Deglycosylation of the Isoflavone <i>C</i> -Glucoside Puerarin by a Combination of Two Recombinant Bacterial Enzymes and 3-Oxo-Glucose
Kenichi Nakamura, Shu Zhu, Katsuko Komatsu, Masao Hattori, Makoto Iwashima
Abstract
One important role of the gut microbiota is to metabolize dietary nutrients and supplements such as flavonoid glycosides. Ingested glycosides are metabolized by intestinal bacteria to more-absorbable aglycones and further degradation products that show beneficial effects in humans. Although numerous glycoside hydrolases that catalyze O -deglycosylation have been reported, enzymes responsible for C -deglycosylation are still limited. In this study, we characterized enzymes involved in the C -deglycosylation of puerarin from a human intestinal bacterium, PUE. Here, we report the purification and characterization of a recombinant oxidoreductase involved in C -glucoside degradation. This study provides new insights for the elucidation of mechanisms of enzymatic C -deglycosylation.