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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Mots clés AGROVOC

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

Informations bibliographiques

Publié dans

Biotechnology letters

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

Editeur

Blackwell Publishing Ltd

D'autres materias

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

Langue

anglais

Type

Text; Journal Article

Sur AGRIS depuis: 2024-02-28

Format: MODS

Fournisseur de données

Cette notice bibliographique a été fournie par National Agricultural Library

Découvrez la collection de ce fournisseur de données dans AGRIS

Liens

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

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