Biological and Pharmaceutical Bulletin
Online ISSN : 1347-5215
Print ISSN : 0918-6158
ISSN-L : 0918-6158
Bacteroides J-37, a Human Intestinal Bacterium, Produces α-Glucuronidase
Dong-Hyun KIMIl-Sung JANGSeung-Won LEE
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1997 Volume 20 Issue 8 Pages 834-837

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Abstract

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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