| Project/Area Number |
24780074
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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 microbiology
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| Research Institution | Ehime University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
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| Keywords | キノプロテイン / グリセロール脱水素酵素 / ピロロキノリンキノン / 酢酸菌 / Gluconobacter / 酸化発酵 / エネルギー代謝 / 呼吸鎖 |
|---|
| Research Abstract |
Quinoprotein glycerol dehydrogenase (GLDH) is a membrane-bound enzyme, which is found in Gluconobacter having attractive industrial applications. In this study, the primary structure of GLDH was compared with other quinoproteins to understand its unique catalytic properties, and then mutant GLDH was prepared in heterologous expression in Gluconobacter.
This study provided the following finding. (i) The propeller structure of PQQ enzyme, especially W1 and W2, are important for GLDH activity. (ii) Heterologous expression system in acetic acid bacteria was constructed to prepare mutant GLDH (iii) GLDH mutants that improved PQQ-binding stability, were prepared by the point mutation based on comparative analysis among PQQ-enzymes. The data will lead to improvement in oxidative fermentation of 5-keto-D-gluconate and others.
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