Enzymatic conversion of flavonoids using bacterial chalcone isomerase and enoate reductase

Angew Chem Int Ed Engl. 2014 Jan 27;53(5):1439-42. doi: 10.1002/anie.201306952. Epub 2013 Dec 20.

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.

Keywords: Eubacterium ramulus; chalcone isomerase; enoate reductase; enzyme biocatalysis; flavonoids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Biocatalysis
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Eubacterium / enzymology*
  • Eubacterium / genetics
  • Flavanones / chemistry
  • Flavanones / metabolism
  • Flavonoids / chemistry
  • Flavonoids / metabolism*
  • Intramolecular Lyases / genetics
  • Intramolecular Lyases / metabolism*
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Protein Structure, Quaternary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Sequence Analysis, DNA

Substances

  • Bacterial Proteins
  • Flavanones
  • Flavonoids
  • Recombinant Proteins
  • Oxidoreductases
  • Intramolecular Lyases
  • chalcone isomerase