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논문 기본 정보

자료유형
학술저널
저자정보
Mi Huynh Thi Ngoc (Metalloenzyme Research Group and Department of Plant Science and Technology, Chung-Ang University, Anseong 17546, Republic of Korea) Kim Heji (Metalloenzyme Research Group and Department of Plant Science and Technology, Chung-Ang University, Anseong 17546, Republic of Korea) Lee Jong Suk (Bio Industry Department, Gyeonggido Business & Science Accelerator (GBSA), Suwon 16229, Republic of Korea) Eser Bekir Engin (Department of Biological and Chemical Engineering, Aarhus University, 8000 Aarhus C, Denmark) Han Jaehong (Metalloenzyme Research Group and Department of Plant Science and Technology, Chung-Ang University, Anseong 17546, Republic of Korea)
저널정보
한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology Vol.34 No.6
발행연도
2024.6
수록면
1,270 - 1,275 (6page)
DOI
10.4014/jmb.2403.03058

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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.
#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

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