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PubMed · 17136743

A versatile esterase from Bacillus subtilis: cloning, expression, characterization, and its application in biocatalysis.

Marlen Schmidt·Erik Henke·Birgit Heinze·Robert Kourist·Aurelio Hidalgo·Uwe T Bornscheuer
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Abstract

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.

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AlcoholsAmidohydrolasesAmino Acid SequenceBacillus subtilisBacterial ProteinsCatalysisCloning, MolecularEnzyme StabilityEsterasesGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicHydrogen-Ion ConcentrationKineticsMolecular Sequence DataMolecular StructureMutationSequence Homology, Amino AcidStereoisomerismTemperatureJournal Article

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Marlen Schmidt, Erik Henke, Birgit Heinze, Robert Kourist, Aurelio Hidalgo, Uwe T Bornscheuer. 2007. A versatile esterase from Bacillus subtilis: cloning, expression, characterization, and its application in biocatalysis.. https://doi.org/10.1002/biot.200600174

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