Abstract
Objective
To identify an esterase-mediated kinetic resolution of secondary alcohols in non-aqueous medium.
Results
An esterase, EST4, from a marine mud metagenomic library, showed high activity and enantioselectivity for the kinetic resolution of secondary alcohols in non-aqueous medium. Using 1-phenylethanol as the model alcohol, the effects of organic solvents, acyl donors, molar ratio, temperatures and biocatalyst loading on the kinetic resolution catalyzed by the EST4 whole-cell biocatalyst were investigated and optimized. The optimized methodology was effective on resolving 16 various racemic secondary alcohols in neat n-hexane, providing excellent enantiomeric excess (up to 99.9 % ee). Moreover, EST4 exhibited a strong tolerance for high substrate concentration (up to 1 M), and the optical purity of the desired secondary alcohols was kept above 99 % ee.
Conclusion
The esterase EST4 is a promising biocatalyst for the enantioselective synthesis of various alcohols and esters with interesting practical applications.
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Acknowledgments
This work was supported by the National Natural Science Foundation of China (No. 21406068/B060804), the Fundamental Research Funds for the Central Universities, and National Basic Research Program of China (No. 2012CB721103).
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Gao, W., Fan, H., Chen, L. et al. Efficient kinetic resolution of secondary alcohols using an organic solvent-tolerant esterase in non-aqueous medium. Biotechnol Lett 38, 1165–1171 (2016). https://doi.org/10.1007/s10529-016-2091-6
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DOI: https://doi.org/10.1007/s10529-016-2091-6