Studies on characterization and applications of carboxylesterases from hyperthermophiles

China Biotechnology

2008, Vol. 28

Issue (3): 118-122 DOI:

Studies on characterization and applications of carboxylesterases from hyperthermophiles

Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO

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Abstract

Abstract This review focuses on the carboxylestereases from hyperthermophiles. Most of them are similar with the hormone-sensitive lipase (HSL) family in structure. Both the carboxylestereases and HSL belong to α/β hydrolase. And their structures become more compact and tenacious compared with mesophilic esterases. This special structure enhances their thermostability. The review introduces the effects of temperature and organic solvents on the catalytic efficiency and enantioselectivity of the carboxylesterases. Generally the optimum substrate of the enzyme is medium chain p-nitrophenyl，and the presence of a GGGX motif in these carboxylesterases suggest the enzyme has the ability to hydrolyze tertiary alcohol esters. Because of their characteristic, the carboxylesterases could be used in various aspects，especially in separation of racemic ester.

Key words： hyperthermophile carboxylesterase structural characteristic protein thermostability application

Received: 14 November 2007 Published: 28 March 2008

Corresponding Authors: Mi SUN

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	Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO
	Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO
	Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO
	Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO
	Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO

Cite this article:

Yao-Jun WANG Gao Qiang Mi SUN Jian-Hua HAO . Studies on characterization and applications of carboxylesterases from hyperthermophiles. China Biotechnology, 2008, 28(3): 118-122.

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https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2008/V28/I3/118

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