Analysis of catalytic mechanism and activation of a highly stable cholesterol oxidase
Project/Area Number |
24580127
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Applied microbiology
|
Research Institution | Toyo University |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
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Keywords | コレステロール / コレステロールオキシダーゼ / 臨床検査 / Chromobacterium |
Outline of Final Research Achievements |
High cholesterol levels are strongly associated with cardiovascular disease because these promote atheroma development in arteries. Cholesterol oxidase is useful for enzymatic determination of cholesterol levels in human blood. We previously discovered a thermal, organic solvent and detergent-tolerant cholesterol oxidase from a gram-negative bacterium Chromobacterium sp. DS-1. In addition, it was found that several amino acid residues near the FAD cofactor probably play an important role in the reactivity and the stability of the enzyme. Therefore, we constructed mutant enzymes which had mutated amino acid residues near the FAD cofactor by site directed mutagenesis, to identify amino acid residues that play an important role in activity and stability. In this study, we constructed a mutant enzyme which is relatively stable at high temperature and in the presence of detergents.
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Report
(4 results)
Research Products
(5 results)