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Experimental and optimization for kinetic resolution of 1-(4-(trifluoromethyl)phenyl)ethanol enantiomers by lipase-catalyzed transesterification in organic phase

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Abstract

Kinetic resolution of 1-(4-(trifluoromethyl)phenyl)ethanol (TFMP) enantiomers was achieved through lipase-catalyzed transesterification in organic solvents. Lipase PS from Pseudomonas cepacia was selected as the best biological catalyst, and vinyl acetate was used as the acyl donor for the transesterification in isooctane. The effects of temperature, enzyme dosage, substrate ratio and time on the reaction were investigated. Response surface methodology was introduced as the tool for process optimization and the optimized conditions were obtained. The experimental results under the optimized conditions involving the temperature of 46 °C, substrate ratio of 1:12, enzyme dosage of 15 mg and time of 104 min, show that TFMP enantiomers were resolved with the enantiomeric excess of the remaining substrate (ees) higher than 99.0% and the conversion (c) of 50.3%, which indicates an efficient kinetic resolution process.

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Acknowledgements

This work was supported by the National Natural Science Foundation of China (Grant No. 21978077), Postgraduate Scientific Research Innovation Project of Hunan Province (CX20211194).

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  1. Department of Chemistry and Chemical Engineering, Hunan Institute of Science and Technology, Yueyang, 414000, China

    Shuhui Wu, Ying Wu, Bizhu Sun, Panliang Zhang & Kewen Tang

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Wu, S., Wu, Y., Sun, B. et al. Experimental and optimization for kinetic resolution of 1-(4-(trifluoromethyl)phenyl)ethanol enantiomers by lipase-catalyzed transesterification in organic phase. Reac Kinet Mech Cat 136, 183–204 (2023). https://doi.org/10.1007/s11144-022-02339-y

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