like in the laundry detergent.
At present, the enzyme activity stability of biological enzymes in laundry detergents is mainly protected by four ways, one way is to modify the biological enzymes, for example, the CN201810286656.2 patent discloses a starch-based dextrin modified casein polypeptide conjugate, a preparation method and an application thereof, wherein the preparation method is to perform covalent grafting reaction on casein polypeptide and starch-based dextrin, and an oil-in-water type starch-based dextrin modified protein polypeptide nano emulsion is obtained by adopting a high-pressure homogenization technology. The nano emulsion has better antioxidant activity, antibacterial property and the like. The second method is to wrap the silk nano-beads with enzyme, for example, the patent CN201710046253.6 discloses a method for preparing enzyme-wrapped silk nano-beads, which first prepares a silk solution, and then wraps the enzyme into the silk to form the enzyme-wrapped silk nano-beads. The silk nano-spheres prepared by the method can effectively protect the activity of the encapsulated enzyme, realize the series reaction of multiple enzymes and have good biocompatibility. The two ways of protecting the biological enzyme have complex preparation methods and higher cost. The third mode is to achieve the effect of stabilizing the enzyme by adding an enzyme stabilizer, for example, CN201110005054.3 discloses a laundry detergent and a preparation method thereof, the stability of the enzyme activity of a laundry detergent system is improved by adding propylene glycol, sodium borate, calcium chloride and the like, and the stability of the enzyme can be improved to a certain extent by the mode, but because the type of a surfactant has a large influence on the stability of the enzyme, when the contents of sulfonic acid and fatty acid in the laundry detergent system are high, the enzyme activity cannot be stabilized by adding a stabilizer, so that the mode of adding the enzyme stabilizer has no universality. The fourth way is by polymer encapsulation, for example, CN 108949372A discloses a way of encapsulating biological enzyme with pH sensitive polymer, where the polymer expands in the range of pH 7-7.5 to release the encapsulated enzyme, and the polymer contracts in the range of pH 8-10 to immobilize the enzyme in the polymer segment, but many of the currently claimed mild laundry detergents have pH around 7, and this encapsulation is not suitable.
Disclosure of Invention
Aiming at the defects and shortcomings of the prior art, the invention mainly aims to provide a biological enzyme capsule. The biological enzyme capsule can solve the problem that the enzyme activity of the existing laundry detergent enzyme preparation is reduced due to the influence of factors such as moisture, pH value, surfactant and the like in the laundry detergent.
Another object of the present invention is to provide a method for preparing the above-mentioned bio-enzyme capsule.
The purpose of the invention is realized by the following technical scheme:
a biological enzyme capsule is a core-shell structure hydrogel capsule, wherein the capsule wall material of the hydrogel capsule comprises a gel material and a water-soluble film-forming material, and the capsule core material is a biological enzyme preparation and polyhydric alcohol.
Further, the gel material is at least one of acacia, aloe gel, hyaluronic acid, sodium alginate, agar, dextran and cyclodextrin.
Further, the water-soluble film forming material is at least one of carboxymethyl cellulose, methyl cellulose, chitosan, hydroxypropyl methyl cellulose, ethyl cellulose, carboxypropyl cellulose, polyvinyl alcohol and polyvinylpyrrolidone.
Further preferably, the gel material is agar and sodium alginate, and the water-soluble film-forming material is polyvinyl alcohol, wherein the weight ratio of the agar, the sodium alginate and the polyvinyl alcohol in the capsule wall is (10-20): (45-60): (15-25). The hydrogel with a triple interpenetrating network structure is constructed by agar, sodium alginate and polyvinyl alcohol in a proper proportion, has proper mechanical strength, and has small volume change under the physical and chemical stimulation conditions of different temperatures, pH values, ionic strengths, solvent components and the like, thereby effectively protecting the stability of the capsule core material.
Further, the biological enzyme preparation is any one of protease, amylase, lipase, cellulase, lysozyme, pectinase and mannanase; the polyalcohol is at least one of glycerol, propylene glycol, sorbitol, maltitol and mannitol, and is preferably propylene glycol.
Further preferably, the mass ratio of the biological enzyme preparation to the polyhydric alcohol is 3 to 1, the biological enzyme preparation can be more stable in the presence of the polyhydric alcohol, and the hydrogel capsule can be fuller and is not easy to shrink.
Further preferably, the mass fraction of the biological enzyme preparation in the biological enzyme hydrogel capsule is 15-25%, and the crushing pressure of the hydrogel capsule is 0.5-1.0N.
Furthermore, the hydrogel capsule is in a shape of a bead, and the diameter of the hydrogel capsule is 1-10 mm.
The preparation method of the biological enzyme capsule comprises the following steps:
fully dissolving the capsule wall material in water at 70-80 ℃ to ensure that the concentration of the capsule wall material is 15-20 wt%, then cooling to 30-40 ℃, and uniformly mixing the core material biological enzyme and the polyhydric alcohol; preparing hydrogel capsules by a dripping method, wherein uniformly stirred capsule wall material solution flows out of a dripper, capsule core material flows out of the dripper to form a sandwiched liquid column, then the liquid column is cut off by a cutter to form a series of liquid drops with certain diameters, calcium chloride aqueous solution is dripped into the liquid drops to be solidified into hydrogel, and the hydrogel capsules wrapping biological enzymes are obtained after filtration and dehydration. If a plurality of biological enzyme capsules need to be prepared, the various biological enzymes are wrapped one by one according to the steps.
Further, the concentration of the calcium chloride aqueous solution is 1-2 wt%.
Compared with the prior art, the invention has the beneficial effects that:
according to the invention, the biological enzyme is embedded in the capsule core, so that the biological enzyme is prevented from being interfered by factors such as moisture, pH value, surfactant and the like in the laundry detergent, and even if various types of biological enzyme capsules are added into the laundry detergent, various types of biological enzyme can still keep good enzyme activity stability; when the laundry detergent is used, the bio-enzyme capsule is easily broken under the action of the suction force of the pump head, and the bio-enzyme in the capsule core can be effectively released, so that the fabric washing effect is enhanced.
Detailed Description
The present invention will be described in further detail with reference to examples, but the embodiments of the present invention are not limited thereto.
In the following examples, the following abbreviations will be used and have the indicated functions.
And (3) LAS: C10-C13 linear alkyl benzene sulfonic acid and anionic surfactant.
AES: ethoxylated fatty alcohol sulfate, fatty alcohol with C12-C14 carbon number and average ethoxylation degree of 2, and anionic surfactant.
AEO9: ethoxylated fatty alcohol, average degree of ethoxylation 9, nonionic surfactant.
TO 5: ethoxylated isomeric tridecanol, average degree of ethoxylation 5, nonionic surfactant.
Acrylic copolymer: the monomer composition comprises: (a) acrylic acid; (b) An aminoalkyl methacrylate selected from the following structures:
wherein R1 is a C3-C5 linear alkylene group, and R2 and R3 are C1-C2 alkyl groups.
The BIT:1, 2-benzisothiazolin-3-one and preservative.
MIT: 2-methylisothiazoline-3-one and a preservative.
CMIT: 5-chloro-2-methylisothiazoline-3-one and a preservative.
Example 1
(1) Dissolving 10g of agar, 45g of sodium alginate and 15g of polyvinyl alcohol in 400g of water at 70 ℃ to form a capsule wall solution, and cooling to 40 ℃ for later use.
(2) Uniformly mixing 100g of protease solution and 34g of propylene glycol for later use;
(3) Preparing a hydrogel capsule by using a dripping method, enabling a capsule wall material solution to flow out of a dripping head, enabling a capsule core material to flow out of the dripping head to form a sandwiched liquid column, cutting off the liquid column by using a cutter to form a series of liquid drops with the diameter of 5-6mm, dripping the liquid drops into a calcium chloride aqueous solution (with the concentration of 1.0 wt%) to be solidified into hydrogel, and filtering to remove water to obtain the protease capsule 1.
The amylase capsule 1, the fatty acid capsule 1 and the cellulase capsule 1 are respectively prepared under the conditions.
Example 2
(1) Dissolving 20g of agar, 60g of sodium alginate and 15g of polyvinyl alcohol in 400g of water at 70 ℃ to form a capsule wall solution, and cooling to 40 ℃ for later use.
(2) Uniformly mixing 150g of amylase solution and 38g of propylene glycol for later use;
(3) Preparing a hydrogel capsule by using a dripping method, wherein a capsule wall material solution flows out of a dripping head, a capsule core material flows out of the dripping head to form a sandwiched liquid column, then the liquid column is cut off by a cutter to form a series of liquid drops with the diameter of 5-6mm, the liquid drops are dripped into a calcium chloride aqueous solution (with the concentration of 1.0 wt%) to be solidified into hydrogel, and the amylase capsule 2 is obtained after filtering and dewatering.
The protease capsule 2, the lipase capsule 2 and the cellulase capsule 2 were prepared under the above conditions, respectively.
Example 3
(1) Dissolving 20g of agar, 45g of sodium alginate and 25g of polyvinyl alcohol in 400g of water at 80 ℃ to form a capsule wall solution, and cooling to 35 ℃ for later use.
(2) 160g of lipase solution and 32g of propylene glycol are uniformly mixed for later use;
(3) Preparing a hydrogel capsule by using a dripping method, wherein a capsule wall material solution flows out of a dripping head, a capsule core material flows out of the dripping head to form a sandwiched liquid column, then the liquid column is cut off by a cutter to form a series of liquid drops with the diameter of 8-9mm, the liquid drops are dripped into a calcium chloride aqueous solution (with the concentration of 1.0 wt%) to be solidified into hydrogel, and the lipase capsule 3 is obtained after filtering and dewatering.
The protease capsule 3, the amylase capsule 3 and the cellulase capsule 3 are respectively prepared under the conditions.
Example 4
(1) Dissolving 15g of agar, 50g of sodium alginate and 20g of polyvinyl alcohol in 400g of water at 80 ℃ to form a capsule wall solution, and cooling to 35 ℃ for later use.
(2) Uniformly mixing 150g of cellulase solution and 30g of propylene glycol for later use;
(3) Preparing a hydrogel capsule by using a dripping method, enabling a capsule wall material solution to flow out of a dripping head, enabling a capsule core material to flow out of the dripping head to form a sandwiched liquid column, cutting off the liquid column by using a cutter to form a series of liquid drops with the diameter of 5-6mm, dripping the liquid drops into a calcium chloride aqueous solution (with the concentration of 1.0 wt%) to be solidified into hydrogel, and filtering to remove water to obtain the cellulase capsule 4.
The protease capsule 4, the amylase capsule 4 and the lipase capsule 4 are respectively prepared under the conditions.
Example 5
(1) Dissolving 15g of agar, 60g of sodium alginate and 20g of polyvinyl alcohol in 500g of water at 75 ℃ to form a capsule wall solution, and cooling to 30 ℃ for later use.
(2) Uniformly mixing 120g of pectinase solution and 30g of propylene glycol for later use;
(3) Preparing a hydrogel capsule by using a dripping method, wherein a capsule wall material solution flows out of a dripper, a capsule core material flows out of the dripper to form a sandwiched liquid column, the liquid column is cut off by a cutter to form a series of liquid drops with the diameter of 3-4mm, the liquid drops are dripped into a calcium chloride aqueous solution (the concentration is 1.0 wt%) to be solidified into hydrogel, and the pectinase capsule 1 is obtained after filtration and dehydration.
The protease capsule 5 and the cellulase capsule 5 were prepared under the above conditions, respectively.
Example 6
(1) Dissolving 10g of agar, 50g of sodium alginate and 25g of carboxymethyl cellulose in 400g of water at 75 ℃ to form a capsule wall solution, and cooling to 30 ℃ for later use.
(2) Uniformly mixing 100g of mannase solution and 34g of propylene glycol for later use;
(3) Preparing a hydrogel capsule by using a dropping method, wherein a capsule wall material solution flows out of a dropping head, a capsule core material flows out of the interior of the dropping head to form a sandwiched liquid column, then a cutter is used for cutting off the liquid column to form a series of liquid drops with the diameter of 3-4mm, the liquid drops are dropped into a calcium chloride aqueous solution (with the concentration of 1.0 wt%) to be solidified into hydrogel, and the mannase capsule 1 is obtained after filtration and dehydration.
Comparative example 1
This comparative example is a method of making a biocellulose-coated enzyme granulate, comprising the steps of:
mechanically compressing and dehydrating the biological cellulose gel film obtained by fermentation to about 25% of water content, preparing protease into 4wt% of enzyme solution, soaking the dehydrated biological cellulose gel film in the enzyme solution for 48 hours, taking out the biological cellulose gel film, and dehydrating to about 70% of water content. Cutting the biological cellulose gel film into 1mm 3 The biological cellulose coated protease particle 1 is obtained.
Preparing lipase granule 1, cellulase granule 1, amylase granule 1, pectinase granule 1 and mannanase granule 1 under the above conditions.
The enzyme capsules and enzyme granules obtained in the above examples and comparative examples are applied in laundry detergent:
adding protease capsules 1-5, amylase capsules 1-4, lipase capsules 1-4, cellulase capsules 1-5, pectinase capsules 1, mannanase capsules 1 corresponding to examples 1-6 and various enzyme granules and liquid enzyme preparations added with enzyme activity stabilizers in comparative example 1 into different laundry detergent systems to prepare enzyme-added laundry detergents for performance investigation and test, wherein the compositions of the enzyme-added laundry detergents are shown in table 1.
TABLE 1 compositions of ingredients of examples 7-14, comparative examples 2-5 enzyme-added laundry detergents
And (3) testing the enzyme activity stability of the laundry detergent, wherein the test method comprises the following steps: samples of examples 7-14 and comparative examples 2-5 were added with the enzyme laundry detergent and placed at (37 + -1) deg.C for 4 weeks and 8 weeks; returning to room temperature (25 +/-5) deg.C, and detecting enzyme activity retention rate according to the method specified in determination method of biological enzyme activity in detergent (detection standard of Chaibao). The results are shown in tables 2 and 3 below.
TABLE 2 enzyme activity retention rates of 4 weeks for examples 7-14 and comparative examples 2-5 enzyme-added laundry detergent samples
TABLE 3 enzyme activity retentions at 8 weeks for examples 7-14 and comparative examples 2-5 of enzyme-added laundry detergent samples
As can be seen from tables 2 and 3, in comparative examples 2 to 5, when the liquid enzyme preparation is added with the enzyme particles coated with the biological cellulose or the enzyme activity stabilizer, the activity of each enzyme is reduced rapidly after the laundry detergent sample is placed at 37 ℃ for 4 weeks and 8 weeks, while the coated type biological enzyme capsules of examples 7 to 14 have relatively stable and slow activity of the enzyme under the same test conditions, and the activity of each enzyme in the test time of 4 weeks and 8 weeks is obviously better than that of the comparative examples in the same period.
The above embodiments are preferred embodiments of the present invention, but the present invention is not limited to the above embodiments, and any other changes, modifications, substitutions, combinations, and simplifications which do not depart from the spirit and principle of the present invention should be construed as equivalents thereof, and all such changes, modifications, substitutions, combinations, and simplifications are intended to be included in the scope of the present invention.
Claims (9)
1. The biological enzyme capsule is characterized in that the biological enzyme capsule is a core-shell structure hydrogel capsule, the wall material of the hydrogel capsule comprises a gel material and a water-soluble film-forming material, and the core material is a biological enzyme preparation and polyhydric alcohol.
2. The bio-enzyme capsule according to claim 1, wherein the gel material is at least one of acacia, aloe gel, hyaluronic acid, sodium alginate, agar, dextran, and cyclodextrin.
3. The bioenzyme capsule according to claim 1, wherein the water-soluble film-forming material is at least one of carboxymethyl cellulose, methyl cellulose, chitosan, hydroxypropyl methyl cellulose, ethyl cellulose, carboxypropyl cellulose, polyvinyl alcohol and polyvinylpyrrolidone.
4. The biological enzyme capsule according to claim 2 or 3, wherein the gel material is agar and sodium alginate, and the water-soluble film-forming material is polyvinyl alcohol, wherein the weight ratio of the agar, the sodium alginate and the polyvinyl alcohol in the capsule wall is (10-20) to (45-60) to (15-25).
5. The bioenzyme capsule according to claim 1, wherein the bioenzyme preparation is any one of protease, amylase, lipase, cellulase, lysozyme, pectinase and mannanase; the polyalcohol is at least one of glycerol, propylene glycol, sorbitol, maltitol and mannitol, and is preferably propylene glycol.
6. The bioenzyme capsule according to claim 5, wherein the mass ratio of the bioenzyme preparation to the polyol is 3; the mass fraction of the biological enzyme preparation in the biological enzyme hydrogel capsule is 15-25%, and the crushing pressure of the hydrogel capsule is 0.5-1.0N.
7. The bioenzyme capsule according to claim 1, wherein the hydrogel capsule is in the shape of a bead with a diameter of 1 to 10mm.
8. The method for preparing a bio-enzyme capsule according to any one of claims 1 to 7, comprising the steps of:
fully dissolving the capsule wall material in water at 70-80 ℃ to ensure that the concentration of the capsule wall material is 15-20 wt%, then cooling to 30-40 ℃, and uniformly mixing the core material biological enzyme and the polyhydric alcohol; preparing hydrogel capsules by a dripping method, wherein uniformly stirred capsule wall material solution flows out of a dripper, capsule core material flows out of the dripper to form a sandwiched liquid column, then the liquid column is cut off by a cutter to form a series of liquid drops with certain diameters, calcium chloride aqueous solution is dripped into the liquid drops to be solidified into hydrogel, and the hydrogel capsules wrapping biological enzymes are obtained after filtration and dehydration.
9. The method for preparing a bio-enzyme capsule according to claim 8, wherein the concentration of the calcium chloride aqueous solution is 1 to 2wt%.
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN115992120A (en) * | 2023-02-13 | 2023-04-21 | 中山市南方新元食品生物工程有限公司 | Enzyme preparation special for caramel treats and preparation method thereof |
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