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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Ключевые слова АГРОВОК

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

Библиографическая информация

Опубликовано в

Biotechnology letters

Том 33 Выпуск 10 Нумерация страниц 2049 - 2055 ISSN 0141-5492

Издатель

Blackwell Publishing Ltd

Другие темы

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

Язык

Английский

Тип

Journal Article; Text

В АГРИСе с: 2024-02-28

Формат: MODS

Поставщик данных

Эту запись предоставил National Agricultural Library

Откройте коллекцию этого поставщика данных в AGRIS

Ссылки

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

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