| Project/Area Number |
15K07355
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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 microbiology
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| Research Institution | Niigata University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
IGARASHI Kiyohiko 東京大学, 大学院農学生命科学研究科, 准教授 (80345181)
SUZUKI Kazushi 新潟大学, 自然科学系, 准教授 (00444183)
SUGIMOTO Hayuki 新潟大学, 自然科学系, 准教授 (60529527)
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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 |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 微生物酵素 / キチナーゼ / CBP21 / AA10タンパク質 / キチン分解細菌 / Searratia marcescens / 結晶性キチン / 高速原子間力顕微鏡 |
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| Outline of Final Research Achievements |
The ultimate goal of this research is proposition of the universal and evolved model of the mechanism for crystalline chitin degradation and utilization by chitinolytic bacteria. Therefore, "the role of the protein (CBP21) that promote degradation of crystalline chitin", "the importance of CBP21 for the biological and ecological function of the chitinolytic bacteria", "the mechanism for biodegradation of α-chitin that exists in nature more abundantly" were studied. As a results, it became clear that CBP21 is especially important for degradation and utilization of chitin close to natural condition, an amino acid residue with aromatic ring of big resonating structure at the entrance of the catalytic cleft of chitinase is very important for hydrolysis of highly crystalline chitin substrate, and that one chitinase molecule jump to another chitin chain in different orientation and begins hydrolysis in opposite direction.
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