2021 Fiscal Year Final Research Report
Single molecule analysis of carbohydrate degrading enzyme with double binding domains form marine bacterium
Project/Area Number |
19H03094
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Review Section |
Basic Section 41050:Environmental agriculture-related
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Research Institution | Shizuoka University |
Principal Investigator |
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Project Period (FY) |
2019-04-01 – 2022-03-31
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Keywords | キチン加水分解酵素 / ビブリオ菌 / 1分子計測 / 糖質吸着ドメイン |
Outline of Final Research Achievements |
Chitinases from marine bacteria have an additional adsorption domain on the C-terminal side of enzymes from terrestrial bacteria. Comparison of the biochemical activities of the full-length Vibrio chitinase and a mutant enzyme with the additional domain removed showed that the full-length enzyme has a high affinity for chitin. The full-length enzyme adsorbed on chitin for a very long time, while the binding rate constants of the two enzymes were similar. The long adsorption on chitin with two adsorption domains may prevent dissociation and diffusion of the enzyme, which may be advantageous for reactions in the ocean.
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Free Research Field |
生物物理学
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Academic Significance and Societal Importance of the Research Achievements |
海中には大量の微細甲殻類が生息しており、その殻としてキチンの年間生産量は14億トンと推計されている。この大量のキチンは海洋性バクテリアによって分解され、海洋中での炭素循環が成り立っている。本研究で海洋中バクテリアに特異的なキチン分解酵素はキチンに吸着する部位を1つ多く持つことで、海洋中でもキチンから離れにくくなり効率的な分解が行えることを明らかにした。この海洋環境での結晶キチン分解システムは、薄い基質濃度化での固体バイオマス分解や海洋環境中に散らばっている微細プラスチック片の分解除去に有用な知見となる。
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