| Project/Area Number |
17K17740
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
Applied biochemistry
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| Research Institution | Niigata University |
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Principal Investigator |
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| Project Period (FY) |
2017-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2019: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2018: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2017: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 連続分解 / キチナーゼ / サブサイト / 芳香族アミノ酸 / 酵素 / 作動機構 |
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| Outline of Final Research Achievements |
Several subsites for substrate binding are lined in the catalytic domain of a processive-type chitinase, BcChiA1. The individual roles of these subsites during the processive hydrolysis reaction remain unknown. Direct kinetic comparisons of the mutants which the amino acid residue at each subsite was substituted were performed, aiming to characterize each subsite. Effects of the mutation at the subsites on the kinetic parameters for the hydrolysis of crystalline beta-chitin differed depending on the location of the subsite in the catalytic domain. It was suggested that for the processive hydrolysis of a substrate, the subsite at the exit of the catalytic domain is more important than that at the entrance.
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| Academic Significance and Societal Importance of the Research Achievements |
本研究では，連続反応性をもち，触媒効率のよい連続分解型キチナーゼのサブサイト（基質と結合する部位）に着目して解析を行い，どのようにして連続的に反応を行うことができるのか，その作動機構の一端を明らかにした。これらの知見は，触媒効率向上のための酵素分子デザインの基盤となる。また，研究対象としたキチナーゼは，結晶性多糖バイオマスのリファイナリーや利活用において欠くことのできない産業用酵素の候補である。結晶性多糖バイオマス資源の酵素分解法の開発に本研究成果を応用することで，環境への負荷の少ない分解・利活用法を確立し，カーボンニュートラル社会の実現の一助として貢献できる
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