| Project/Area Number |
07660120
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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 |
応用微生物学・応用生物化学
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| Research Institution | Faculty of Literature and Home Science, Wayo Women's University |
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Principal Investigator |
OHNO Nobuko Faculty of Literature and Home Science, Wayo Women's University, Professor, 文家政学部, 教授 (80213817)
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| Co-Investigator(Kenkyū-buntansha) |
FUJII Takaaki Faculty of Horticulture, Chiba University, Professor, 園芸学部, 教授 (50125952)
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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 |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1996: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1995: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | alpha-amylase / beta-xylosidase / glucoamylase / glycerol / inositol / oleic acid / dimorphism / キシラン / キシラナーゼ |
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| Research Abstract |
1. Morphological changes and intracellular structures of Fusidium sp. BX-1 were examined with cells grown on various carbon and nitrogen sources. Cells grown on glycerol, glucose and starch showed a yeast-like form. Strain BX-1 showed a peculiar change from a large peanut-like cell to a short and thick hypha when the organism was incubated in a inositol medium. Cells grown on oleic acid and olive oil showed short mycelial forms. Only typical yeast like cells were observed in the media containing potassium nitrate in spite of carbon sources. A lot of mitochondria and fatty granules were observed in cells grown on these carbon sources.
2. The production of beta-xylosidase by strain BX-1 was remarkably enhanced in a medium containing 0.5% glycerol and 3.0% washed wheat bran. From this culture, the enzyme was purified as an electrophoretically homogeneous protein. Its molecular weigth was estimated about 120,000. The optimum pH for its activity was 3-4. The optimum temperature was 65ﾟC.The activity was enhanced 1.5-1.8 times by incubating with 50-60% ethanol.
3. The N-terminal amino acid sequences of alpha-amylase (alpha-AMY) and glucoamylase (G-AMY) from strain BX-1 were compared with enzymes from various microorganisms. alpha-AMY and G-AMY of strain BX-1 were found to have 60-70% homology with enzymes of Aspergillus species and Saccharomyces species.
An incrase of antaibody titers for alpha-AMY was about 8 times higher than that of G-AMY.Antibodies against alpha-AMY and G-AMY were purified from antiserums provided by the immunization of rats.
mRNAs were extracted from cells of strain BX-1 producing amylases in a glycerol medium.
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