Literature DB >> 24459060

Enzymatic conversion of flavonoids using bacterial chalcone isomerase and enoate reductase.

Mechthild Gall1, Maren Thomsen, Christin Peters, Ioannis V Pavlidis, Patrick Jonczyk, Philipp P Grünert, 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.   

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.
Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

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

Mesh:

Substances:

Year:  2013        PMID: 24459060     DOI: 10.1002/anie.201306952

Source DB:  PubMed          Journal:  Angew Chem Int Ed Engl        ISSN: 1433-7851            Impact factor:   15.336


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