| Project/Area Number |
12680840
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biomedical engineering/Biological material science
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| Research Institution | Osaka Prefecture Unversity |
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Principal Investigator |
FURUTA Masakazu Research Institute for Advanced Sciences and Technology, Research Associate, 先端科学研究所, 助手 (40181458)
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| Co-Investigator(Kenkyū-buntansha) |
OKA Masahito Research Institute for Advanced Sciences and Technology, Associate Professor, 先端科学研究所, 助教授 (70203966)
HAYASHI Toshio Research Institute for Advanced Sciences and Technology, Professor, 先端科学研究所, 教授 (90026089)
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| Project Period (FY) |
2000 – 2001
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2001: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 2000: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | Emulsion polymerization / Poly (amino acid) / Microsphere / Surface Surfactant / Enzyme / Immobilization |
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| Research Abstract |
We investigated the emulsion polymerization of r-benzyl-L-glutamete N-carboxyanhydride, r-methyl-L-glutamete N-carboxyanhydride, and leucine N-carboxyanhydride in mixtures of organic solvents and various surface surfactants under various reaction conditions in order to establish the approbate condition to obtain high molecular weight ploy (α-amino acid) microspheres quantatively. Copolymer microspheres obtained by using polyethylene glycol (MW 200) as surface surfactant and their diameter was within the range of 50-60 micrometers confirmed by electron microscope. As a result of the further examinations changing the composition of monomers and surfactants in the reaction mixture, we succeeded in obtaining the microspheres whose diameter was within the order of 100-200 nm constantly.
Lipase was immobilized onto These microspheres by water-soluble carbodiimid method and to check their capacity to enhance the thermal and storage stabilities of the enzyme after the incubation in water under different PH condition. While the free enzyme lost its activity after several hours under acidic PH, the immobilized enzyme retained 80 % of the initial activity under the same condition. The immobilized enzyme also displayed considerable thermal stability retaining 20 % of the initial activity even under 80ーC. Any activity loss was not observed at extremely high PH. These results suggested that the change of the conformation of the enzyme by storage, heating, and change of pH could be inhibited by immobilization and that the microsphere may function as a barrier against the deterioration by microorganisms and other factors.
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