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A versatile esterase from Bacillus subtilis : Cloning, expression, characterization, and its application in biocatalysis
Author(s) -
Schmidt Marlen,
Henke Erik,
Heinze Birgit,
Kourist Robert,
Hidalgo Aurelio,
Bornscheuer Uwe T.
Publication year - 2007
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.200600174
Subject(s) - bacillus subtilis , esterase , biocatalysis , enzyme , amidase , chemistry , cloning (programming) , substrate (aquarium) , stereochemistry , biochemistry , biology , bacteria , catalysis , reaction mechanism , ecology , genetics , computer science , programming language
An esterase from Bacillus subtilis DSM402 (BS2) was cloned and functionally expressed in E. coli. The enzyme is active up to 50°C, and the V max (1449 mM/min) and K M values (119 mM) were determined using p ‐nitrophenyl acetate as substrate. BS2 belongs to the few hydrolases that can act on tertiary alcohols and was therefore used to resolve racemic acetates of selected tertiary alcohols, but also to selectively remove the tert ‐butyl ester protecting group from peptides. In addition, the enzyme shows promiscuous amidase activity.