Schmidt Marlen, Henke Erik, Heinze Birgit, Kourist Robert, Hidalgo Aurelio, Bornscheuer Uwe T
Institute of Biochemistry, Department of Biotechnology and Enzyme Catalysis, Greifswald University, Greifswald, Germany.
Biotechnol J. 2007 Feb;2(2):249-53. doi: 10.1002/biot.200600174.
An esterase from Bacillus subtilis DSM402 (BS2) was cloned and functionally expressed in E. coli. The enzyme is active up to 50 degrees 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.
克隆了来自枯草芽孢杆菌DSM402（BS2）的一种酯酶，并在大肠杆菌中实现了其功能表达。该酶在高达50摄氏度时仍具有活性，以对硝基苯乙酸酯为底物测定其V(max)（1449 mM/分钟）和K(M)值（119 mM）。BS2属于少数能够作用于叔醇的水解酶，因此被用于拆分选定叔醇的外消旋乙酸酯，还用于从肽中选择性去除叔丁酯保护基团。此外，该酶还表现出混杂的酰胺酶活性。
