| Project/Area Number |
25870271
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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 |
Applied biochemistry
Biofunction/Bioprocess
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| Research Institution | University of Fukui |
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Principal Investigator |
Satomura Takenori 福井大学, 工学(系)研究科(研究院), 准教授 (50412317)
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| Research Collaborator |
SAKURABA HARUHIKO 香川大学, 農学部, 教授 (90205823)
OHSHIMA TOSHIHISA 大阪工業大学, 工学部, 教授 (10093345)
SUYE SHIN-ICHIRO 福井大学, 大学院工学研究科, 教授 (90206376)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | D-アミノ酸 / 色素依存性脱水素酵素 / 好熱菌 / ヒドロキシプロリン代謝 / 色素依存性D-アミノ酸脱水素酵素 / バイオセンサ / D-フェニルアラニン脱水素酵素 |
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| Outline of Final Research Achievements |
The novel dye-lined D-amino acid dehydrogenase was found in thermophilic bacterium, Rhodothermus marinus. The primary structure of the enzyme was largely different from that of mesophilic dye-linked D-amino acid dehydrogenases so far reported. The dye-linked D-amino acid dehydrogenase was overexpressed in Escherichia coli, and its product was purified and characterized. When enzyme-catalyzed dehydrogenation of several D-amino acids was carried out using 2,6-dichloroindophenol as the electron acceptor, D-phenylalanine was the most preferable substrate among the D-amino acids tested. In addition, the enzyme was stable over a wide range of pH and did not also lose its activity by incubating 70 degrees C for 10 min. Thus, the highly thermostable dye-linked D-amino acid dehydrogenase exhibits a high potential usefulness for application to the D-amino acid bio-sensor.
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