| Project/Area Number |
14360054
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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 | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
KATAOKA Michihiko KYOTO UNIVERSITY Grad.Sch.Agriculture, Associate Professor, 農学研究科, 助教授 (90252494)
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| Co-Investigator(Kenkyū-buntansha) |
SAKAMOTO Keiji Daiichi Fine Chemical Co., Researcher, 研究部, 基盤技術開発担当部長(研究職)
OGAWA Jun KYOTO UNIVERSITY Grad.Sch.Agriculture, Assistant Professor, 農学研究科, 助手 (70281102)
SHIMIZU Sakayu KYOTO UNIVERSITY Grad.Sch.Agriculture, Professor, 農学研究科, 教授 (70093250)
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| Project Period (FY) |
2002 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥15,000,000 (Direct Cost: ¥15,000,000)
Fiscal Year 2003: ¥4,200,000 (Direct Cost: ¥4,200,000)
Fiscal Year 2002: ¥10,800,000 (Direct Cost: ¥10,800,000)
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| Keywords | lactonase / lactone / Fusarium oxysporum / Agrobacterium tumefaciens / Optical resolution / Lactone-ring cleaving enzyme / Acinetobacter calcoaceticus / Asymmetric hydrolysis |
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| Research Abstract |
Microbial lactonohydrolases (intramolecular ester bond-hydrolyzing enzymes) with unique properties were found and characterized. The lactonohydrolase from Fusarium oxysporum catalyzes enantioselective hydrolysis of aldonate lactones and D-pantoyl lactone (D-PL). This enzyme is useful for the large-scale optical resolution of racemic PL.. The gene encoding latonohydrolase of F. oxysporum could be overexpressed in Aspergillus oryzae.
The Agrobacterium tumefaciens enzyme catalyzes, asymmetric hydrolysis of PL, but the stereospecificity is opposite to that of the Fusarium enzyme. This enzyme gene also, could be expressed in E. coli transformant cells.
Dihydrocoumarin hydrolase (DCH) from Acinetobacter calcoaceticus is a bifunctional enzyme, which catalyzes not only hydrolysis of aromatic lactones but also bromination of monochlorodirnedon in the presence of H_2O_2 and dihydrocoumarin. DCH also hydrolyzes several linear esters, and is useful for enantioselective hydrolysis of methyl DL-β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate. DCH in vivo detoxified peroxoacids in conjunction with the catalase.
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