WO2005097984A1 - リパーゼ粉末、その製造方法及びその使用 - Google Patents
リパーゼ粉末、その製造方法及びその使用 Download PDFInfo
- Publication number
- WO2005097984A1 WO2005097984A1 PCT/JP2005/006908 JP2005006908W WO2005097984A1 WO 2005097984 A1 WO2005097984 A1 WO 2005097984A1 JP 2005006908 W JP2005006908 W JP 2005006908W WO 2005097984 A1 WO2005097984 A1 WO 2005097984A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- lipase
- milk
- powder
- aqueous solution
- animal milk
- Prior art date
Links
- 108090001060 Lipase Proteins 0.000 title claims abstract description 263
- 102000004882 Lipase Human genes 0.000 title claims abstract description 261
- 239000004367 Lipase Substances 0.000 title claims abstract description 261
- 235000019421 lipase Nutrition 0.000 title claims abstract description 261
- 239000000843 powder Substances 0.000 title claims abstract description 106
- 238000000034 method Methods 0.000 title claims abstract description 24
- 239000007864 aqueous solution Substances 0.000 claims abstract description 50
- 239000007787 solid Substances 0.000 claims abstract description 45
- 235000020244 animal milk Nutrition 0.000 claims abstract description 32
- 239000006071 cream Substances 0.000 claims abstract description 17
- 239000000203 mixture Substances 0.000 claims abstract description 17
- 238000001694 spray drying Methods 0.000 claims abstract description 10
- 238000004108 freeze drying Methods 0.000 claims abstract description 9
- 235000013336 milk Nutrition 0.000 claims description 54
- 239000008267 milk Substances 0.000 claims description 54
- 210000004080 milk Anatomy 0.000 claims description 54
- 239000000243 solution Substances 0.000 claims description 34
- 238000005809 transesterification reaction Methods 0.000 claims description 22
- 239000003921 oil Substances 0.000 claims description 19
- 239000002245 particle Substances 0.000 claims description 19
- 239000003925 fat Substances 0.000 claims description 17
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 17
- 238000004519 manufacturing process Methods 0.000 claims description 11
- 241000235403 Rhizomucor miehei Species 0.000 claims description 4
- 241000223257 Thermomyces Species 0.000 claims description 4
- 238000005886 esterification reaction Methods 0.000 claims description 4
- 241000588986 Alcaligenes Species 0.000 claims description 3
- 241000235402 Rhizomucor Species 0.000 claims description 3
- 241000235527 Rhizopus Species 0.000 claims description 3
- 230000032050 esterification Effects 0.000 claims description 2
- 235000019626 lipase activity Nutrition 0.000 abstract description 14
- 239000002904 solvent Substances 0.000 abstract description 5
- 238000001556 precipitation Methods 0.000 abstract description 4
- 230000000052 comparative effect Effects 0.000 description 27
- 239000012141 concentrate Substances 0.000 description 24
- 239000007921 spray Substances 0.000 description 24
- 230000000694 effects Effects 0.000 description 19
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 18
- 235000019198 oils Nutrition 0.000 description 15
- 235000019197 fats Nutrition 0.000 description 14
- 238000006243 chemical reaction Methods 0.000 description 13
- 239000008363 phosphate buffer Substances 0.000 description 12
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 11
- 239000012528 membrane Substances 0.000 description 11
- 239000007788 liquid Substances 0.000 description 9
- 238000001035 drying Methods 0.000 description 8
- 235000014113 dietary fatty acids Nutrition 0.000 description 6
- 239000000194 fatty acid Substances 0.000 description 6
- 229930195729 fatty acid Natural products 0.000 description 6
- 239000002244 precipitate Substances 0.000 description 6
- VLPFTAMPNXLGLX-UHFFFAOYSA-N trioctanoin Chemical compound CCCCCCCC(=O)OCC(OC(=O)CCCCCCC)COC(=O)CCCCCCC VLPFTAMPNXLGLX-UHFFFAOYSA-N 0.000 description 6
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 239000000306 component Substances 0.000 description 5
- 150000004665 fatty acids Chemical class 0.000 description 5
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 5
- 229940093609 tricaprylin Drugs 0.000 description 5
- 241000588810 Alcaligenes sp. Species 0.000 description 4
- 108010048733 Lipozyme Proteins 0.000 description 4
- 235000019484 Rapeseed oil Nutrition 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 150000002148 esters Chemical class 0.000 description 4
- -1 etc. Substances 0.000 description 4
- FCCDDURTIIUXBY-UHFFFAOYSA-N lipoamide Chemical compound NC(=O)CCCCC1CCSS1 FCCDDURTIIUXBY-UHFFFAOYSA-N 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 239000002994 raw material Substances 0.000 description 4
- 238000005507 spraying Methods 0.000 description 4
- 238000003756 stirring Methods 0.000 description 4
- PHYFQTYBJUILEZ-IUPFWZBJSA-N triolein Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OCC(OC(=O)CCCCCCC\C=C/CCCCCCCC)COC(=O)CCCCCCC\C=C/CCCCCCCC PHYFQTYBJUILEZ-IUPFWZBJSA-N 0.000 description 4
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 240000005384 Rhizopus oryzae Species 0.000 description 3
- 235000013752 Rhizopus oryzae Nutrition 0.000 description 3
- UYXTWWCETRIEDR-UHFFFAOYSA-N Tributyrin Chemical compound CCCC(=O)OCC(OC(=O)CCC)COC(=O)CCC UYXTWWCETRIEDR-UHFFFAOYSA-N 0.000 description 3
- BAECOWNUKCLBPZ-HIUWNOOHSA-N Triolein Natural products O([C@H](OCC(=O)CCCCCCC/C=C\CCCCCCCC)COC(=O)CCCCCCC/C=C\CCCCCCCC)C(=O)CCCCCCC/C=C\CCCCCCCC BAECOWNUKCLBPZ-HIUWNOOHSA-N 0.000 description 3
- PHYFQTYBJUILEZ-UHFFFAOYSA-N Trioleoylglycerol Natural products CCCCCCCCC=CCCCCCCCC(=O)OCC(OC(=O)CCCCCCCC=CCCCCCCCC)COC(=O)CCCCCCCC=CCCCCCCCC PHYFQTYBJUILEZ-UHFFFAOYSA-N 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000012869 ethanol precipitation Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 238000005374 membrane filtration Methods 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 235000000346 sugar Nutrition 0.000 description 3
- URAYPUMNDPQOKB-UHFFFAOYSA-N triacetin Chemical compound CC(=O)OCC(OC(C)=O)COC(C)=O URAYPUMNDPQOKB-UHFFFAOYSA-N 0.000 description 3
- 229940117972 triolein Drugs 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- 241001558145 Mucor sp. Species 0.000 description 2
- 239000001888 Peptone Substances 0.000 description 2
- 108010080698 Peptones Proteins 0.000 description 2
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 239000003054 catalyst Substances 0.000 description 2
- 235000005822 corn Nutrition 0.000 description 2
- 235000013312 flour Nutrition 0.000 description 2
- 238000004817 gas chromatography Methods 0.000 description 2
- 235000013773 glyceryl triacetate Nutrition 0.000 description 2
- 238000000227 grinding Methods 0.000 description 2
- 235000014593 oils and fats Nutrition 0.000 description 2
- 238000010979 pH adjustment Methods 0.000 description 2
- 235000019319 peptone Nutrition 0.000 description 2
- 239000011574 phosphorus Substances 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 229960002622 triacetin Drugs 0.000 description 2
- 235000015112 vegetable and seed oil Nutrition 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- LDVVTQMJQSCDMK-UHFFFAOYSA-N 1,3-dihydroxypropan-2-yl formate Chemical compound OCC(CO)OC=O LDVVTQMJQSCDMK-UHFFFAOYSA-N 0.000 description 1
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 1
- MGGVALXERJRIRO-UHFFFAOYSA-N 4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]-2-[2-oxo-2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethyl]-1H-pyrazol-5-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C=1C(=NN(C=1)CC(=O)N1CC2=C(CC1)NN=N2)O MGGVALXERJRIRO-UHFFFAOYSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- 241000186361 Actinobacteria <class> Species 0.000 description 1
- 241000186073 Arthrobacter sp. Species 0.000 description 1
- 241000228257 Aspergillus sp. Species 0.000 description 1
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 241000193464 Clostridium sp. Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 241000603729 Geotrichum sp. Species 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- 241000186610 Lactobacillus sp. Species 0.000 description 1
- 108010013563 Lipoprotein Lipase Proteins 0.000 description 1
- 102100022119 Lipoprotein lipase Human genes 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 244000187664 Nerium oleander Species 0.000 description 1
- 241000187681 Nocardia sp. Species 0.000 description 1
- 102100033357 Pancreatic lipase-related protein 2 Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 241000235400 Phycomyces Species 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000592823 Puccinia sp. Species 0.000 description 1
- 241000952054 Rhizopus sp. Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241001360381 Saccharomycopsis sp. Species 0.000 description 1
- 235000019485 Safflower oil Nutrition 0.000 description 1
- 241001147693 Staphylococcus sp. Species 0.000 description 1
- 229930182558 Sterol Natural products 0.000 description 1
- 241000187180 Streptomyces sp. Species 0.000 description 1
- 241001285933 Thermomyces sp. Species 0.000 description 1
- 241001148118 Xanthomonas sp. Species 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 238000006136 alcoholysis reaction Methods 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 150000008044 alkali metal hydroxides Chemical class 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- OEERIBPGRSLGEK-UHFFFAOYSA-N carbon dioxide;methanol Chemical compound OC.O=C=O OEERIBPGRSLGEK-UHFFFAOYSA-N 0.000 description 1
- 150000001733 carboxylic acid esters Chemical class 0.000 description 1
- 150000001735 carboxylic acids Chemical class 0.000 description 1
- 239000012159 carrier gas Substances 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 229920001429 chelating resin Polymers 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 235000005687 corn oil Nutrition 0.000 description 1
- 239000002285 corn oil Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- DJLUGWFUVRDHLO-UHFFFAOYSA-N ethyl 4,5-dimethyl-6-oxo-7-propyl-7,8-dihydrocyclopenta[e][1]benzofuran-2-carboxylate Chemical class O=C1C(CCC)CC2=C1C(C)=C(C)C1=C2C=C(C(=O)OCC)O1 DJLUGWFUVRDHLO-UHFFFAOYSA-N 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 239000001087 glyceryl triacetate Substances 0.000 description 1
- 235000020251 goat milk Nutrition 0.000 description 1
- 239000001307 helium Substances 0.000 description 1
- 229910052734 helium Inorganic materials 0.000 description 1
- SWQJXJOGLNCZEY-UHFFFAOYSA-N helium atom Chemical compound [He] SWQJXJOGLNCZEY-UHFFFAOYSA-N 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 239000012051 hydrophobic carrier Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- ZUBZATZOEPUUQF-UHFFFAOYSA-N isopropylhexane Natural products CCCCCCC(C)C ZUBZATZOEPUUQF-UHFFFAOYSA-N 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000012533 medium component Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000012046 mixed solvent Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000004570 mortar (masonry) Substances 0.000 description 1
- 229930014626 natural product Natural products 0.000 description 1
- 229940049964 oleate Drugs 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 229920002492 poly(sulfone) Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 235000005713 safflower oil Nutrition 0.000 description 1
- 239000003813 safflower oil Substances 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 239000008159 sesame oil Substances 0.000 description 1
- 235000011803 sesame oil Nutrition 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 239000003549 soybean oil Substances 0.000 description 1
- 235000012424 soybean oil Nutrition 0.000 description 1
- 238000013112 stability test Methods 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- 235000003702 sterols Nutrition 0.000 description 1
- 150000005846 sugar alcohols Polymers 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- 235000019871 vegetable fat Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/64—Fats; Fatty oils; Ester-type waxes; Higher fatty acids, i.e. having at least seven carbon atoms in an unbroken chain bound to a carboxyl group; Oxidised oils or fats
- C12P7/6436—Fatty acid esters
- C12P7/6445—Glycerides
- C12P7/6458—Glycerides by transesterification, e.g. interesterification, ester interchange, alcoholysis or acidolysis
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/64—Fats; Fatty oils; Ester-type waxes; Higher fatty acids, i.e. having at least seven carbon atoms in an unbroken chain bound to a carboxyl group; Oxidised oils or fats
- C12P7/6436—Fatty acid esters
- C12P7/6445—Glycerides
- C12P7/6454—Glycerides by esterification
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
- C12N9/20—Triglyceride splitting, e.g. by means of lipase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/98—Preparation of granular or free-flowing enzyme compositions
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P7/00—Preparation of oxygen-containing organic compounds
- C12P7/64—Fats; Fatty oils; Ester-type waxes; Higher fatty acids, i.e. having at least seven carbon atoms in an unbroken chain bound to a carboxyl group; Oxidised oils or fats
Definitions
- the present invention relates to a lipase powder that can be suitably used for various esterification reactions, transesterification reactions, and the like, a method for producing the same, a lipase composition in which the lipase powder is immersed or infiltrated in fats and oils, and a lipase powder.
- the present invention relates to a method for transesterification of fats and oils using the same.
- Lipases are widely used in esterification reactions between various carboxylic acids such as fatty acids and alcohols such as monoalcohols and polyhydric alcohols, and transesterification reactions between a plurality of carboxylic acid esters. Of these, transesterification is an important technology for the production of esters, sugar esters and steroids of various fatty acids, including the modification of animal and vegetable fats and oils. If lipase, which is a fat and oil hydrolase, is used as a catalyst for these reactions, transesterification can be carried out under mild conditions at room temperature to about 70 ° C. The lipase as a catalyst is a natural product, and its safety is also high. In addition, the target product can be efficiently produced due to its substrate specificity and positional specificity.
- lipase has conventionally been used as a carrier such as an anion exchange resin (Patent Document 1), a phenol-adsorbed resin (Patent Document 2), a hydrophobic carrier (Patent Document 3), and a cation exchange resin (Patent Document 1). 4), immobilized on chelating resins (Patent Document 5) and the like, and used for esterification and ester exchange reactions.
- a carrier such as an anion exchange resin (Patent Document 1), a phenol-adsorbed resin (Patent Document 2), a hydrophobic carrier (Patent Document 3), and a cation exchange resin (Patent Document 1). 4), immobilized on chelating resins (Patent Document 5) and the like, and used for esterification and ester exchange reactions.
- lipase is immobilized and used for the transesterification reaction.
- a powerful immobilized lipase is not only accompanied by loss of the original lipase activity due to the immobilization process, but also has a porous structure.
- an acidic carrier was used, the pores were clogged with raw materials and products, resulting in a decrease in the transesterification rate.
- water retained by the carrier is brought into the reaction system, so that a side reaction, for example, It was difficult to avoid the production of diglyceride / monoglyceride in the transesterification of oils and fats.
- a lipase is added to the ester-containing raw material so that 90% or more of the dispersed lipase powder particles are maintained at a particle size in the range of 1 to 100 ⁇ m during the transesterification reaction.
- a method of performing a transesterification reaction by dispersing a powder has been proposed (Patent Document 6). It has also been proposed to use an enzyme powder obtained by drying an enzyme solution containing a phospholipid and a fat-soluble vitamin (Patent Document 7).
- Patent Document 1 Japanese Patent Application Laid-Open No. Sho 60-98984
- Patent Document 2 JP-A-61-202688
- Patent document 3 JP-A-2-138986
- Patent Document 4 JP-A-3-61485
- Patent Document 5 JP-A-1-2622795
- Patent Document 6 Patent No. 2668187
- Patent Document 7 JP-A-2000-106873
- the present invention provides a method for producing a lipase, which comprises granulating lipase using the solid content of animal milk and powdering the lipase. This is based on the finding that sex and stability are further improved, and that when the lipase is a 1,3-specific lipase, the 1,3 selectivity is further improved.
- the present invention provides a lipase powder which is a granulated product containing lipase and animal milk solids.
- the present invention also provides a lipase composition wherein the lipase powder is immersed or infiltrated in fat or oil.
- the present invention also provides a method for producing a lipase powder, comprising adding animal milk or a cream derived from animal milk to a lipase-containing aqueous solution and spray-drying, freeze-drying or solvent-precipitating.
- the present invention also provides a lipase for transesterification or transesterification containing the lipase powder.
- the present invention also provides a method for transesterifying fats and oils, which comprises using a transesterification lipase.
- lipase used in the present invention examples include lipoprotein lipase, monoacyldaricellolipase, diacylglycerolipase, triacinoregglycerolipase, galactolipase, and phospholipase. Of these, triacyldaricellolipase is preferred.
- Microorganisms that produce these lipases include, but are not limited to, bacteria, yeasts, filamentous fungi, actinomycetes, etc., but include the genera Pseudomonas, Alcaligenes sp. Arthrobacter sp.), Staphylococcus sp., Tonolopsis sp.
- Chromobacterum sp. Chromobacterum sp., Xanthomonas sp., Lactobacillus sp., Clostridium, Clostridium sp., Candida sp., Geotricum (Geotrichum sp.), Saccharomycopsis sp.
- Bocchromycopsis sp. Nokanoreai— / Genus (Nocardia sp., Fusarium II, Fuzarium sp.), Aspergillus sp.), ⁇ -silium (Penicillum sp.), Muconore (Mucor sp.), Rhizopus (Rhizopus sp.), Phycomyces (Phycomycese sp.), Puccinia sp., Bacillus sp., Streptomyces sp.
- Streptmycese sp. Streptmycese sp.
- Thermomyces sp. And the like.
- 1,3-specific lipases are preferred, and in particular, 1,3-specific lipases derived from Rhizomucor and Alcaligenes are preferable. 1,3-specific lipase from Alcaligenes sp. Conventionally, Rhizomucor miehei may be treated as a genus Mucor sp.
- 1,3-specific lipases derived from the genera Rhizopus and Thermomyces are particularly preferred, and 1,3-specific lipases derived from Rhizopus oryzae and Thermomyces lanugenousu are particularly preferred. preferable.
- Animal milk used in the present invention includes milk, goat milk and the like. Among them, milk is preferred, and particularly, the solid content of animal milk is preferably milk or a solid content of milk-derived talmes.
- the ratio of lipase to animal milk can be various ratios, but it is preferable that the amount is 0.1 to 20 times the mass of lipase in the solid content of the animal milk. It is better to do so.
- the lipase powder of the present invention essentially contains lipase and animal milk solids, but may further contain lipase medium components and the like.
- Lipase powder of the present invention is preferably the water content is not more than 10 wt% instrument particularly, and even preferably at 6.5 to 8.5 mass 0/0! /,.
- the particle size of the lipase powder of the present invention can be arbitrarily set, it is preferable that 90% by mass or more of the lipase powder has a particle size of 1 to 100 ⁇ m.
- the average particle size is preferably from 20 to 80 ⁇ m, more preferably from 20 to 50 ⁇ m.
- the particle size of the lipase powder is preferably spherical.
- the particle size of the lipase powder can be measured, for example, using a particle size distribution analyzer (LA-500) manufactured by HORIBA.
- LA-500 particle size distribution analyzer manufactured by HORIBA.
- the lipase powder of the present invention is prepared by, for example, a method in which animal milk or a cream derived from animal milk is added to an aqueous solution containing lipase, spray-dried, freeze-dried or solvent-precipitated and then dried. You can get more.
- the solvent used in the solvent precipitation method include ethanol, acetone, methanol, isopropyl alcohol, and hexane, and a mixed solvent thereof can also be used. Among them, it is preferable to use ethanol or acetone in order to further enhance the activity of the lipase powder.
- it can be performed by drying under reduced pressure.
- the lipase-containing aqueous solution includes a lipase culture solution from which cells have been removed, a purified culture solution, a solution obtained by dissolving and dispersing lipase powder obtained from these in water, and a commercially available lipase powder dissolved and dispersed in water again. And a commercially available liquid lipase. Further, those from which low-molecular components such as salts are removed to further enhance lipase activity are preferable, and those from which low-molecular components such as sugar are removed to further improve powder properties are more preferable.
- Lipase cultures include, for example, soy flour, peptone, corn 'Stap' liquor, KH
- Aqueous solution containing PO, (NH) SO, MgSO containing PO, (NH) SO, MgSO.
- soy flour 0.1 to 20 wt% preferably from 1.0 to 10 wt%, peptone 0.1 to 30 mass 0/0, preferably from 0.5 to 10 weight 0/0, corn ' Suthep 'liquor from 0.1 to 30 weight 0/0, preferably rather is from 0.5 to 10 weight 0/0, ⁇ ⁇ 0. 01 ⁇ 20 mass 0/0, preferably from 0.1 to 5 mass 0/0
- soy flour 0.1 to 20 wt% preferably from 1.0 to 10 wt%, peptone 0.1 to 30 mass 0/0, preferably from 0.5 to 10 weight 0/0, corn ' Suthep 'liquor from 0.1 to 30 weight 0/0, preferably rather is from 0.5 to 10 weight 0/0, ⁇ ⁇ 0. 01 ⁇ 20 mass 0/0, preferably from 0.1 to 5 mass 0/0
- peptone 0.1 to 30 mass 0/0 preferably from 0.5 to 10 weight 0/0
- ⁇ is 0.01 to 20% by mass, preferably 0.05 to 5% by mass.
- Culture conditions are culture temperature
- Isolation of the cells is preferably performed by centrifugation, membrane filtration, or the like. Further, removal of low molecular components such as salts and sugars can be performed by UF membrane treatment. Specifically, after performing UF membrane treatment, concentrating the aqueous solution containing lipase to a volume of 1Z2, and then adding the same amount of phosphate buffer as the concentrated solution, it is repeated 1 to 5 times. A lipase-containing aqueous solution from which low molecular components have been removed can be obtained.
- the centrifugation is preferably controlled at 200 to 20,000 X g, and the membrane filtration is preferably controlled at a pressure of 3.0 kg / m 2 or less using an MF membrane, a filter press or the like.
- Homogenizer for intracellular enzymes First, it is preferable to crush the cells with a Warlinda blender, ultrasonic crushing, French press, ball mill, or the like, and remove cell residues by centrifugation, membrane filtration, or the like.
- the rotation speed of the homogenizer is 500 ⁇ 30, OOOrpm, preferably ⁇ 1,000 ⁇ 15, OOOrpm, and the rotation speed of the Worthing Blender is 500 ⁇ 10,000rpm, preferably ⁇ 1,000 ⁇ 5, OOOrpm. is there.
- the stirring time is 0.5 to 10 minutes, preferably 1 to 5 minutes.
- the ultrasonic crushing is preferably performed under the conditions of 1 to 50 KHz, preferably 10 to 20 KHz. It is better to use glass balls having a diameter of about 0.1 to 0.5 mm for the ball mill.
- aqueous solution containing 5 to 30% by mass as a solid content it is preferable to use an aqueous solution containing 5 to 30% by mass as a solid content as the lipase-containing aqueous solution.
- the amount of animal milk or cream derived from animal milk to be added is preferably 0.1 to 20 times the solid content of the aqueous solution containing lipase, preferably 0.3 to 10 times the solid content. More preferably, an amount of 0.3 to 5 times is most preferable.
- the solid content concentration in the lipase-containing aqueous solution and the solid content concentration in animal milk or animal milk-derived cream can be measured using, for example, a refractometer (BRX-242, manufactured by CIS Co., Ltd.). Brix.%.
- the pH of the lipase-containing aqueous solution After adding animal milk or animal milk-derived cream, it is preferable to adjust the pH of the lipase-containing aqueous solution to 6 to 7.5. In particular, it is preferable to adjust the pH to 7.0 or less and further to adjust the pH to a range of 6.5 to 7.0.
- the pH adjustment is preferably performed immediately before a drying step such as spray drying.However, it may be performed in any of the preceding steps, and the lipase may be adjusted in advance so that the pH immediately before the drying step is within the above range.
- the pH of the aqueous solution may be adjusted.
- an alkali metal hydroxide such as sodium hydroxide which can use various alkali agents and acids! /.
- the lipase-containing aqueous solution may be concentrated in a middle step before the drying step.
- the method of concentration is not particularly limited, but evaporator, flash evaporator, UF membrane concentration, MF membrane concentration, salting out with inorganic salts, precipitation method with a solvent, adsorption method with ion exchange cellulose, etc., water absorbing gel Water absorption method.
- UF membrane concentration and evaporator are used.
- a flat or hollow fiber membrane with a molecular weight cut-off of 3,000 to 000, preferably ⁇ 6,000 to 50,000, and a positive material Acrylic-tolyl type, polysulfone type and the like are preferable.
- Spray drying is preferably performed using a spray drier such as a nozzle countercurrent type, a disk countercurrent type, a nozzle cocurrent type, and a disk cocurrent type. It is preferable to use a disk parallel flow type, and the atomizer has a rotation speed of 4,000 to 20, OOOrpm, and calo heat at an inlet temperature of 100 to 200. C, it is preferable to spray dry by controlling the outlet temperature at 40 to 100 ° C.
- a spray drier such as a nozzle countercurrent type, a disk countercurrent type, a nozzle cocurrent type, and a disk cocurrent type. It is preferable to use a disk parallel flow type, and the atomizer has a rotation speed of 4,000 to 20, OOOrpm, and calo heat at an inlet temperature of 100 to 200. C, it is preferable to spray dry by controlling the outlet temperature at 40 to 100 ° C.
- freeze drying is also preferred.
- it is preferably performed by a lab-size freeze dryer for small amounts and a tray type freeze drying.
- it can be prepared by drying under reduced pressure.
- the lipase powder thus prepared can be used as it is. It is handled as a lipase composition immersed or infiltrated in fats and oils.
- the mass of the fat or oil in the lipase composition is preferably 0.1 to 20 times the lipase powder, more preferably 1 to 20 times.
- the lipase composition is prepared by adding fats and oils to lipase powder produced by spray drying or the like, and stirring the mixture uniformly with a stirrer three-one motor or by adding fats and oils in advance to the powder recovery part of the spray dryer. It can be easily obtained by a method of uniformly stirring after collection and removing excess fats and oils by filtration.
- oils and fats to be impregnated into the lipase powder are not particularly limited, and vegetable oils such as rapeseed oil, soybean oil, oleander oil, olive oil, safflower oil, corn oil, coconut oil, sesame oil, etc., and triolein (Glycerin trioleate), tricaprylin (glycerin trioctanoate), triacetin (glycerin triacetate), tributyrin (glycerin tributyrate), and one or more mixtures of triacylglycerols, fatty acid esters, sterol esters, and the like.
- vegetable oils such as rapeseed oil, soybean oil, oleander oil, olive oil, safflower oil, corn oil, coconut oil, sesame oil, etc.
- triolein Tricaprylin (glycerin trioctanoate), triacetin (glycerin triacetate), tributyrin (glycerin tributyrate),
- the lipase powder according to the present invention has a very high 1,3_ selectivity.
- a transesterification reaction of fats and oils, a transesterification reaction of fats and fatty acid esters, a transesterification reaction of alcoholysis acid lysis, or a transesterification reaction of glycerin and fatty acids is performed in a usual manner using the lipase powder. Can be performed efficiently.
- a lipase powder having improved lipase activity and stability is provided.
- the lipase is a 1,3-specific lipase
- its 1,3 selectivity is improved in each step, and the fatty acid residue at position 2 of the raw material triglyceride is retained in the transesterified product at a very high ratio. can do.
- a liquid lipase (trade name: Palatase20000L) derived from Rhizomucor miehei manufactured by Novozyms Japan K.K. to obtain a lipase containing aqueous solution 1 to remove molecular components (solids concentration 20.1 wt 0/0). Specifically, a liquid lipase (paratase 20000L) was treated with a UF membrane under ice-cooling, concentrated to a volume of 1Z2, and then 0.01M phosphate buffer of pH 7 was added in the same amount as the concentrated solution.
- This liquid was sprayed using a spray dryer (SD-1000: manufactured by Tokyo Rika Kikai Co., Ltd.) under the conditions of an inlet temperature of 130 ° C, a dry air volume of 0.7 to 1. lmVmin, and a spray pressure of ll to 12 kpa.
- SD-1000 manufactured by Tokyo Rika Kikai Co., Ltd.
- a spray dryer manufactured by Tokyo Rika Kikai Co., Ltd.
- a spray dryer SD-1000: manufactured by Tokyo Rika Kikai Co., Ltd.
- the shape of the lipase powder particles was spherical, and 90% by mass or more of the lipase powder was in the range of particle size 1 to L00 ⁇ m, and the average particle size was 7.6 ⁇ m.
- the particle size was measured using a particle size distribution analyzer (LA-500) manufactured by HORIBA.
- the solid content of the lipase-containing aqueous solution and the solid content of milk were determined by the following methods. Brix.% was determined using a refractometer (BRX-242 manufactured by Shi-Iss Co., Ltd.).
- Example 2 The same amount of water as the concentrated solution was added to the concentrated lipase solution obtained in Example 1 to obtain a lipase-containing aqueous solution 2 (the lipase concentrated solution: water volume ratio was 1: 1).
- a lipase powder was obtained in the same manner as in Example 1 except that the lipase-containing aqueous solution 1 of Example 1 was replaced with the lipase-containing aqueous solution 2.
- the volume ratio of lipase concentrate: water: milk is 0.5: 0.5: 1, and the solid content of milk is 1.05 times the solid content of the lipase-containing aqueous solution (UF).
- Example 1 To the lipase concentrate obtained in Example 1, the same amount of the concentrate as 0.01 M phosphate buffer at pH 7 was added, and the lipase-containing aqueous solution 3 (lipase concentrate: buffer at a volume ratio of 1: 1) was added. Obtained.
- a lipase powder was obtained in the same manner as in Example 1 except that the lipase-containing aqueous solution 1 in Example 1 was replaced with the lipase-containing aqueous solution 3.
- the volume ratio of lipase concentrate: phosphate buffer 1: milk was 0.5: 0.5: 1, and the solid content of milk was 1.03 times the mass of the solid content of the aqueous solution containing lipase. .
- Example 1 To the lipase concentrate obtained in Example 1 was added the same amount of a 0.01 M phosphate buffer having a pH of 8 as the concentrate, and an aqueous solution 4 containing lipase (lipase concentrate: buffer at a volume ratio of 1: 1) was added. Obtained. To 4, 20 ml of this lipase-containing aqueous solution, 10 ml of milk (Koiwai Milk Tasting, manufactured by Koiwai Dairy Co., Ltd .: solid content concentration: 12.9% by mass) was added. The pH of the solution thus obtained was adjusted to pH 6.8 to 6.9 using an aqueous sodium hydroxide solution. The volume ratio of lipase concentrate: phosphate buffer: milk was 0.5: 0.5: 0.5, and the solid content of milk was 0.52 times the solid content of the lipase-containing aqueous solution. Was.
- Example 1 To the lipase concentrate obtained in Example 1 was added the same amount of a 0.01 M phosphate buffer having a pH of 8 as the concentrate, and an aqueous solution 5 containing lipase (lipase concentrate: buffer at a volume ratio of 1: 1) was added. Obtained. The relative lipase-containing aqueous solution 5, 20 ml, cream (trade name: Hokkaido net positive cream 35, Takanashi Milk Products Co., Ltd., solid concentration 43 wt 0/0) was added 2 ml. in this way The pH of the resulting solution was adjusted to 6.8 to 6.9 using an aqueous sodium hydroxide solution.
- cream trade name: Hokkaido net positive cream 35, Takanashi Milk Products Co., Ltd., solid concentration 43 wt 0/0
- the volume ratio of lipase concentrate: phosphate buffer: fresh cream is 0.5: 0.5: 0.1, and the solid content of the fresh cream is 0.34 times the solid content of the lipase-containing aqueous solution. Met. Thereafter, a lipase powder was obtained in the same manner as in Example 1.
- Example 2 To the lipase concentrated solution obtained in Example 1, the same amount of the concentrated solution as 0.01 M phosphate buffer at pH 8 was added, and the lipase-containing aqueous solution 6 (lipase concentrated solution: buffer at a volume ratio of 1: 1) was added. Obtained. To 6 and 20 ml of the lipase-containing aqueous solution, 20 ml of jersey milk (Aso Oguni Jersey 4.5 milk: manufactured by Aso Agricultural Cooperative, solid content concentration 13.2% by mass) was added. The pH of the solution thus obtained was adjusted to pH 6.8 to 6.9 using an aqueous sodium hydroxide solution.
- the volume ratio of lipase concentrate: phosphate buffer: milk was 0.5: 0.5: 1, and the solid content of milk was 1.06 times the solid content of the lipase-containing aqueous solution. Thereafter, a lipase powder was obtained in the same manner as in Example 1.
- a lipase powder was obtained in the same manner as in Example 1, except that freeze drying was performed instead of spray drying as a method of powdering.
- freeze-drying a lipase-containing aqueous solution adjusted to pH 6.8 to 6.9 is placed in an eggplant-shaped flask, frozen with dry ice methanol, and then freeze-dried by Tokyo Rika Kikai Co., Ltd. (FDU-830). And freeze-dried at 0.15 Torr for 1-2 days. After drying, the mixture was lightly ground in a mortar to obtain a lipase powder.
- a lipase powder was obtained in the same manner as in Example 3 except that no milk was added.
- the volume ratio of lipase concentrated solution: phosphate buffer was 1: 1.
- the lipase activity of the lipase powder thus obtained was measured by the following method. The results are shown in Table 1.
- Reaction rate (%) ⁇ C34 area / (C24 area + C34 area) ⁇ X 100
- C24 indicates tricaprylin
- C34 indicates that one fatty acid of tricaprylin is replaced by 18, and area indicates the area of those areas.
- the reaction rate constant K was determined by analysis software (Orijin ver. 6.1) based on the reaction rate at each time.
- the lipase activity was expressed as a relative activity when the ⁇ value of Comparative Example 1 was set to 100.
- the reaction rate constant K was determined using the reaction rate force analysis software (orijin ver. 6.1) at each time. The value of the final reaction rate at this time is variable. The reactivity of the 1,3-positions when the reactivity of the 2-position was set to 1 was determined.
- Carrier gas helium
- the half-life of the lipase powder obtained in Example 1 was 913 hours, and the half-life of the lipase powder obtained in Comparative Example 1 was 234 hours.According to the lipase powder of the present invention, It can be seen that the stability is more than doubled.
- Powdered lipase manufactured by Meito Sangyo Co., Ltd. (trade name: Lipase QL, derived from Alcaligenes sp.) was suspended in water to obtain an aqueous solution containing lipase (solid content: 2.0% by mass).
- aqueous solution containing lipase solid content: 2.0% by mass
- milk Koiwai milk freshly prepared by Koiwai Dairy Co., Ltd .: solid content concentration: 12.9% by mass
- the volume ratio of the lipase-containing aqueous solution: milk was 10: 1, and the solid content of the milk was 0.65 times the mass of the solid content of the lipase-containing aqueous solution.
- the pH of the solution thus obtained was adjusted to pH 6.8 to 6.9 using an aqueous sodium hydroxide solution.
- a spray drier (SD-1000: manufactured by Tokyo Rika Kikai Co., Ltd.), spray this liquid at an outlet temperature of 130 ° C, dry air volume of 0.7 to 1.lmVmin, and spray pressure of ll to 12kpa. Spraying was performed underneath to obtain a lipase powder.
- the shape of the lipase powder particles was spherical, and 90% by mass or more of the lipase powder had a particle size of 1 to: LOO ⁇ m, and the average particle size was 35 ⁇ m.
- the particle size was measured using a particle size distribution analyzer (LA-500) manufactured by HORIBA.
- a lipase powder was obtained by spray drying in the same manner as in Example 8, except that no milk was added.
- the lipase activity of these lipase powders was measured and expressed as a relative value when the activity of the lipase powder of Comparative Example 1 was set at 100.
- Table 3 summarizes the results.
- Example 2 To the lipase powder obtained in Example 1, a 5-fold amount of rapeseed oil was added, the rapeseed oil was impregnated with the lipase powder, excess oil was removed by filtration, and the mass% of lipase powder / rapeseed oil was 55/45. A lipase composition was prepared.
- a powder (freeze-dried) lipase (Ribase D "Amano") derived from Rhizopus oryzae manufactured by Amano Enzym Co., Ltd. was re-suspended in water at a concentration of 5% by mass, and spray-dried (SD-1000: Tokyo Rika Science) Using an instrument (manufactured by Kiki Co., Ltd.), the lipase powder was obtained by spraying under the conditions of an inlet temperature of 130 ° C., an amount of dry air ⁇ a ⁇ ⁇ ! ⁇ /! ⁇ !!.
- the obtained precipitate is collected with a centrifugal separator (manufactured by Beckman: GS-6KR) 3000 rpm.10 min., And then depressurized with a dryer (manufactured by Tokyo Rikaki K.K .: FDU-830) for 16 to 20 hours. It was dried to obtain a lipase powder.
- the activities of these lipase powders were measured and expressed as relative values when the activity of the lipase powder of Comparative Example 3 was set to 100. The results are summarized in Table-4.
- SD-1000 manufactured by Tokyo Rika Kiki Co., Ltd.
- Spraying was performed under the conditions of 12 Kpa to obtain a lipase powder.
- a liquid lipase (trade name: Lipozyme Tl 100L) derived from Thermomyces lanugenousu manufactured by Novozyms Japan Co., Ltd. was spray-dried (Type SD-1000: manufactured by Tokyo Rikakikai Co., Ltd.) using an inlet temperature of 130 ° C and dry air. Spraying was performed under the conditions of an amount of 0.7 to 1.1113 / m2 and a spray pressure of 11 to 12 Kpa to obtain a lipase powder.
- Example 13 To 1 ml of the same liquid lipase (Lipozyme Tl 100 L) as in Comparative Example 5, 10 ml of milk (Meiji Delicious Milk, manufactured by Meiji Dairies Co., Ltd., solid content concentration: 12.9% by mass) was added.
- the lipase solution was spray-dried using a spray dryer (SD-1000: Tokyo Rikakiki Co., Ltd.) at an inlet temperature of 130 ° C, a dry air volume of 0.7 to l.lm3 / min., And a spray pressure of ll to 12 Kpa. It was sprayed under the conditions to obtain a lipase powder.
- SD-1000 Tokyo Rikakiki Co., Ltd.
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Fats And Perfumes (AREA)
Abstract
Description
Claims
Priority Applications (9)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
AT05728493T ATE452971T1 (de) | 2004-04-08 | 2005-04-08 | Lipasepulver, verfahren zur herstellung davon und verwendung davon |
CN2005800005470A CN1806043B (zh) | 2004-04-08 | 2005-04-08 | 脂肪酶粉末、其制备方法及其应用 |
CA002529985A CA2529985A1 (en) | 2004-04-08 | 2005-04-08 | A lipase powder, methods for producing the same and use thereof |
DE602005018468T DE602005018468D1 (de) | 2004-04-08 | 2005-04-08 | Lipasepulver, verfahren zur herstellung davon und verwendung davon |
EP05728493A EP1734114B1 (en) | 2004-04-08 | 2005-04-08 | Lipase powder, process for producing the same and use thereof |
DK05728493.7T DK1734114T3 (da) | 2004-04-08 | 2005-04-08 | Lipasepulver, fremgangsmåde til fremstilling deraf og anvendelse deraf |
JP2006519482A JP4828418B2 (ja) | 2004-04-08 | 2005-04-08 | リパーゼ粉末、その製造方法及びその使用 |
US11/320,756 US20060105935A1 (en) | 2004-04-08 | 2005-12-30 | Lipase powder, methods for producing the same and use thereof |
US12/314,473 US8110386B2 (en) | 2004-04-08 | 2008-12-11 | Lipase powder, methods for producing the same and use thereof |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2004-114443 | 2004-04-08 | ||
JP2004114443 | 2004-04-08 |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US11/320,756 Continuation US20060105935A1 (en) | 2004-04-08 | 2005-12-30 | Lipase powder, methods for producing the same and use thereof |
Publications (1)
Publication Number | Publication Date |
---|---|
WO2005097984A1 true WO2005097984A1 (ja) | 2005-10-20 |
Family
ID=35125069
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/JP2005/006908 WO2005097984A1 (ja) | 2004-04-08 | 2005-04-08 | リパーゼ粉末、その製造方法及びその使用 |
Country Status (13)
Country | Link |
---|---|
US (2) | US20060105935A1 (ja) |
EP (1) | EP1734114B1 (ja) |
JP (1) | JP4828418B2 (ja) |
KR (1) | KR20070006656A (ja) |
CN (1) | CN1806043B (ja) |
AT (1) | ATE452971T1 (ja) |
CA (1) | CA2529985A1 (ja) |
DE (1) | DE602005018468D1 (ja) |
DK (1) | DK1734114T3 (ja) |
ES (1) | ES2336012T3 (ja) |
MY (1) | MY142014A (ja) |
TW (1) | TW200538550A (ja) |
WO (1) | WO2005097984A1 (ja) |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2008010543A1 (fr) * | 2006-07-19 | 2008-01-24 | The Nisshin Oillio Group, Ltd. | Procédé destiné à produire un beurre solide adapté à un produit de chocolaterie |
JP2010110283A (ja) * | 2008-11-07 | 2010-05-20 | Kobayashi Pharmaceut Co Ltd | ヒハツ抽出物を含有する飲食品組成物及びヒハツ抽出物含有飲食品組成物の味改善方法 |
WO2011068076A1 (ja) * | 2009-12-01 | 2011-06-09 | 日清オイリオグループ株式会社 | リパーゼ粉末製剤及びその使用 |
JP5145609B2 (ja) * | 2007-03-16 | 2013-02-20 | 日清オイリオグループ株式会社 | リパーゼ粉末製剤、その製造方法及び使用 |
Families Citing this family (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
TWI429400B (zh) * | 2007-09-07 | 2014-03-11 | Nisshin Oillio Group Ltd | 硬奶油的製造方法 |
UY33548A (es) * | 2010-08-06 | 2012-02-29 | Eurand Pharmaceuticals Inc | Formula nutricional predigerida |
CN102226173B (zh) * | 2011-05-06 | 2014-02-12 | 华南理工大学 | 一种稳定型酶制剂及其制备方法和应用 |
CN114916590B (zh) * | 2022-05-20 | 2024-05-14 | 甘南牦牛乳研究院 | 一种牦牛乳酥油脱膻增香方法 |
CN115418275A (zh) * | 2022-07-22 | 2022-12-02 | 武汉新华扬生物股份有限公司 | 一种中链脂肪酸的提取方法及其应用 |
Citations (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5417179A (en) * | 1977-07-08 | 1979-02-08 | Sankyo Co Ltd | Preparation of powdered enzyme |
JPH05244948A (ja) * | 1992-08-07 | 1993-09-24 | Amano Pharmaceut Co Ltd | アスコルビン酸酸化酵素の安定化方法 |
JPH0779789A (ja) * | 1993-09-17 | 1995-03-28 | Nisshin Oil Mills Ltd:The | リパーゼ粉末を用いたエステル交換法 |
WO1996011264A1 (fr) * | 1994-10-11 | 1996-04-18 | Ajinomoto Co., Inc. | Transglutaminase stabilisee et preparation enzymatique contenant cette transglutaminase |
JPH08187095A (ja) * | 1995-01-10 | 1996-07-23 | Toyobo Co Ltd | コレステロールオキシダーゼの安定化法 |
JPH11349491A (ja) * | 1998-06-01 | 1999-12-21 | Amano Pharmaceut Co Ltd | アスペルギルス・ニガー由来のリパーゼの安定化組成物および安定化法 |
Family Cites Families (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
FR2362863A1 (fr) * | 1976-08-24 | 1978-03-24 | Degussa | Preparations de lipases a action amelioree et preparations medicales ameliorees contenant des lipases d'origine non animale |
DE2638089C2 (de) * | 1976-08-24 | 1985-04-25 | Degussa Ag, 6000 Frankfurt | Lipase-Präparate mit verbesserter Wirkung |
DK402583D0 (da) | 1983-09-05 | 1983-09-05 | Novo Industri As | Fremgangsmade til fremstilling af et immobiliseret lipasepraeparat og anvendelse deraf |
DK153762C (da) | 1985-02-27 | 1989-01-09 | Novo Industri As | Fremgangsmaade til fremstilling af et immobiliseret lipasepraeparat |
US4766074A (en) * | 1986-01-17 | 1988-08-23 | Miles Inc. | Thermostable Rhizomucor rennet having increased milk clotting activity |
GB8729890D0 (en) | 1987-12-22 | 1988-02-03 | Unilever Plc | Improvements in & relating to fat processes |
JP2749587B2 (ja) | 1988-04-11 | 1998-05-13 | 花王株式会社 | 固定化酵素の製造方法 |
JP2794201B2 (ja) | 1989-07-31 | 1998-09-03 | 味の素株式会社 | 固定化リパーゼ酵素剤 |
IL129086A0 (en) * | 1999-03-22 | 2000-02-17 | Enzymotec Ltd | Surfactant-lipase complex immobilized on insoluble matrix |
JP2000106873A (ja) | 1998-10-06 | 2000-04-18 | Nisshin Oil Mills Ltd:The | 熱安定性酵素およびその製造法 |
US6635303B1 (en) * | 2000-06-30 | 2003-10-21 | Hawley & Hoops, Inc. | Powdered milk solids for providing a developed milk flavor to chocolate, the method of preparation and chocolate prepared with the same |
CN1406630A (zh) * | 2001-08-29 | 2003-04-02 | 郑振标 | 一种复合酶反应液 |
-
2005
- 2005-04-07 MY MYPI20051555A patent/MY142014A/en unknown
- 2005-04-08 TW TW094111250A patent/TW200538550A/zh unknown
- 2005-04-08 AT AT05728493T patent/ATE452971T1/de not_active IP Right Cessation
- 2005-04-08 CN CN2005800005470A patent/CN1806043B/zh active Active
- 2005-04-08 EP EP05728493A patent/EP1734114B1/en not_active Not-in-force
- 2005-04-08 ES ES05728493T patent/ES2336012T3/es active Active
- 2005-04-08 JP JP2006519482A patent/JP4828418B2/ja active Active
- 2005-04-08 KR KR1020067000995A patent/KR20070006656A/ko not_active Application Discontinuation
- 2005-04-08 CA CA002529985A patent/CA2529985A1/en not_active Abandoned
- 2005-04-08 DK DK05728493.7T patent/DK1734114T3/da active
- 2005-04-08 WO PCT/JP2005/006908 patent/WO2005097984A1/ja not_active Application Discontinuation
- 2005-04-08 DE DE602005018468T patent/DE602005018468D1/de active Active
- 2005-12-30 US US11/320,756 patent/US20060105935A1/en not_active Abandoned
-
2008
- 2008-12-11 US US12/314,473 patent/US8110386B2/en not_active Expired - Fee Related
Patent Citations (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5417179A (en) * | 1977-07-08 | 1979-02-08 | Sankyo Co Ltd | Preparation of powdered enzyme |
JPH05244948A (ja) * | 1992-08-07 | 1993-09-24 | Amano Pharmaceut Co Ltd | アスコルビン酸酸化酵素の安定化方法 |
JPH0779789A (ja) * | 1993-09-17 | 1995-03-28 | Nisshin Oil Mills Ltd:The | リパーゼ粉末を用いたエステル交換法 |
WO1996011264A1 (fr) * | 1994-10-11 | 1996-04-18 | Ajinomoto Co., Inc. | Transglutaminase stabilisee et preparation enzymatique contenant cette transglutaminase |
JPH08187095A (ja) * | 1995-01-10 | 1996-07-23 | Toyobo Co Ltd | コレステロールオキシダーゼの安定化法 |
JPH11349491A (ja) * | 1998-06-01 | 1999-12-21 | Amano Pharmaceut Co Ltd | アスペルギルス・ニガー由来のリパーゼの安定化組成物および安定化法 |
Non-Patent Citations (2)
Title |
---|
PENCREAC'H G. ET AL.: "An ultraviolet spectrophotometric assay for measuring lipase activity using long-chain triacyglycerols from Aleurites fordii seeds.", ANAL. BIOCHEM., vol. 303, no. 1, 2002, pages 17 - 24, XP002990175 * |
XIAO Y. ET AL.: "Purification and partial characterization of Rhizomucor miehei lipase for ester synthesis.", APPL. BIOCHEM. BIOTECHN., vol. 59, no. 2, 1996, pages 146 - 58, XP008052456 * |
Cited By (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2008010543A1 (fr) * | 2006-07-19 | 2008-01-24 | The Nisshin Oillio Group, Ltd. | Procédé destiné à produire un beurre solide adapté à un produit de chocolaterie |
JPWO2008010543A1 (ja) * | 2006-07-19 | 2009-12-17 | 日清オイリオグループ株式会社 | チョコレート製品に適するハードバターの製造方法 |
RU2445351C2 (ru) * | 2006-07-19 | 2012-03-20 | Дзе Ниссин Ойллио Груп, Лтд. | Способ получения твердого масла, подходящего для шоколадных продуктов |
JP5145609B2 (ja) * | 2007-03-16 | 2013-02-20 | 日清オイリオグループ株式会社 | リパーゼ粉末製剤、その製造方法及び使用 |
JP2010110283A (ja) * | 2008-11-07 | 2010-05-20 | Kobayashi Pharmaceut Co Ltd | ヒハツ抽出物を含有する飲食品組成物及びヒハツ抽出物含有飲食品組成物の味改善方法 |
WO2011068076A1 (ja) * | 2009-12-01 | 2011-06-09 | 日清オイリオグループ株式会社 | リパーゼ粉末製剤及びその使用 |
Also Published As
Publication number | Publication date |
---|---|
JP4828418B2 (ja) | 2011-11-30 |
EP1734114A1 (en) | 2006-12-20 |
EP1734114B1 (en) | 2009-12-23 |
MY142014A (en) | 2010-08-16 |
TW200538550A (en) | 2005-12-01 |
KR20070006656A (ko) | 2007-01-11 |
CN1806043A (zh) | 2006-07-19 |
US20060105935A1 (en) | 2006-05-18 |
CN1806043B (zh) | 2011-04-20 |
CA2529985A1 (en) | 2005-10-20 |
ATE452971T1 (de) | 2010-01-15 |
US8110386B2 (en) | 2012-02-07 |
DE602005018468D1 (de) | 2010-02-04 |
US20090104680A1 (en) | 2009-04-23 |
EP1734114A4 (en) | 2007-06-06 |
DK1734114T3 (da) | 2010-04-26 |
JPWO2005097984A1 (ja) | 2008-02-28 |
ES2336012T3 (es) | 2010-04-07 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP4828418B2 (ja) | リパーゼ粉末、その製造方法及びその使用 | |
WO2006022166A1 (ja) | リパーゼ粉末組成物及びそれを用いたエステル化物の製造方法 | |
JP5145609B2 (ja) | リパーゼ粉末製剤、その製造方法及び使用 | |
WO2005097985A1 (ja) | 1,3-特異性リパーゼ粉末、その製造方法及びその使用 | |
JPWO2006077860A1 (ja) | 精製リパーゼの製造方法 | |
JP2007068426A (ja) | リパーゼ粉末製剤、その製造方法及び使用 | |
JP5728335B2 (ja) | エステル交換油脂の製造方法及びその装置 | |
WO2011068076A1 (ja) | リパーゼ粉末製剤及びその使用 | |
WO2006030889A1 (ja) | リパーゼ粉末、その製造方法及びその使用 | |
JP5258941B2 (ja) | リパーゼ活性の回復方法 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
WWE | Wipo information: entry into national phase |
Ref document number: 200580000547.0 Country of ref document: CN |
|
AK | Designated states |
Kind code of ref document: A1 Designated state(s): AE AG AL AM AT AU AZ BA BB BG BR BW BY BZ CA CH CN CO CR CU CZ DE DK DM DZ EC EE EG ES FI GB GD GE GH GM HR HU ID IL IN IS JP KE KG KM KP KR KZ LC LK LR LS LT LU LV MA MD MG MK MN MW MX MZ NA NI NO NZ OM PG PH PL PT RO RU SC SD SE SG SK SL SM SY TJ TM TN TR TT TZ UA UG US UZ VC VN YU ZA ZM ZW |
|
AL | Designated countries for regional patents |
Kind code of ref document: A1 Designated state(s): GM KE LS MW MZ NA SD SL SZ TZ UG ZM ZW AM AZ BY KG KZ MD RU TJ TM AT BE BG CH CY CZ DE DK EE ES FI FR GB GR HU IE IS IT LT LU MC NL PL PT RO SE SI SK TR BF BJ CF CG CI CM GA GN GQ GW ML MR NE SN TD TG |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2006519482 Country of ref document: JP |
|
WWE | Wipo information: entry into national phase |
Ref document number: 2529985 Country of ref document: CA |
|
121 | Ep: the epo has been informed by wipo that ep was designated in this application | ||
WWE | Wipo information: entry into national phase |
Ref document number: 2005728493 Country of ref document: EP |
|
WWE | Wipo information: entry into national phase |
Ref document number: 11320756 Country of ref document: US |
|
WWE | Wipo information: entry into national phase |
Ref document number: 1020067000995 Country of ref document: KR |
|
WWP | Wipo information: published in national office |
Ref document number: 11320756 Country of ref document: US |
|
NENP | Non-entry into the national phase |
Ref country code: DE |
|
WWW | Wipo information: withdrawn in national office |
Ref document number: DE |
|
WWP | Wipo information: published in national office |
Ref document number: 2005728493 Country of ref document: EP |
|
WWP | Wipo information: published in national office |
Ref document number: 1020067000995 Country of ref document: KR |