Lipase-catalyzed kinetic resolution of 1-(2-Hydroxycyclohexyl)indoles in batch and continuous-flow systems

Péter Falus, Zoltán Boros, Péter Kovács, László Poppe, József Nagy

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The lipase catalyzed kinetic resolution of three trans-1-(2-hydroxycyclohexyl)-indoles in both batch and continuous-flow systems is reported. Ring opening of cyclohexene oxide by the corresponding indole followed by enzymatic acylation with vinyl acetate resulted in novel, highly enantioenriched indole-substituted cyclohexanols and cyclohexyl acetates. The effect of the temperature on enantiomeric ratio (E) and productivity (specific reaction rate, rflow) in the continuous-flow mode acylation was studied at analytical scale in the 0-70 °C range. Preparative scale kinetic resolution of the three indole derivatives was performed in mixed continuous-and recirculation-flow mode resulting in almost complete conversion and good to excellent enantiomeric purity of the products.

Original languageEnglish
Pages (from-to)125-134
Number of pages10
JournalJournal of Flow Chemistry
Volume4
Issue number3
DOIs
Publication statusPublished - Sep 17 2014

Keywords

  • continuous-flow biotransformation
  • enantiomer selectivity
  • heterocyclic secondary alcohol
  • kinetic resolution
  • lipase
  • temperature effect

ASJC Scopus subject areas

  • Chemistry (miscellaneous)
  • Fluid Flow and Transfer Processes
  • Organic Chemistry

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