• DOI:10.1016/J.MOLCATB.2013.11.008
Corpus ID: 84622516

Improving the enantioselectivity of an esterase toward (S)-ketoprofen ethyl ester through protein engineering

@article{Yoon2014ImprovingTE,
  title={Improving the enantioselectivity of an esterase toward (S)-ketoprofen ethyl ester through protein engineering},
  author={Sangyoung Yoon and S. Kim and Songyi Park and Eunsoo Hong and Jinyeong Kim and Sangchul Kim and T. Yoo and Y. Ryu},
  journal={Journal of Molecular Catalysis B-enzymatic},
  year={2014},
  volume={100},
  pages={25-31}
}

Sangyoung Yoon, S. Kim, +5 authors Y. Ryu

Published 2014

Chemistry

Journal of Molecular Catalysis B-enzymatic

Abstract Esterases, enzymes that hydrolyze ester bonds, have been utilized to synthesize optically pure compounds like (S)-ketoprofen, which can be produced by the esterase-catalyzed hydrolysis of rac -ketoprofen ethyl ester. We previously reported a novel esterase, Est25, which was expressed in active form in Escherichia coli , and showed high hydrolyzing activities for various substrates. However, the enzyme did not show any preference for either of rac -ketoprofen ethyl ester. In this study… CONTINUE READING

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