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Enzymatic Conversion of Flavonoids using Bacterial ChalconeIsomerase and Enoate Reductase

  • Mechthild Gall
  • , Maren Thomsen
  • , Christin Peters
  • , Ioannis V. Pavlidis
  • , Patrick Jonczyk
  • , Philipp P. Grunert
  • , Sascha Beutel
  • , Thomas Scheper
  • , Egon Gross
  • , Michael Backes
  • , Torsten Geißler
  • , Jakob P. Ley
  • , Jens Michael Hilmer
  • , Gerhard Krammer
  • , Gottfried J. Palm
  • , Winfried Hinrichs
  • , Uwe T. Bornscheuer*
  • *Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer review

Abstract

Flavonoids are a large group of plant secondary metabolites with a variety of biological properties and are therefore of interest to many scientists, as they can lead to industrially interesting intermediates. The anaerobic gut bacterium Eubacterium ramulus can catabolize flavonoids, but until now, the pathway has not been experimentally confirmed. In the present work, a chalcone isomerase (CHI) and an enoate reductase (ERED) could be identified through whole genome sequencing and gene motif search. These two enzymes were successfully cloned and expressed in Escherichia coli in their active form, even under aerobic conditions. The catabolic pathway of E. ramulus was confirmed by biotransformations of flavanones into dihydrochalcones. The engineered E. coli strain that expresses both enzymes was used for the conversion of several flavanones, underlining the applicability of this biocatalytic cascade reaction.

Translated title of the contributionEnzymatische Umsetzung von Flavonoiden mit einer bakteriellen Chalconisomerase und einer Enoatreduktase
Original languageEnglish
Pages (from-to)1439-1442
Number of pages4
JournalAngewandte Chemie
Volume53
Issue number5
DOIs
Publication statusPublished - 20 Dec 2013

Keywords

  • Chalcone isomerase
  • Enoate reductase
  • Enzyme biocatalysis
  • Eubacterium ramulus
  • Flavonoids

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry

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