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Biocatalytic resolution of Boc-dl-alanine methyl ester by a newly isolated Bacillus amyloliquefaciens WZZ002

Paper ID Volume ID Publish Year Pages File Format Full-Text
49484 46746 2015 4 PDF Available
Title
Biocatalytic resolution of Boc-dl-alanine methyl ester by a newly isolated Bacillus amyloliquefaciens WZZ002
Abstract

•We report the biosynthesis of Boc-d-Ala-OMe by B. amyloliquefaciens WZZ002.•The esterase exhibits excellent enantioselectivity and high substrate tolerance.•The e.e.s and e.e.p are greater than 99% under optimized enzymatic conditions.

A new esterase-producing strain (Bacillus amyloliquefaciens WZZ002) that exhibits high hydrolytic activity, excellent enantioselectivity, and high substrate tolerance on Boc-dl-Alanine methyl ester was isolated from soil samples. The reaction temperature, pH, and neutralizer optima of the cell-mediated biocatalysis were 35 °C, pH 8.0, and NH3·H2O, respectively. The optimal substrate concentration was 2 M, with a biocatalyst loading of 50 g/L. Results showed that the enantiomeric excess values of substrate and product were both greater than 99%. Thus, bioprocessing with the use of the isolated strain is a promising route for the commercial production of Boc-d-Ala-OMe.

Keywords
Esterase; Bacillus amyloliquefaciens; Enantioselective hydrolysis; Biocatalytic resolution; d-Alanine; High substrate loading
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Biocatalytic resolution of Boc-dl-alanine methyl ester by a newly isolated Bacillus amyloliquefaciens WZZ002
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Publisher
Database: Elsevier - ScienceDirect
Journal: Catalysis Communications - Volume 60, 5 February 2015, Pages 134–137
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Catalysis
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