Esterase EstK from Pseudomonas putida mt-2: An enantioselective acetylesterase with activity for deacetylation of xylan and poly(vinylacetate)

被引：8

作者：

Millar, Robert ^{[1
]}

Rahmanpour, Rahman ^{[1
]}

Yuan, Eugenie Wei Jia ^{[1
]}

White, Catharine ^{[1
]}

Bugg, Timothy D. H. ^{[1
]}

机构：

[1] Univ Warwick, Dept Chem, Coventry CV4 7AL, W Midlands, England

来源：

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY | 2017年 / 64卷 / 06期

基金：

英国生物技术与生命科学研究理事会;

关键词：

esterase; poly(vinylacetate); Pseudomonas putida mt-2; xylan esterase; RHODOCOCCUS-JOSTII RHA1; BIOCHEMICAL-CHARACTERIZATION; EXTRACELLULAR ESTERASE; ALPHA/BETA-HYDROLASE; FERULOYL ESTERASES; ASPERGILLUS-NIGER; PURIFICATION; LIGNIN; CARBOXYLESTERASE; CLASSIFICATION;

D O I：

10.1002/bab.1536

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An extracellular esterase gene estK was identified in Pseudomonas putida mt-2 and overexpressed at high levels in Escherichia coli. The recombinant EstK enzyme was purified and characterized kinetically against p-nitrophenyl ester and other aryl-alkyl ester substrates and found to be selective for hydrolysis of acetyl ester substrates with high activity for p-nitrophenyl acetate (k(cat) 5.5 Sec(-1), K-M 285 mu M). Recombinant EstK was found to catalyze deacetylation of acetylated beech xylan, indicating a possible in vivo function for this enzyme, and partial deacetylation of a synthetic polymer (poly(vinylacetate)). EstK was found to catalyze enantioselective hydrolysis of racemic 1-phenylethyl acetate, generating 1R-phenylethanol with an enantiomeric excess of 80.4%. (C) 2016 International Union of Biochemistry and Molecular Biology, Inc.

引用

页码：803 / 809

页数：7