| Project/Area Number |
07555245
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 試験 |
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| Research Field |
反応・分離工学
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| Research Institution | KYUSHU UNIVERSITY |
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Principal Investigator |
NAKASHIO Fumiyuki Kyushu Univ., Chem. Sci & Technolo., Professor, 工学部, 教授 (70037729)
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| Co-Investigator(Kenkyū-buntansha) |
TSUBOI Hirotada MITSUI CTTEC,Ltd., Mobara Research & Development, Director, 技術研究所, 所長
KAKOI Takahiko Kyushu Univ., Chem. Sci & Technolo., Research Associate, 工学部, 助手 (20233679)
GOTO Masahiro Kyushu Univ., Chem. Sci & Technolo., Associated Professor, 工学部, 助教授 (10211921)
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| Project Period (FY) |
1995 – 1996
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| Project Status |
Completed (Fiscal Year 1996)
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| Budget Amount *help |
¥7,200,000 (Direct Cost: ¥7,200,000)
Fiscal Year 1996: ¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1995: ¥5,100,000 (Direct Cost: ¥5,100,000)
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| Keywords | Enzyme / Surfactant / Lipase / Esterification / Peptide / Organic solvent / Biotechnology / Biocatalyst / 酵素 / バイオテクノロジー / ペプチド合成 / 生物工学 / 光学分割 / キモトリプシン / 分離 / 重合 / 分子刷り込み |
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| Research Abstract |
The utility of enxymes in organic media has attracted much interest during the last ten years due to some remarkable novel properties compared to those in water. Biocatalyst engineering has been used successfully to improve biocatalysis in organic media and obtaining stable biocatalysts is a main target of biotechnology. Enzymes in nonaqueous solvents can catalyze a synthesis reaction of hydrophobic compounds such as esterification, steroid conversions and peptide formation. The substrate specificity and reactivity in an enzyme conversion are extremely high compared with those of conventional chemical synthesis. Thus an application of enzymatic reaction has been expected to produce optically active materials with an industrial scale.
However, in order to take full advantage of the biocatalysis in organic media, it is necessary to modify the enzyme to be soluble in an organic solvent from the viewpoint of reduced diffusional limitations of substrates and increase in the reaction rate. Al
… More
though using a powder enzyme in a suspension state is simple, the reaction rate is usually very low due to the heterogeneity and several days are required to attain a high reaction yield. In this study, a novel preparation method for surfactant-enzyme complexes has been developed utilizing water-in-oil emulsions. Preparation conditions to obtain a suitable surfactant-lipase complex were investigated. Using the surfactant-lipase complexes, the estarification of benzyl alcohol with lauric acid was conducted in organic solvents. The enzymatic activity of lipase in a hydrophobic organic solvent was significantly enhanced by entrapping in a surfactant matrix. The surfactant-lipase complex catalyzed the esterification effect ively in organic media. The esterification rate from the surfactant-lipase complex was much higher than that from the powder lipase. The activity of the lipase complex strongly depends on the entrapping surfactant and the aqueous pH in the preparation. The surfactant-lipase complexes were thermostable at high temperature compared to the native lipase. Furthermore, the lipase complex showed a high storage stability. This modification method will enable us to utilize a lot of enzymes as new biocatalysts which had not shown enzymatic activity in organic media. Less
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