2017 Fiscal Year Final Research Report
Function, structure, and application of extremely halophilic 2-deoxy-D-ribose-5-phosphate aldolase
| Project/Area Number |
15K07395
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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 |
Applied biochemistry
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| Research Institution | Kagawa University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
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) |
2015-04-01 – 2018-03-31
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| Keywords | 高度好塩菌 / アルドラーゼ / 2-デオキシリボース-5-リン酸アルドラーゼ / アーキア / 抗高脂血症剤 |
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| Outline of Final Research Achievements |
2-Deoxy-D-ribose-5-phosphate aldolase (DERA) catalyzes the aldol reaction between two aldehydes and is useful for the production of a variety of stereo-specific materials. However, practical application of the enzyme from a mesophilic organism such as Escherichia coli is still limited by its poor resistance to high aldehyde concentrations. The enzymes from extreme halophilic archaea generally retain considerable activity in organic solvents and this may overcome the problem of DERA utilization. Therefore, we overexpressed the gene encoding DERA from extreme halophilic archaeon in Escherichia coli. The enzyme was highly resistant to a high concentration of acetaldehyde under which E. coli DERA is completely inactivated. The enzyme exhibited much higher activity at ordinary temperature than hyperthermophilic DERAs. Our results suggest that the extremely halophilic DERA has high potential to serve as a biocatalyst in organic syntheses.
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| Free Research Field |
応用生物化学
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