| Project/Area Number |
15K07393
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Okayama University |
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Principal Investigator |
KANZAKI HIROSHI 岡山大学, 環境生命科学研究科, 教授 (60183787)
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| Research Collaborator |
SUGANUMA Shoko 岡山大学, 大学院環境生命科学研究科
KOIDE Mana 岡山大学, 農学部
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2017: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
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| Keywords | 糖質加水分解酵素 / beta-glucosidase / GlcNAcase / 基質特異性 / 基質認識機構 / TMG-chitotriomycin / 糖転移反応 / アスコルビン酸配糖体 / β-glucosidase / ascorbic acid glucoside / PNP-TMG |
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| Outline of Final Research Achievements |
In the case of β-Glucosidase studies, we purified three different pNPG-hydrolyzing enzymes (50kDa, 102kDa, 117kDa) from the enzyme preparation of Penicillium multicolor and found that the 102kDa enzyme exhibited the unique substrate specificity. In the case of GlcNAcase studies, microorganisms assimilating pNP-TMG, an analog of TMG-chitotriomycin, were isolated, and some of them exhibited pNP-TMG- and pNP-GlcNAc-hydrolyzing activities. As pNP-TMG was found to inihibit the known GlcNAcase, elucidation of the substrate recognition mechanism of the enzymes of pNP-TMG-asimilating microorganisms is supposed to be interesting.
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