Improvement of the thermostability and enzymatic activity of cholesterol oxidase by site-directed mutagenesis

Sun, Yan; Yang, Hailing; Wang, Wu

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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AGROVOC Keywords

brevibacterium chemistry cholesterol cholesterol enzyme activity enzymology genetics metabolism models mutagenesis mutation sequence alignment thermal stability

Bibliographic information

Published in

Biotechnology letters

Volume 33 Issue 10 Pagination 2049 - 2055 ISSN 0141-5492

Publisher

Blackwell Publishing Ltd

Other Subjects

Site-directed mutagenesis; Structure-activity relationship; Cholesterol oxidase; Hydrogen-ion concentration; Amino acid sequence; Molecular; Enzyme stability; Site-directed; Molecular sequence data; Hot temperature

Language

English

Type

Journal Article; Text

In AGRIS since: 2024-02-28

Format: MODS

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Links

DOI http://dx.doi.org/10.1007/s10529-011-0669-6

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