Purification and characterisation of an ester hydrolase from a strain of Arthrobacter species:: Its application in asymmetrisation of 2-benzyl-1,3-propanediol acylates

被引：37

作者：

Johri, S ^{[1
]}

Verma, V ^{[1
]}

Parshad, R ^{[1
]}

Koul, S ^{[1
]}

Taneja, SC ^{[1
]}

Qazi, GN ^{[1
]}

机构：

[1] Reg Res Lab, CSIR, Jammu 180001, India

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 2001年 / 9卷 / 02期

关键词：

D O I：

10.1016/S0968-0896(00)00240-6

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 ester hydrolase (ABL) has been isolated from a strain of Arthrobacter species (RRLJ-1/95) maintained in the culture collection of this laboratory. The purified enzyme has a specific activity of 1700 U/mg protein and is found to be composed of a single subunit (Mr 32,000), exhibiting both lipase and esterase activities shown by hydrolysis of triglycerides and p-nitrophenyl acetate respectively. Potential application of the enzyme concerns the asymmetrisation of prochiral 2-benzyl-1,3-propanediol esters besides enantioselective hydrolysis of alkyl esters of unsubstituted and substituted 1-phenyl ethanols. (C) 2001 Elsevier Science Ltd. All rights reserved.

引用

页码：269 / 273

页数：5

共 30 条

[1] Bacterial lipolytic enzymes: classification and properties [J].