JPS645876B2 - - Google Patents

Info

Publication number: JPS645876B2
Authority: JP; Japan
Prior art keywords: emulsion; urethane; solution; reaction; bacterial cells
Prior art date: 1984-05-01
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

JP8887984A

Other languages

English (en)

Japanese (ja)

Other versions

JPS60232089A (ja

Inventor

Atsuo Tanaka

Kenji Sonomoto

Akira Koshiro

Juzo Ozaki

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.)

Toyo Tire Corp

Original Assignee

Toyo Tire and Rubber Co Ltd

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.)

1984-05-01

Filing date

1984-05-01

Publication date

1989-02-01

1984-05-01 Application filed by Toyo Tire and Rubber Co Ltd filed Critical Toyo Tire and Rubber Co Ltd

1984-05-01 Priority to JP8887984A priority Critical patent/JPS60232089A/ja

1985-11-18 Publication of JPS60232089A publication Critical patent/JPS60232089A/ja

1989-02-01 Publication of JPS645876B2 publication Critical patent/JPS645876B2/ja

Status Granted legal-status Critical Current

Links

239000000839 emulsion Substances 0.000 claims description 31
102000004190 Enzymes Human genes 0.000 claims description 25
108090000790 Enzymes Proteins 0.000 claims description 25
238000000034 method Methods 0.000 claims description 23
229920002635 polyurethane Polymers 0.000 claims description 14
239000004814 polyurethane Substances 0.000 claims description 14
239000011942 biocatalyst Substances 0.000 claims description 13
125000003010 ionic group Chemical group 0.000 claims description 9
230000003100 immobilizing effect Effects 0.000 claims description 7
238000003756 stirring Methods 0.000 claims description 5
239000000203 mixture Substances 0.000 claims description 4
239000007864 aqueous solution Substances 0.000 claims description 3
239000007900 aqueous suspension Substances 0.000 claims description 2
150000001768 cations Chemical class 0.000 claims 1
210000004027 cell Anatomy 0.000 description 16
ZWEHNKRNPOVVGH-UHFFFAOYSA-N 2-Butanone Chemical compound CCC(C)=O ZWEHNKRNPOVVGH-UHFFFAOYSA-N 0.000 description 15
JOYRKODLDBILNP-UHFFFAOYSA-N Ethyl urethane Chemical compound CCOC(N)=O JOYRKODLDBILNP-UHFFFAOYSA-N 0.000 description 14
230000001580 bacterial effect Effects 0.000 description 14
229940088598 enzyme Drugs 0.000 description 12
239000000243 solution Substances 0.000 description 12
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 12
238000006243 chemical reaction Methods 0.000 description 11
-1 isocyanate compound Chemical class 0.000 description 9
239000002609 medium Substances 0.000 description 9
244000005700 microbiome Species 0.000 description 9
LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 8
239000004100 Oxytetracycline Substances 0.000 description 7
125000000129 anionic group Chemical group 0.000 description 7
IWVCMVBTMGNXQD-PXOLEDIWSA-N oxytetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3[C@H](O)[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O IWVCMVBTMGNXQD-PXOLEDIWSA-N 0.000 description 7
229960000625 oxytetracycline Drugs 0.000 description 7
235000019366 oxytetracycline Nutrition 0.000 description 7
IWVCMVBTMGNXQD-UHFFFAOYSA-N terramycin dehydrate Natural products C1=CC=C2C(O)(C)C3C(O)C4C(N(C)C)C(O)=C(C(N)=O)C(=O)C4(O)C(O)=C3C(=O)C2=C1O IWVCMVBTMGNXQD-UHFFFAOYSA-N 0.000 description 7
239000000499 gel Substances 0.000 description 6
230000007062 hydrolysis Effects 0.000 description 6
238000006460 hydrolysis reaction Methods 0.000 description 6
125000002091 cationic group Chemical group 0.000 description 5
238000004519 manufacturing process Methods 0.000 description 5
229920005862 polyol Polymers 0.000 description 5
229920001817 Agar Polymers 0.000 description 4
241000894006 Bacteria Species 0.000 description 4
RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
239000004367 Lipase Substances 0.000 description 4
102000004882 Lipase Human genes 0.000 description 4
108090001060 Lipase Proteins 0.000 description 4
239000008272 agar Substances 0.000 description 4
235000019421 lipase Nutrition 0.000 description 4
239000007788 liquid Substances 0.000 description 4
BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 4
229920000642 polymer Polymers 0.000 description 4
150000003077 polyols Chemical class 0.000 description 4
238000012360 testing method Methods 0.000 description 4
239000004970 Chain extender Substances 0.000 description 3
108010093096 Immobilized Enzymes Proteins 0.000 description 3
ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 3
230000000052 comparative effect Effects 0.000 description 3
239000008367 deionised water Substances 0.000 description 3
229910021641 deionized water Inorganic materials 0.000 description 3
238000006116 polymerization reaction Methods 0.000 description 3
230000035484 reaction time Effects 0.000 description 3
238000010992 reflux Methods 0.000 description 3
239000002904 solvent Substances 0.000 description 3
UPMLOUAZCHDJJD-UHFFFAOYSA-N 4,4'-Diphenylmethane Diisocyanate Chemical compound C1=CC(N=C=O)=CC=C1CC1=CC=C(N=C=O)C=C1 UPMLOUAZCHDJJD-UHFFFAOYSA-N 0.000 description 2
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
102000004195 Isomerases Human genes 0.000 description 2
108090000769 Isomerases Proteins 0.000 description 2
239000004721 Polyphenylene oxide Substances 0.000 description 2
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
WERYXYBDKMZEQL-UHFFFAOYSA-N butane-1,4-diol Chemical compound OCCCCO WERYXYBDKMZEQL-UHFFFAOYSA-N 0.000 description 2
239000000969 carrier Substances 0.000 description 2
230000003247 decreasing effect Effects 0.000 description 2
230000000694 effects Effects 0.000 description 2
239000011521 glass Substances 0.000 description 2
238000002329 infrared spectrum Methods 0.000 description 2
230000005764 inhibitory process Effects 0.000 description 2
238000002156 mixing Methods 0.000 description 2
239000003921 oil Substances 0.000 description 2
235000019198 oils Nutrition 0.000 description 2
239000004006 olive oil Substances 0.000 description 2
235000008390 olive oil Nutrition 0.000 description 2
KJFMBFZCATUALV-UHFFFAOYSA-N phenolphthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2C(=O)O1 KJFMBFZCATUALV-UHFFFAOYSA-N 0.000 description 2
229910052697 platinum Inorganic materials 0.000 description 2
229920000570 polyether Polymers 0.000 description 2
239000000047 product Substances 0.000 description 2
239000007787 solid Substances 0.000 description 2
239000000126 substance Substances 0.000 description 2
229920002803 thermoplastic polyurethane Polymers 0.000 description 2
DVKJHBMWWAPEIU-UHFFFAOYSA-N toluene 2,4-diisocyanate Chemical compound CC1=CC=C(N=C=O)C=C1N=C=O DVKJHBMWWAPEIU-UHFFFAOYSA-N 0.000 description 2
ULGJWNIHLSLQPZ-UHFFFAOYSA-N 7-[(6,8-dichloro-1,2,3,4-tetrahydroacridin-9-yl)amino]-n-[2-(1h-indol-3-yl)ethyl]heptanamide Chemical compound C1CCCC2=NC3=CC(Cl)=CC(Cl)=C3C(NCCCCCCC(=O)NCCC=3C4=CC=CC=C4NC=3)=C21 ULGJWNIHLSLQPZ-UHFFFAOYSA-N 0.000 description 1
241000186361 Actinobacteria <class> Species 0.000 description 1
239000004382 Amylase Substances 0.000 description 1
102000013142 Amylases Human genes 0.000 description 1
108010065511 Amylases Proteins 0.000 description 1
108700016171 Aspartate ammonia-lyases Proteins 0.000 description 1
241000589151 Azotobacter Species 0.000 description 1
241000193755 Bacillus cereus Species 0.000 description 1
244000063299 Bacillus subtilis Species 0.000 description 1
235000014469 Bacillus subtilis Nutrition 0.000 description 1
102100026189 Beta-galactosidase Human genes 0.000 description 1
102100035882 Catalase Human genes 0.000 description 1
108010053835 Catalase Proteins 0.000 description 1
241000588724 Escherichia coli Species 0.000 description 1
IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 1
241000233866 Fungi Species 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
239000004366 Glucose oxidase Substances 0.000 description 1
108010015776 Glucose oxidase Proteins 0.000 description 1
102000004157 Hydrolases Human genes 0.000 description 1
108090000604 Hydrolases Proteins 0.000 description 1
241000588915 Klebsiella aerogenes Species 0.000 description 1
108010059881 Lactase Proteins 0.000 description 1
241000186660 Lactobacillus Species 0.000 description 1
108090000856 Lyases Proteins 0.000 description 1
102000004317 Lyases Human genes 0.000 description 1
CERQOIWHTDAKMF-UHFFFAOYSA-M Methacrylate Chemical compound CC(=C)C([O-])=O CERQOIWHTDAKMF-UHFFFAOYSA-M 0.000 description 1
229920001730 Moisture cure polyurethane Polymers 0.000 description 1
239000004677 Nylon Substances 0.000 description 1
241000207836 Olea <angiosperm> Species 0.000 description 1
229930182555 Penicillin Natural products 0.000 description 1
JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
229920002367 Polyisobutene Polymers 0.000 description 1
239000004793 Polystyrene Substances 0.000 description 1
241000588767 Proteus vulgaris Species 0.000 description 1
240000004808 Saccharomyces cerevisiae Species 0.000 description 1
DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
241000187213 Streptomyces limosus Species 0.000 description 1
241000187419 Streptomyces rimosus Species 0.000 description 1
102000004357 Transferases Human genes 0.000 description 1
108090000992 Transferases Proteins 0.000 description 1
108010046334 Urease Proteins 0.000 description 1
UKLDJPRMSDWDSL-UHFFFAOYSA-L [dibutyl(dodecanoyloxy)stannyl] dodecanoate Chemical compound CCCCCCCCCCCC(=O)O[Sn](CCCC)(CCCC)OC(=O)CCCCCCCCCCC UKLDJPRMSDWDSL-UHFFFAOYSA-L 0.000 description 1
238000007605 air drying Methods 0.000 description 1
230000001476 alcoholic effect Effects 0.000 description 1
150000001412 amines Chemical class 0.000 description 1
108010003977 aminoacylase I Proteins 0.000 description 1
235000019418 amylase Nutrition 0.000 description 1
230000000844 anti-bacterial effect Effects 0.000 description 1
238000003556 assay Methods 0.000 description 1
239000011324 bead Substances 0.000 description 1
108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
108010005774 beta-Galactosidase Proteins 0.000 description 1
230000003115 biocidal effect Effects 0.000 description 1
229940041514 candida albicans extract Drugs 0.000 description 1
239000003054 catalyst Substances 0.000 description 1
239000007795 chemical reaction product Substances 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
229920001577 copolymer Polymers 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
230000009849 deactivation Effects 0.000 description 1
239000012975 dibutyltin dilaurate Substances 0.000 description 1
238000009792 diffusion process Methods 0.000 description 1
VAYGXNSJCAHWJZ-UHFFFAOYSA-N dimethyl sulfate Chemical compound COS(=O)(=O)OC VAYGXNSJCAHWJZ-UHFFFAOYSA-N 0.000 description 1
238000001035 drying Methods 0.000 description 1
229920001971 elastomer Polymers 0.000 description 1
210000003527 eukaryotic cell Anatomy 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
239000000284 extract Substances 0.000 description 1
239000008103 glucose Substances 0.000 description 1
229940116332 glucose oxidase Drugs 0.000 description 1
235000019420 glucose oxidase Nutrition 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
230000006872 improvement Effects 0.000 description 1
238000011081 inoculation Methods 0.000 description 1
239000001573 invertase Substances 0.000 description 1
235000011073 invertase Nutrition 0.000 description 1
239000012948 isocyanate Substances 0.000 description 1
229940116108 lactase Drugs 0.000 description 1
229940039696 lactobacillus Drugs 0.000 description 1
150000002596 lactones Chemical class 0.000 description 1
238000009630 liquid culture Methods 0.000 description 1
238000005259 measurement Methods 0.000 description 1
238000000691 measurement method Methods 0.000 description 1
235000013372 meat Nutrition 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Substances 0.000 description 1
229910000000 metal hydroxide Inorganic materials 0.000 description 1
150000004692 metal hydroxides Chemical class 0.000 description 1
229910044991 metal oxide Inorganic materials 0.000 description 1
150000004706 metal oxides Chemical class 0.000 description 1
CRVGTESFCCXCTH-UHFFFAOYSA-N methyl diethanolamine Chemical compound OCCN(C)CCO CRVGTESFCCXCTH-UHFFFAOYSA-N 0.000 description 1
239000000178 monomer Substances 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
229920001778 nylon Polymers 0.000 description 1
229940049954 penicillin Drugs 0.000 description 1
229920000162 poly(ureaurethane) Polymers 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
229920001281 polyalkylene Polymers 0.000 description 1
229920000768 polyamine Polymers 0.000 description 1
229920000728 polyester Polymers 0.000 description 1
229920001451 polypropylene glycol Polymers 0.000 description 1
229920002223 polystyrene Polymers 0.000 description 1
229920003226 polyurethane urea Polymers 0.000 description 1
239000005373 porous glass Substances 0.000 description 1
230000002062 proliferating effect Effects 0.000 description 1
229940007042 proteus vulgaris Drugs 0.000 description 1
238000011002 quantification Methods 0.000 description 1
238000004445 quantitative analysis Methods 0.000 description 1
238000005956 quaternization reaction Methods 0.000 description 1
229920005989 resin Polymers 0.000 description 1
239000011347 resin Substances 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
238000007127 saponification reaction Methods 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
239000012086 standard solution Substances 0.000 description 1
239000007858 starting material Substances 0.000 description 1
230000001954 sterilising effect Effects 0.000 description 1
238000004659 sterilization and disinfection Methods 0.000 description 1
150000008053 sultones Chemical class 0.000 description 1
230000004083 survival effect Effects 0.000 description 1
229920001059 synthetic polymer Polymers 0.000 description 1
239000013076 target substance Substances 0.000 description 1
125000001302 tertiary amino group Chemical group 0.000 description 1
239000012085 test solution Substances 0.000 description 1
238000004448 titration Methods 0.000 description 1
230000009466 transformation Effects 0.000 description 1
241001446247 uncultured actinomycete Species 0.000 description 1
238000001429 visible spectrum Methods 0.000 description 1
238000005406 washing Methods 0.000 description 1
239000012138 yeast extract Substances 0.000 description 1

Landscapes

Immobilizing And Processing Of Enzymes And Microorganisms (AREA)

JP8887984A 1984-05-01 1984-05-01 ポリウレタンエマルジヨンによる生体触媒類の固定化方法 Granted JPS60232089A (ja)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP8887984A JPS60232089A (ja)	1984-05-01	1984-05-01	ポリウレタンエマルジヨンによる生体触媒類の固定化方法

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP8887984A JPS60232089A (ja)	1984-05-01	1984-05-01	ポリウレタンエマルジヨンによる生体触媒類の固定化方法

Publications (2)

Publication Number	Publication Date
JPS60232089A JPS60232089A (ja)	1985-11-18
JPS645876B2 true JPS645876B2 (de)	1989-02-01

Family

ID=13955285

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP8887984A Granted JPS60232089A (ja)	1984-05-01	1984-05-01	ポリウレタンエマルジヨンによる生体触媒類の固定化方法

Country Status (1)

Country	Link
JP (1)	JPS60232089A (de)

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPH01107849A (ja) *	1987-10-21	1989-04-25	Seiren Co Ltd	生触媒固定化法

1984
- 1984-05-01 JP JP8887984A patent/JPS60232089A/ja active Granted

Also Published As

Publication number	Publication date
JPS60232089A (ja)	1985-11-18

Publication	Publication Date	Title
US4004979A (en)	1977-01-25	Preparation of active proteins cross-linked to inactive proteins
US4266030A (en)	1981-05-05	Macroporous polymeric carrier for covalently binding proteins, its preparation and its use for fixing active proteins
Romaškevič et al.	2006	Application of polyurethane-based materials for immobilization of enzymes and cells: a review
US4237229A (en)	1980-12-02	Immobilization of biological material with polyurethane polymers
US4970156A (en)	1990-11-13	Immobilization of active protein by cross-linking to inactive protein
US3962038A (en)	1976-06-08	Preparation of water-insoluble enzymes
US4195127A (en)	1980-03-25	Process for immobilizing proteins
Hanušová et al.	2013	Development of antimicrobial packaging materials with immobilized glucose oxidase and lysozyme
US4250267A (en)	1981-02-10	Immobilized biological material
US3905923A (en)	1975-09-16	Poly (urea-urethane) foams containing immobilized active enzymes
JPS61254190A (ja)	1986-11-11	酵素を担体に固定する方法
Mori et al.	1973	Enzymatic properties of microcapsules containing asparaginase
Seabra et al.	2007	Cotton gauze bandage: a support for protease immobilization for use in biomedical applications
JPH0716409B2 (ja)	1995-03-01	酵素を固定化する方法
US4371611A (en)	1983-02-01	Enzymatic diagnostic composition
Kokufuta et al.	1986	Immobilization of Paracoccus denitrificans cells with polyelectrolyte complex and denitrifying activity of the immobilized cells
Rejikumar et al.	1998	Preparation and characterization of urease bound on crosslinked poly (vinyl alcohol)
EP0197784A1 (de)	1986-10-15	Verfahren zum Immobilisieren eines biologischen Materials
Shukla et al.	2005	Covalent coupling of peroxidase to a copolymer of acrylamide (AAm)-2-hydroxyethyl methaacrylate (HEMA) and its use in phenol oxidation
JPS60232089A (ja)	1985-11-18	ポリウレタンエマルジヨンによる生体触媒類の固定化方法
Anita et al.	1997	Immobilization of urease using Amberlite MB-1
Baran et al.	1997	Comparison of β‐galactosidase immobilization by entrapment in and adsorption on poly (2‐hydroxyethylmethacrylate) membranes
IE51318B1 (en)	1986-12-10	Immobilized lactase,its preparation and use
CZ169496A3 (en)	1996-09-11	Enzymes fixed on to a carrier
Kacar et al.	2001	Preparation of reversibly immobilized lysozyme onto Procion Green H-E4BD-attached poly (hydroxyethylmethacrylate) film for hydrolysis of bacterial cells