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Surfactant-modified Aspergillus oryzae lipase as a highly active and enantioselective catalyst for the kinetic resolution of (RS)-1-phenylethanol

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Abstract

The lipase from Aspergillus oryzae was modified with a surfactant and then observed to exhibit high catalytic efficiency and enantioselectivity for the kinetic resolution of (RS)-1-phenylethanol. The influential factors of the modified-lipase preparation were investigated, including the surfactant source, the organic cosolvent, and the buffer pH. The optimum modification conditions were found with a surfactant of polyoxyethylene sorbitan monopalmitate, an organic cosolvent of tetrahydrofuran and a phosphate buffer of pH 7.0. In the transesterification of (RS)-1-phenylethanol with vinyl acetate, the surfactant-modified lipase showed excellent enantioselectivity for the R-isomer (E > 200), giving an enantiomeric excess of higher than 99% for (R)-1-phenylethyl acetate at 46.8% conversion with the reaction time of 2 h at 30 °C. The enzymatic activity had barely altered after 30 days even at 50 °C when it was saved in a powdered state. The results indicated that the modification strategy was useful and highly efficient, and that modified A. oryzae lipase was a promising biocatalyst in the kinetic resolution of (RS)-1-phenylethanol.

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Acknowledgements

This research was supported by the National Key Research and Development Program (no. 2016YFD0400803).

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Authors and Affiliations

  1. College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, 310014, People’s Republic of China

    Hong De Yan, Bing Han Guo, Zhao Wang & Jun Qing Qian

  2. College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310014, People’s Republic of China

    Jun Qing Qian

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  1. Hong De Yan
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  2. Bing Han Guo
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  3. Zhao Wang
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Correspondence to Jun Qing Qian.

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Yan, H.D., Guo, B.H., Wang, Z. et al. Surfactant-modified Aspergillus oryzae lipase as a highly active and enantioselective catalyst for the kinetic resolution of (RS)-1-phenylethanol. 3 Biotech 9, 265 (2019). https://doi.org/10.1007/s13205-019-1796-3

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