Improvement of the thermostability and enzymatic activity of cholesterol oxidase by site-directed mutagenesis
2011
Sun, Yan | Yang, Hailing | Wang, Wu
Site-directed mutagenesis was applied to enhance the thermostability and enzymatic activity of cholesterol oxidase (ChOx) isolated from Brevibacterium sp. Three amino acid residues (Q153E, F128L, and S143H) located near the FAD-binding site of the enzyme were substituted based on structural analysis. The specific activity of the two-sites mutant Q153E/F128L increased by 11.6% and the relative activity increased by 47% when grown for 2 h at 50°C. This mutant is a potential industrial strain for producing ChOx.
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书目信息
Biotechnology letters
卷
33
期
10
页码
2049
- 2055
ISSN
0141-5492
出版者
Blackwell Publishing Ltd
其它主题
Site-directed mutagenesis; Structure-activity relationship; Cholesterol oxidase; Hydrogen-ion concentration; Amino acid sequence; Molecular; Enzyme stability; Site-directed; Molecular sequence data; Hot temperature
语言
英语
类型
Journal Article; Text
2024-02-28
MODS
