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Significant enhancement of lipase enantioselectivity toward (S)- Ketoprofen ester at pH 2

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Abstract

The optimal activity of a Candida rugosa lipase (Lipase OF) for hydrolysis of 2-chloroethyl ester of Ketoprofen [2-(3- benzoyphenyl) propionic acid] was at pH 4.0, while the best enantioselectivity (E) was at pH 2.2 where the enzyme was still 60% active and stable.

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Authors and Affiliations

  1. State Key Laboratory of Bioreactor Engineering and Research Institute of Biochemical Engineering, East China University of Science and Technology, Shanghai, 200237, P.R. China

    You-Yan Liu, Jian-He Xu, Qiu-Ge Xu & Ying Hu

Authors
  1. You-Yan Liu
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  2. Jian-He Xu
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  3. Qiu-Ge Xu
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  4. Ying Hu
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Liu, YY., Xu, JH., Xu, QG. et al. Significant enhancement of lipase enantioselectivity toward (S)- Ketoprofen ester at pH 2. Biotechnology Letters 21, 143–146 (1999). https://doi.org/10.1023/A:1005413100578

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  • DOI: https://doi.org/10.1023/A:1005413100578

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