Enzymatic Conversion of Flavonoids using Bacterial Chalcone Isomerase and Enoate Reductase |
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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 |
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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) |
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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. |
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Keywords: | chalcone isomerase enoate reductase enzyme biocatalysis Eubacterium ramulus flavonoids |
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