Deglycosylation of the Isoflavone C -Glucoside Puerarin by a Combination of Two Recombinant Bacterial Enzymes and 3-Oxo-Glucose

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.