JPH0320232B2 - - Google Patents

Info

Publication number: JPH0320232B2
Authority: JP; Japan
Prior art keywords: gel; protein; solution; casein; units
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.): Expired

Application number

JP17588182A

Other languages

English (en)

Japanese (ja)

Other versions

JPS5966886A (ja

Inventor

Masao Motoki

Norimare Nio

Koichi Takinami

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

1991-03-18

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

102000004169 proteins and genes Human genes 0.000 claims description 34
108090000623 proteins and genes Proteins 0.000 claims description 34
102000004190 Enzymes Human genes 0.000 claims description 18
108090000790 Enzymes Proteins 0.000 claims description 18
108060008539 Transglutaminase Proteins 0.000 claims description 15
102000003601 transglutaminase Human genes 0.000 claims description 15
239000013543 active substance Substances 0.000 claims description 14
238000000034 method Methods 0.000 claims description 13
239000000499 gel Substances 0.000 description 37
235000018102 proteins Nutrition 0.000 description 30
239000000243 solution Substances 0.000 description 30
239000005018 casein Substances 0.000 description 29
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 29
235000021240 caseins Nutrition 0.000 description 29
229940088598 enzyme Drugs 0.000 description 16
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 12
230000000694 effects Effects 0.000 description 10
108010015776 Glucose oxidase Proteins 0.000 description 8
239000004366 Glucose oxidase Substances 0.000 description 8
239000000872 buffer Substances 0.000 description 8
238000006243 chemical reaction Methods 0.000 description 8
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 8
229940116332 glucose oxidase Drugs 0.000 description 8
235000019420 glucose oxidase Nutrition 0.000 description 8
102000016938 Catalase Human genes 0.000 description 7
108010053835 Catalase Proteins 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
239000000463 material Substances 0.000 description 6
239000000203 mixture Substances 0.000 description 6
101000950981 Bacillus subtilis (strain 168) Catabolic NAD-specific glutamate dehydrogenase RocG Proteins 0.000 description 5
102000016901 Glutamate dehydrogenase Human genes 0.000 description 5
238000002835 absorbance Methods 0.000 description 5
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
239000000758 substrate Substances 0.000 description 4
108010010803 Gelatin Proteins 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
102000005744 Glycoside Hydrolases Human genes 0.000 description 3
108010031186 Glycoside Hydrolases Proteins 0.000 description 3
102000001696 Mannosidases Human genes 0.000 description 3
108010054377 Mannosidases Proteins 0.000 description 3
108020002230 Pancreatic Ribonuclease Proteins 0.000 description 3
102000005891 Pancreatic ribonuclease Human genes 0.000 description 3
239000008273 gelatin Substances 0.000 description 3
229920000159 gelatin Polymers 0.000 description 3
235000019322 gelatine Nutrition 0.000 description 3
235000011852 gelatine desserts Nutrition 0.000 description 3
238000001879 gelation Methods 0.000 description 3
238000004519 manufacturing process Methods 0.000 description 3
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
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 2
229920001817 Agar Polymers 0.000 description 2
102000008186 Collagen Human genes 0.000 description 2
108010035532 Collagen Proteins 0.000 description 2
108010082495 Dietary Plant Proteins Proteins 0.000 description 2
108010093096 Immobilized Enzymes 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
229920001436 collagen Polymers 0.000 description 2
230000003100 immobilizing effect Effects 0.000 description 2
229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 2
BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 2
238000006116 polymerization reaction Methods 0.000 description 2
239000012460 protein solution Substances 0.000 description 2
239000001632 sodium acetate Substances 0.000 description 2
235000017281 sodium acetate Nutrition 0.000 description 2
239000000126 substance Substances 0.000 description 2
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
PHOLIFLKGONSGY-CSKARUKUSA-N (e)-(3-methyl-1,3-benzothiazol-2-ylidene)hydrazine Chemical compound C1=CC=C2S\C(=N\N)N(C)C2=C1 PHOLIFLKGONSGY-CSKARUKUSA-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
IFBHRQDFSNCLOZ-ZIQFBCGOSA-N 4-nitrophenyl alpha-D-glucoside 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-ZIQFBCGOSA-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
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
102000014914 Carrier Proteins Human genes 0.000 description 1
108010078791 Carrier Proteins Proteins 0.000 description 1
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 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
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 1
235000010469 Glycine max Nutrition 0.000 description 1
244000068988 Glycine max Species 0.000 description 1
102000014171 Milk Proteins Human genes 0.000 description 1
108010011756 Milk Proteins Proteins 0.000 description 1
FBWADIKARMIWNM-UHFFFAOYSA-N N-3,5-dichloro-4-hydroxyphenyl-1,4-benzoquinone imine Chemical compound C1=C(Cl)C(O)=C(Cl)C=C1N=C1C=CC(=O)C=C1 FBWADIKARMIWNM-UHFFFAOYSA-N 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
102000003992 Peroxidases Human genes 0.000 description 1
239000008351 acetate buffer Substances 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
239000001110 calcium chloride Substances 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
235000011148 calcium chloride Nutrition 0.000 description 1
239000000969 carrier Substances 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
230000009849 deactivation Effects 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
-1 diafluorase Proteins 0.000 description 1
GGSUCNLOZRCGPQ-UHFFFAOYSA-N diethylaniline Chemical compound CCN(CC)C1=CC=CC=C1 GGSUCNLOZRCGPQ-UHFFFAOYSA-N 0.000 description 1
239000012153 distilled water Substances 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
239000006260 foam Substances 0.000 description 1
235000013305 food Nutrition 0.000 description 1
239000008103 glucose Substances 0.000 description 1
239000003999 initiator Substances 0.000 description 1
239000008101 lactose Substances 0.000 description 1
239000007788 liquid Substances 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
235000021239 milk protein Nutrition 0.000 description 1
239000011259 mixed solution Substances 0.000 description 1
229950006238 nadide Drugs 0.000 description 1
239000001301 oxygen Substances 0.000 description 1
229910052760 oxygen Inorganic materials 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
239000008363 phosphate buffer Substances 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
229920000642 polymer Polymers 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

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 JPS5966886A (ja)	1984-04-16
JPH0320232B2 true JPH0320232B2 (de)	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 (de)

Families Citing this family (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
JPH02107163A (ja) *	1988-10-15	1990-04-19	Suntory Ltd	新規なゲル状食品の製造方法
DE19732917C1 (de) *	1997-07-30	1998-10-15	Fuchsbauer Hans Lothar	Verfahren zum Transglutaminase-katalysierten Koppeln von Protein oder Peptid an einen Träger
AU761467B2 (en) *	1998-06-09	2003-06-05	Ajinomoto Co., Inc.	Novel enzyme-treated protein-containing food, and methods for producing the same

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

Also Published As

Publication number	Publication date
JPS5966886A (ja)	1984-04-16

Publication	Publication Date	Title
Dahlqvist et al.	1973	Hydrolysis of β‐galactosides using polymer‐entrapped lactase. A study towards producing lactose‐free milk
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
EP0523130A1 (de)	1993-01-20	Enzymstabilisierung
Dahlqvist et al.	1977	Hydrolysis of lactose in milk and whey with minute amounts of lactase
Zezin et al.	1989	Interpolyelectrolyte complexes as a new family of enzyme carriers
JPH0320232B2 (de)	1991-03-18
US20180110868A1 (en)	2018-04-26	Reactive and sorbent materials
JPH05268950A (ja)	1993-10-19	修飾酵素
Ohmiya et al.	1978	Preparation and properties of proteases immobilized on anion exchange resin with glutaraldehyde
JPS61111685A (ja)	1986-05-29	安定化された酵素及びその製造方法
JPS5974984A (ja)	1984-04-27	固定化酵素もしくは固定化微生物の製造方法
Rai et al.	1998	Production of D-amino acids using immobilized D-hydantoinase from lentil, Lens esculenta, seeds
EP0390633B1 (de)	1992-12-23	Teilhydrolysat aus Molkeproteinen, frei von Lactoglobulin und enzymatisches Verfahren zu dessen Gewinnung
JPH0678783A (ja)	1994-03-22	タンパクゲル化物の製造方法
Simon et al.	1985	Immobilization of pig muscle 3-phosphoglycerate kinase
Salleh et al.	1982	Protein-alginate gel for enzyme immobilisation
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
EP0899331B1 (de)	2007-02-21	Gereinigtes proteolytisches Enzym und Verfahren zur Reinigung
JPS5876089A (ja)	1983-05-09	酵素もしくは微生物の固定化方法
SU1472505A1 (ru)	1989-04-15	Способ иммобилизации ферментов
Chibber et al.	1974	Immobilized human plasmins: preparation and enzymatic properties
Al-Khafaji et al.	2009	Immobilization of urease in gelatin beads for urea estimation
JPS58152482A (ja)	1983-09-10	耐熱性蛋白分解酵素アクアライシンｉおよびその製造法
JP2748416B2 (ja)	1998-05-06	生理活性物質固定化膜の製造法
JPS63304992A (ja)	1988-12-13	油脂の分解法