Lipase-catalyzed Kinetic Resolution of 3-hydroxy Esters: Optimization, Batch, and Continuous Reactions

Research output: Contribution to journalArticleResearchpeer review

Authors

  • U. Bornscheuer
  • A. Herar
  • A. Capewell
  • V. Wendel
  • L. Kreye
  • T. Scheper
  • E. Voss
  • K. Wünsche
  • H. H. Meyer

External Research Organisations

  • Nagoya University
  • University of Stuttgart
  • University of Münster
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Details

Original languageEnglish
Pages (from-to)215-221
Number of pages7
JournalAnnals of the New York Academy of Sciences
Volume750
Issue number1
Publication statusPublished - Mar 1995
Externally publishedYes

Abstract

The results show that enzyme-catalyzed kinetic resolutions represent an effective method for the synthesis of enantiomerically pure compounds. Continuous enzyme reactors are especially important for industrial applications. Supercritical fluids offer the advantage of easier downstream processing.

ASJC Scopus subject areas

Cite this

Lipase-catalyzed Kinetic Resolution of 3-hydroxy Esters: Optimization, Batch, and Continuous Reactions. / Bornscheuer, U.; Herar, A.; Capewell, A. et al.
In: Annals of the New York Academy of Sciences, Vol. 750, No. 1, 03.1995, p. 215-221.

Research output: Contribution to journalArticleResearchpeer review

Bornscheuer U, Herar A, Capewell A, Wendel V, Kreye L, Scheper T et al. Lipase-catalyzed Kinetic Resolution of 3-hydroxy Esters: Optimization, Batch, and Continuous Reactions. Annals of the New York Academy of Sciences. 1995 Mar;750(1):215-221. doi: 10.1111/j.1749-6632.1995.tb19954.x
Bornscheuer, U. ; Herar, A. ; Capewell, A. et al. / Lipase-catalyzed Kinetic Resolution of 3-hydroxy Esters: Optimization, Batch, and Continuous Reactions. In: Annals of the New York Academy of Sciences. 1995 ; Vol. 750, No. 1. pp. 215-221.
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