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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Palabras clave de AGROVOC

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

Información bibliográfica

Publicado en

Biotechnology letters

Volumen 33 Edición 10 Paginación 2049 - 2055 ISSN 0141-5492

Editorial

Blackwell Publishing Ltd

Otras materias

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

Idioma

Inglés

Tipo

Journal Article; Text

En AGRIS desde: 2024-02-28

Formato: MODS

Proveedor de Datos

Este registro bibliográfico ha sido proporcionado por National Agricultural Library

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Enlaces

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

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