Distinct way to prepare the hyper-stable and stress-tolerant enzymes-halophilic enzyme engineering and hyper-functional cell production
| Project/Area Number |
20580372
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied molecular and cellular biology
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| Research Institution | Kagoshima University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
ISHIBASHI Matsujiro 鹿児島大学, 農学部, 准教授 (20305163)
TOKUNAGA Hiroko 鹿児島大学, 農学部, 技能補佐員 (60381191)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2010: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2008: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | 蛋白質・糖鎖工学 / 極限環境微生物 / 蛋白質発現 / 高機能化 / 好塩性酵素 / 酸性アミノ酸 / 構造可逆性 / 好塩性α-アミラーゼ / 融合蛋白質 / 可溶性 / 封入体 / 大腸菌発現系 |
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| Research Abstract |
The amino acid composition of halophilic enzymes is in general characterized by an abundant content of acidic amino acid leading to high aqueous solubility without aggregation in both native and denatured states and hence allowing efficient renaturation of halophilic proteins after heat or denaturant treatment. The replacement of neutral or basic amino acid residues in non-halophilic proteins with acidic amino acid residues converted non-halophilic to halophilic proteins which show higher aqueous solubility and stability.
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Report
(4 results)
Research Products
(13 results)
