1995 Fiscal Year Final Research Report Summary
Structure and function of a novel fungal enzyme, lactonohydrolase, and its application to optical resolution of pantolactone
Project/Area Number |
06453167
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Research Category |
Grant-in-Aid for General Scientific Research (B)
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Allocation Type | Single-year Grants |
Research Field |
応用微生物学・応用生物化学
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Research Institution | KYOTO UNIVERSITY |
Principal Investigator |
SHIMIZU Sakayu Kyoto Univ.Fac.of Agr.Prof., 農学部, 教授 (70093250)
|
Co-Investigator(Kenkyū-buntansha) |
KATAOKA Michihiko Kyoto Univ.Fac.of Agr.Assist., 農学部, 助手 (90252494)
KOBAYASHI Michihiko Kyoto Univ.Fac.of Agr.Lec., 農学部, 講師 (70221976)
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Project Period (FY) |
1994 – 1995
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Keywords | Pantolactone / Optical resolution / Lactonase / Fusarium oxysporum / High-mannose sugarchain |
Research Abstract |
A fungal lactonohydrolase catalyzes the stereospecific hydrolysis of the intramolecular ester bond of D-pantoyl lactone and is useful for optical resolution of racemic pantoyl lactone. High activity of this stereospecific hydrolysis reaction was found in several filamentous fungi belonging to the genera Fusarium, Gibberella and Cylindrocarpon through the screening in a variety of microorganisms. Fusarium oxysporum AKU 3702 showed high productivity of the enzyme and the cells containing the enzyme could be used repeatedly for this hydrolysis reaction. On incubation with the mycelia of this fungus, which had been cultivated in 3% glycerol, 0.5% Polypepton, 0.5% yeast extract and 0.5% corn steep liquor, pH 6.0,46.0% of the recemic pantoyl lactone (700 mg/ml) was hydrolyzed and the optical purity of the pantoic acid formed was 96% enantiomeric excess for the D-isomer.
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Research Products
(10 results)