Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10233432 | Enzyme and Microbial Technology | 2005 | 6 Pages |
Abstract
A thermally stable Klebsiella oxytoca hydrolase was explored as an enantioselective biocatalyst for the hydrolytic resolution of (R,S)-ethyl mandelate in biphasic media. Effects of various process parameters such as solvent type, temperature, pH, product inhibition, enzyme loading and substrate concentration on the enzyme performance were studied, leading to the high enzyme (S)-enantioselectivity of E = 56 at 45 °C for the reaction media consisting of iso-octane and pH 7 buffer. The optimal conditions of pH between 7 and 8, temperature 45 °C and enzyme loading no less than 0.5 mg/ml were proposed for obtaining optically pure (R)-ethyl mandelate remained in the organic phase.
Keywords
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Pei-Yun Wang, Shau-Wei Tsai,