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Enzymatic Conversion of Flavonoids using Bacterial Chalcone Isomerase and Enoate Reductase
Authors:Dipl‐Biol Mechthild Gall  Dipl‐Biochem Maren Thomsen  Dipl‐Biochem Christin Peters  Dr Ioannis V Pavlidis  M?Sc Patrick Jonczyk  M?Sc Philipp P Grünert  Dr Sascha Beutel  Prof?Dr Thomas Scheper  Egon Gross  Dr Michael Backes  Dr Torsten Geißler  Dr Jakob P Ley  Dr Jens‐Michael Hilmer  Dr Gerhard Krammer  Dr Gottfried J Palm  Prof?Dr Winfried Hinrichs  Prof?Dr Uwe T Bornscheuer
Affiliation:1. Institute of Biochemistry, Department of Biotechnology & Enzyme Catalysis, Greifswald University, Felix‐Hausdorff‐Strasse 4, 17487 Greifswald (Germany) http://biotech.uni‐greifswald.de;2. Institute of Biochemistry, Department of Structural Biology, Greifswald University, Felix‐Hausdorff‐Strasse 4, 17487 Greifswald (Germany);3. Institute of Technical Chemistry, Gottfried Wilhelm Leibniz University of Hannover, Callinstrasse 5, 30167 Hannover (Germany);4. Symrise, P.O. Box 1253, 37603 Holzminden (Germany)
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:chalcone isomerase  enoate reductase  enzyme biocatalysis  Eubacterium ramulus  flavonoids
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