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Flavonoids Biotransformation by Human Gut Bacterium Dorea sp. MRG-IFC3 Cell-Free Extract

  • Huynh Thi Ngoc Mi (Metalloenzyme Research Group and Department of Plant Science and Technology, Chung-Ang University) ;
  • Heji Kim (Metalloenzyme Research Group and Department of Plant Science and Technology, Chung-Ang University) ;
  • Jong Suk Lee (Bio Industry Department, Gyeonggido Business & Science Accelerator (GBSA)) ;
  • Bekir Engin Eser (Department of Biological and Chemical Engineering, Aarhus University) ;
  • Jaehong Han (Metalloenzyme Research Group and Department of Plant Science and Technology, Chung-Ang University)
  • Received : 2024.03.28
  • Accepted : 2024.04.15
  • Published : 2024.06.28

Abstract

Human gut bacterium Dorea sp. MRG-IFC3 is unique in that it is capable of metabolizing puerarin, an isoflavone C-glycoside, whereas it shows broad substrate glycosidase activity for the various flavonoid O-glycosides. To address the question on the substrate specificity, as well as biochemical characteristics, cell-free biotransformation of flavonoid glycosides was performed under various conditions. The results showed that there are two different enzyme systems responsible for the metabolism of flavonoid C-glycosides and O-glycosides in the MRG-IFC3 strain. The system responsible for the conversion of puerarin was inducible and comprised of two enzymes. One enzyme oxidizes puerarin to 3"-oxo-puerarin and the other enzyme converts 3"-oxo-puearin to daidzein. The second enzyme was only active toward 3"-oxo-puerarin. The activity of puerarin conversion to daidzein was enhanced in the presence of Mn2+ and NAD+. It was concluded that the puerarin C-deglycosylation by Dorea sp. MRG-IFC3 possibly adopts the same biochemical mechanism as the strain PUE, a species of Dorea longicatena.

Keywords

Acknowledgement

This research was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (NRF-2021R1A2C2007712).

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