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Enzymatic Conversion of Flavonoids using Bacterial Chalcone Isomerase and Enoate Reductase
Author(s) -
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 JensMichael,
Krammer Gerhard,
Palm Gottfried J.,
Hinrichs Winfried,
Bornscheuer Uwe T.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201306952
Subject(s) - enzyme , chalcone isomerase , biochemistry , isomerase , escherichia coli , chalcone , chemistry , biotransformation , biology , gene , chalcone synthase , biosynthesis , stereochemistry
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.