| Project/Area Number |
06650910
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
生物・生体工学
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| Research Institution | Shinshu University |
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Principal Investigator |
ARIGA Osamu Shinshu University, Faculty of Textile Science and Technology Research asistant, 繊維学部, 助手 (80168012)
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| Co-Investigator(Kenkyū-buntansha) |
NAGURA Masanobu Shinshu University, Faculty of Textile Science and Technology Professor, 繊維学部, 教授 (70021178)
SANO Yoshiki Shinshu University, Faculty of Textile Science and Technology Professor, 繊維学部, 教授 (80021129)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1995: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1994: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | polyvinyl alcohol / immobilization / biocatalyst / encapsulation / recombinant / protein / メタノール / β-ガラクトシダーゼ / 包括性 |
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| Research Abstract |
The authors investigated optimal preparation conditions of PVA encapsulation and immobilization of biocatalysts. Toluene-permeabilized cells of Escherichia coli having beta-galactosidase was encapsulated in PVA capsule and kinetic properties of the enzyme were determined assuming Michaelis-Menten and competitive inhibition kinetics. The reduction of Vm is due to inactivation of the enzyme. The Km and Ki of the immobilized enzyme were larger than that of the free enzyme. The increases may have been the contribution by PVA in the core of the capsule, because increases in Km and Ki of the free enzyme by addition of PVA into a reaction mixture was observed. Thus, the immobilization of the enzyme reduced the affinity between the enzyme and substrate. The stability of PVA-encapsulated enzyme was considerably affected by the preparation conditions.
The recombinant bacteria were immobilized in PVA capsule and enzyme proteins were produced. This indicates that the proteins can permeate the membrane of a PVA capsule. The productivities of the enzyme were affected by the preparation conditions.
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