JPS5966886A - 酵素の固定化方法 - Google Patents

酵素の固定化方法

Info

Publication number: JPS5966886A
Authority: JP; Japan
Prior art keywords: protein; gel; solution; enzyme; active substance
Prior art date: 1982-10-06
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Granted

Application number

JP17588182A

Other languages

English (en)

Japanese (ja)

Other versions

JPH0320232B2 (2

Inventor

Masao Motoki

本木　正雄

Norimare Nio

式希丹尾

Koichi Takinami

弘一滝波

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Ajinomoto Co Inc

Original Assignee

Ajinomoto Co Inc

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1982-10-06

Filing date

1982-10-06

Publication date

1984-04-16

1982-10-06 Application filed by Ajinomoto Co Inc filed Critical Ajinomoto Co Inc

1982-10-06 Priority to JP17588182A priority Critical patent/JPS5966886A/ja

1984-04-16 Publication of JPS5966886A publication Critical patent/JPS5966886A/ja

1991-03-18 Publication of JPH0320232B2 publication Critical patent/JPH0320232B2/ja

Status Granted legal-status Critical Current

Links

102000004190 Enzymes Human genes 0.000 title claims abstract description 22
108090000790 Enzymes Proteins 0.000 title claims abstract description 22
102000004169 proteins and genes Human genes 0.000 claims abstract description 37
108090000623 proteins and genes Proteins 0.000 claims abstract description 37
239000013543 active substance Substances 0.000 claims abstract description 18
108060008539 Transglutaminase Proteins 0.000 claims abstract description 13
102000003601 transglutaminase Human genes 0.000 claims abstract description 13
238000000034 method Methods 0.000 claims description 17
235000018102 proteins Nutrition 0.000 abstract description 33
239000011259 mixed solution Substances 0.000 abstract description 4
108010093096 Immobilized Enzymes Proteins 0.000 abstract description 3
238000001879 gelation Methods 0.000 abstract description 3
102000005744 Glycoside Hydrolases Human genes 0.000 abstract description 2
108010031186 Glycoside Hydrolases Proteins 0.000 abstract description 2
102000014171 Milk Proteins Human genes 0.000 abstract description 2
108010011756 Milk Proteins Proteins 0.000 abstract description 2
229940079593 drug Drugs 0.000 abstract description 2
239000003814 drug Substances 0.000 abstract description 2
235000013305 food Nutrition 0.000 abstract description 2
235000021239 milk protein Nutrition 0.000 abstract description 2
239000000126 substance Substances 0.000 abstract description 2
102000001696 Mannosidases Human genes 0.000 abstract 1
108010054377 Mannosidases Proteins 0.000 abstract 1
108010073771 Soybean Proteins Proteins 0.000 abstract 1
239000007864 aqueous solution Substances 0.000 abstract 1
239000011230 binding agent Substances 0.000 abstract 1
238000010438 heat treatment Methods 0.000 abstract 1
235000019710 soybean protein Nutrition 0.000 abstract 1
239000000499 gel Substances 0.000 description 30
239000000243 solution Substances 0.000 description 30
239000005018 casein Substances 0.000 description 24
BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 24
235000021240 caseins Nutrition 0.000 description 24
229940088598 enzyme Drugs 0.000 description 19
230000000694 effects Effects 0.000 description 12
238000006243 chemical reaction Methods 0.000 description 8
239000000872 buffer Substances 0.000 description 7
239000000203 mixture Substances 0.000 description 7
QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 6
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
102000002322 Egg Proteins Human genes 0.000 description 6
108010000912 Egg Proteins Proteins 0.000 description 6
235000014103 egg white Nutrition 0.000 description 6
210000000969 egg white Anatomy 0.000 description 6
102000016938 Catalase Human genes 0.000 description 5
108010053835 Catalase Proteins 0.000 description 5
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 5
238000002835 absorbance Methods 0.000 description 5
239000008103 glucose Substances 0.000 description 5
101000950981 Bacillus subtilis (strain 168) Catabolic NAD-specific glutamate dehydrogenase RocG Proteins 0.000 description 4
102000016901 Glutamate dehydrogenase Human genes 0.000 description 4
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
239000000758 substrate Substances 0.000 description 4
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 3
238000004519 manufacturing process Methods 0.000 description 3
239000000463 material Substances 0.000 description 3
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
229920001817 Agar Polymers 0.000 description 2
244000163122 Curcuma domestica Species 0.000 description 2
235000003392 Curcuma domestica Nutrition 0.000 description 2
108010082495 Dietary Plant Proteins Proteins 0.000 description 2
108010010803 Gelatin Proteins 0.000 description 2
108010015776 Glucose oxidase Proteins 0.000 description 2
239000004366 Glucose oxidase Substances 0.000 description 2
102000009127 Glutaminase Human genes 0.000 description 2
108010073324 Glutaminase Proteins 0.000 description 2
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 2
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
235000021120 animal protein Nutrition 0.000 description 2
239000007853 buffer solution Substances 0.000 description 2
235000003373 curcuma longa Nutrition 0.000 description 2
230000007423 decrease Effects 0.000 description 2
239000008273 gelatin Substances 0.000 description 2
229920000159 gelatin Polymers 0.000 description 2
235000019322 gelatine Nutrition 0.000 description 2
235000011852 gelatine desserts Nutrition 0.000 description 2
229940116332 glucose oxidase Drugs 0.000 description 2
235000019420 glucose oxidase Nutrition 0.000 description 2
230000003100 immobilizing effect Effects 0.000 description 2
-1 kolaken Substances 0.000 description 2
238000006116 polymerization reaction Methods 0.000 description 2
239000001632 sodium acetate Substances 0.000 description 2
235000017281 sodium acetate Nutrition 0.000 description 2
235000013976 turmeric Nutrition 0.000 description 2
AEELXMHQIJJMKP-QWWZWVQMSA-N (2r,3r)-3-sulfanylbutane-1,2,4-triol Chemical compound OC[C@@H](O)[C@H](S)CO AEELXMHQIJJMKP-QWWZWVQMSA-N 0.000 description 1
IFBHRQDFSNCLOZ-GCHJQGSQSA-N (2r,3s,4s,5s,6r)-2-(hydroxymethyl)-6-(4-nitrophenoxy)oxane-3,4,5-triol Chemical compound O[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC1=CC=C([N+]([O-])=O)C=C1 IFBHRQDFSNCLOZ-GCHJQGSQSA-N 0.000 description 1
LJRDOKAZOAKLDU-UDXJMMFXSA-N (2s,3s,4r,5r,6r)-5-amino-2-(aminomethyl)-6-[(2r,3s,4r,5s)-5-[(1r,2r,3s,5r,6s)-3,5-diamino-2-[(2s,3r,4r,5s,6r)-3-amino-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-hydroxycyclohexyl]oxy-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl]oxyoxane-3,4-diol;sulfuric ac Chemical compound OS(O)(=O)=O.N[C@@H]1[C@@H](O)[C@H](O)[C@H](CN)O[C@@H]1O[C@H]1[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](N)C[C@@H](N)[C@@H]2O)O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)N)O[C@@H]1CO LJRDOKAZOAKLDU-UDXJMMFXSA-N 0.000 description 1
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
KPGXRSRHYNQIFN-UHFFFAOYSA-N 2-oxoglutaric acid Chemical compound OC(=O)CCC(=O)C(O)=O KPGXRSRHYNQIFN-UHFFFAOYSA-N 0.000 description 1
DEXFNLNNUZKHNO-UHFFFAOYSA-N 6-[3-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperidin-1-yl]-3-oxopropyl]-3H-1,3-benzoxazol-2-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C1CCN(CC1)C(CCC1=CC2=C(NC(O2)=O)C=C1)=O DEXFNLNNUZKHNO-UHFFFAOYSA-N 0.000 description 1
FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical compound O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 description 1
229930024421 Adenine Natural products 0.000 description 1
GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 1
102000014914 Carrier Proteins Human genes 0.000 description 1
108010078791 Carrier Proteins Proteins 0.000 description 1
102000008186 Collagen Human genes 0.000 description 1
108010035532 Collagen Proteins 0.000 description 1
101710088194 Dehydrogenase Proteins 0.000 description 1
JOYRKODLDBILNP-UHFFFAOYSA-N Ethyl urethane Chemical compound CCOC(N)=O JOYRKODLDBILNP-UHFFFAOYSA-N 0.000 description 1
229930091371 Fructose Natural products 0.000 description 1
239000005715 Fructose Substances 0.000 description 1
RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
244000068988 Glycine max Species 0.000 description 1
235000010469 Glycine max Nutrition 0.000 description 1
101100448410 Mus musculus Gkn1 gene Proteins 0.000 description 1
101100109871 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) aro-8 gene Proteins 0.000 description 1
102000004316 Oxidoreductases Human genes 0.000 description 1
108090000854 Oxidoreductases Proteins 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
102000003992 Peroxidases Human genes 0.000 description 1
102000006382 Ribonucleases Human genes 0.000 description 1
108010083644 Ribonucleases Proteins 0.000 description 1
229920002494 Zein Polymers 0.000 description 1
239000008351 acetate buffer Substances 0.000 description 1
239000002253 acid Substances 0.000 description 1
229960000643 adenine Drugs 0.000 description 1
239000008272 agar Substances 0.000 description 1
229940072056 alginate Drugs 0.000 description 1
235000010443 alginic acid Nutrition 0.000 description 1
229920000615 alginic acid Polymers 0.000 description 1
150000001413 amino acids Chemical class 0.000 description 1
QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
239000000969 carrier Substances 0.000 description 1
229920001436 collagen Polymers 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
230000009849 deactivation Effects 0.000 description 1
239000012153 distilled water Substances 0.000 description 1
125000004119 disulfanediyl group Chemical group *SS* 0.000 description 1
239000000835 fiber Substances 0.000 description 1
239000003999 initiator Substances 0.000 description 1
210000003127 knee Anatomy 0.000 description 1
239000008101 lactose Substances 0.000 description 1
239000007788 liquid Substances 0.000 description 1
230000007774 longterm Effects 0.000 description 1
235000013336 milk Nutrition 0.000 description 1
239000008267 milk Substances 0.000 description 1
210000004080 milk Anatomy 0.000 description 1
229930014626 natural product Natural products 0.000 description 1
239000001301 oxygen Substances 0.000 description 1
229910052760 oxygen Inorganic materials 0.000 description 1
239000008188 pellet Substances 0.000 description 1
229960001639 penicillamine Drugs 0.000 description 1
108040007629 peroxidase activity proteins Proteins 0.000 description 1
239000000825 pharmaceutical preparation Substances 0.000 description 1
229940127557 pharmaceutical product Drugs 0.000 description 1
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
239000010452 phosphate Substances 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
239000012460 protein solution Substances 0.000 description 1
239000011347 resin Substances 0.000 description 1
229920005989 resin Polymers 0.000 description 1
238000001179 sorption measurement Methods 0.000 description 1
239000007921 spray Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
239000005019 zein Substances 0.000 description 1
229940093612 zein Drugs 0.000 description 1

Landscapes

Immobilizing And Processing Of Enzymes And Microorganisms (AREA)

JP17588182A 1982-10-06 1982-10-06 酵素の固定化方法 Granted JPS5966886A (ja)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP17588182A JPS5966886A (ja)	1982-10-06	1982-10-06	酵素の固定化方法

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP17588182A JPS5966886A (ja)	1982-10-06	1982-10-06	酵素の固定化方法

Publications (2)

Publication Number	Publication Date
JPS5966886A true JPS5966886A (ja)	1984-04-16
JPH0320232B2 JPH0320232B2 (2)	1991-03-18

Family

ID=16003836

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP17588182A Granted JPS5966886A (ja)	1982-10-06	1982-10-06	酵素の固定化方法

Country Status (1)

Country	Link
JP (1)	JPS5966886A (2)

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS61227783A (ja) *	1985-04-03	1986-10-09	Ajinomoto Co Inc	固定化酵素膜の製造法
US5037664A (en) *	1988-10-15	1991-08-06	Suntory Limited	Process for producing novel gel-like food articles
WO1999006446A3 (de) *	1997-07-30	1999-04-08	Fuchsbauer Hans Lothar	Verfahren zum transglutaminase-katalysierten koppeln von protein oder peptid an einen träger
EP0963704A3 (en) *	1998-06-09	1999-12-22	Ajinomoto Co., Ltd.	Food containing proteinaceous material treated with a transglutaminase and an oxidoreductase

1982
- 1982-10-06 JP JP17588182A patent/JPS5966886A/ja active Granted

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS61227783A (ja) *	1985-04-03	1986-10-09	Ajinomoto Co Inc	固定化酵素膜の製造法
US5037664A (en) *	1988-10-15	1991-08-06	Suntory Limited	Process for producing novel gel-like food articles
WO1999006446A3 (de) *	1997-07-30	1999-04-08	Fuchsbauer Hans Lothar	Verfahren zum transglutaminase-katalysierten koppeln von protein oder peptid an einen träger
EP0963704A3 (en) *	1998-06-09	1999-12-22	Ajinomoto Co., Ltd.	Food containing proteinaceous material treated with a transglutaminase and an oxidoreductase
JP2000060431A (ja) *	1998-06-09	2000-02-29	Ajinomoto Co Inc	新規酵素処理蛋白質含有食品、その製造方法及びそれに使用する酵素製剤

Also Published As

Publication number	Publication date
JPH0320232B2 (2)	1991-03-18

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Tavano et al.	2018	Biotechnological applications of proteases in food technology
JP3003045B2 (ja)	2000-01-24	粒子状抗菌物質の製造方法および得られた抗菌物質
JPH0665280B2 (ja)	1994-08-24	タンパクゲル化剤及びそれを用いるタンパクのゲル化方法
CA1041351A (en)	1978-10-31	Process for the production of protein-containing food additives
JPH11276162A (ja)	1999-10-12	酵素による蛋白質の架橋法
US6399117B1 (en)	2002-06-04	Method for the modification of protein structure in finish shaped feed pellets, balls or the like in order to achieve shape stability, and feed mass made in accordance with the method
JPH08508933A (ja)	1996-09-24	水性媒体において膜をゲル化粒子の少なくとも表面に形成するためのエステル化多糖とポリアミンとの間のアシル交換反応の使用、それにより生成した粒子、それらの製造方法及び前記粒子を含有する組成物
PT98564B (pt)	1999-01-29	Processo para a realizacao de processos catalizados por enzimas com cristais reticulados como forma de imobilizacao de enzimas e dispositivos que os contem
JPS59113889A (ja)	1984-06-30	固定化酵素もしくは固定化微生物菌体の製造方法
Dahlqvist et al.	1977	Hydrolysis of lactose in milk and whey with minute amounts of lactase
JPH0154985B2 (2)	1989-11-21
JP5282252B2 (ja)	2013-09-04	澱粉粒又はセルロース粉末固定化リパーゼの製造方法、乳化素材の製造方法及び乳化剤
Mariniello et al.	2005	Transglutaminases as biotechnological tools
JPH05268950A (ja)	1993-10-19	修飾酵素
JP2650366B2 (ja)	1997-09-03	固形脂及びその製造法
JPH0320232B2 (2)	1991-03-18
JPH0160235B2 (2)	1989-12-21
JPH11116935A (ja)	1999-04-27	パントテン酸カルシウムを用いたゲルの調製方法
JP4295387B2 (ja)	2009-07-15	分解ペプチド類の製造法
JP2580732B2 (ja)	1997-02-12	変性タンパク質を基材とするカプセル
JPH08224063A (ja)	1996-09-03	タンパクゲル化組成物
TWI299257B (en)	2008-08-01	γ-POLYGLUTAMIC ACID (γ-PGA, H FORM), γ-POLYGLUTAMATES AND γ-POLYGLUTAMATE HYDROGEL FOR USE AS NUTRITION SUPPLEMENTS IN DIETARY PRODUCTS
JPH0678783A (ja)	1994-03-22	タンパクゲル化物の製造方法
Bouzas et al.	1984	Protein polymerization in red cell membranes
JPH1175887A (ja)	1999-03-23	ペルオキシダーゼによる蛋白質の架橋高分子化方法