Enzymatic Conversion of Flavonoids using Bacterial Chalcone Isomerase and Enoate Reductase1. Issue 5 (20th December 2013)

• Record Type: Journal Article
• Authors: Gall, Mechthild; Thomsen, Maren; Peters, Christin; Pavlidis, Ioannis V.; Jonczyk, Patrick; Grünert, Philipp P.; Beutel, Sascha; Scheper, Thomas; Gross, Egon; Backes, Michael; Geißler, Torsten; Ley, Jakob P.; Hilmer, Jens‐Michael; Krammer, Gerhard; Palm, Gottfried J.; Hinrichs, Winfried; Bornscheuer, Uwe T.
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 5(2014)
• Page Start: 1439
• Page End: 1442
• Publication Date: 2013-12-20
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201306952
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>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 <italic>Eubacterium ramulus</italic> 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 <italic>Escherichia coli</italic> in their active form, even under aerobic conditions. The catabolic pathway of <italic>E. ramulus</italic> was confirmed by biotransformations of flavanones into dihydrochalcones. The engineered <italic>E. coli</italic> strain that expresses both enzymes was used for the conversion of several flavanones, underlining the applicability of this biocatalytic cascade reaction.</p> </abstract>