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

• 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.