Biological and Pharmaceutical Bulletin p. 834 - 837 (1997)
Update date:2022-08-16
Topics:
Kim, Dong-Hyun
Jang, Il-Sung
Lee, Seung-Won
β-Glucuronidases of mammalian tissues metabolized glycyrrhizin (18β- glycyrrhetinic acid, β-D-glucuronyl α-D-glucuronic acid, GL) to glycyrrhetinic acid (GA) via 18β-glycyrrhetinic acid α-D-glucuronic acid (GAMG); they hydrolyzed β-glucuronic acid conjugates better than α- glucuronic acid conjugates. However, human intestinal bacteria directly metabolized GL to GA, and minorly to GA via GAMG. Bacteroides J-37, isolated from human intestinal bacteria, transformed GL or GAMG to GA, but not baicalin; it produced α-glucuroniase, which hydrolyzed the α-linkage of glucuronic acid conjugates. α-Glucuronidase of Bacteroides J-37 hydrolyzed α-glucuronic acid conjugates better than β-glucuronic acid conjugates. β- Glucuronidase from E. coli, a human intestinal bacterium, hydrolyzed baicalin to baicalein, but did not transform GL.
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