| Project/Area Number |
23560946
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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 |
Biofunction/Bioprocess
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| Research Institution | Kagawa University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
YABUTANI Tomoki 徳島大学, 大学院ソシオテクノサイエンス研究部, 准教授 (80335786)
OHSHIMA Toshihisa 大阪工業大学, 工学部・生命工学科, 教授 (10093345)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 超好熱菌 / デヒドロゲナーゼ / バイオセンサー / フェニルアラニン / 乳酸 / プロリン / 結晶構造解析 / 耐熱性酵素 / 脱水素酵素 / 色素依存性デヒドロゲナーゼ / Ｘ線結晶構造解析 |
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| Research Abstract |
Many types of dye-linked dehydrogenases(dye-DHs)have been identified in mesophilic microorganisms, and it has been suggested that they have the potential for use as specific elements in biosensors. However, their instability has limited the practical application of mesophilic dye-DHs. On the other hand, hyperthermophiles are known to produce highly stable dye-DHs. Their high stability make them more amenable to practical application. In this study, on the basis of genome information, we observed novel D-phenylalanine dehydrogenase, three types of D-lactate dehydrogenase, and L-proline dehydrogenase (LPDH) in hyperthermophiles. We revealed enzymological properties of these enzymes. Moreover, we succeeded in the crystal structure analysis of LPDH. Finally, we constructed enzyme-immobilized electrodes with hyperthermophilic dye-DHs and confirmed that these electrodes are available for stable biosensors.
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