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

Authors
Johri, S Verma, V Parshad, R Koul, S Taneja, SC Qazi, GN
Citation
S. Johri et al., Purification and characterisation of an ester hydrolase from a strain of Arthrobacter species: Its application in asymmetrisation of 2-benzyl-1,3-propanediol acylates, BIO MED CH, 9(2), 2001, pp. 269-273
Citations number
30
Categorie Soggetti
Chemistry & Analysis
Journal title
BIOORGANIC & MEDICINAL CHEMISTRY
ISSN journal
09680896 → ACNP
Volume
9
Issue
2
Year of publication
2001
Pages
269 - 273
Database
ISI
SICI code
0968-0896(200102)9:2<269:PACOAE>2.0.ZU;2-0
Abstract
An ester hydrolase (ABL) has been isolated from a strain of Arthrobacter sp ecies (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 fou nd to be composed of a single subunit (Mr 32,000), exhibiting both lipase a nd esterase activities shown by hydrolysis of triglycerides and p-nitrophen yl acetate respectively. Potential application of the enzyme concerns the a symmetrisation of prochiral 2-benzyl-1,3-propanediol esters besides enantio selective hydrolysis of alkyl esters of unsubstituted and substituted 1-phe nyl ethanols. (C) 2001 Elsevier Science Ltd. All rights reserved.