Screening of thermophilic aldolases and application for the synthesis of sugar related materials
Project/Area Number |
20560730
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biofunction/Bioprocess
|
Research Institution | Kagawa University |
Principal Investigator |
SAKURABA Haruhiko Kagawa University, 農学部, 教授 (90205823)
|
Co-Investigator(Renkei-kenkyūsha) |
TOSHIHISA Ohshima 九州大学, 大学院・農学研究院, 教授 (10093345)
|
Project Period (FY) |
2008 – 2010
|
Project Status |
Completed (Fiscal Year 2010)
|
Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2010: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2009: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2008: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | 結晶構造解析 / 超好熱菌 / アーキア / 好熱菌 / アルドラーゼ / DERA / キメラ酵素 / PCRスワッピング / eDNA / KDGA / Sulfolobus |
Research Abstract |
The hyperthermophilic 2-deoxy-D-ribose-5-phosphate aldolase (DERA) gene was amplified from environmental DNA by PCR. These fragments were swapped with corresponding sequence of the known hyperthermophilic DERA gene and the expression vector for the chimera enzyme was constructed. The specific activity of the recombinant chimera DERA produced in Escherichia coli was two times higher than that of the wild type enzyme. In addition, we succeeded in determination of the crystal structure of hyperthermophilic 2-keto-3-deoxygluconate aldolases.
|
Report
(4 results)
Research Products
(26 results)