Glycyrrhizin .BETA.-D-glucuronidase of Eubacterium sp. from human intestinal flora.

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Abstract
A bacterial strain capable of hydrolyzing glycyrrhizin (GL) to glycyrrhetic acid (GA) was isolated from human feces. This bacterium was identified as Eubacterium sp. The GL-hydrolyzing activity increased in parallel with the growth of this bacterium, which also produced .beta.-D-glucuronidase (EC 3.2.1.31) acting on .beta.-D-glucoronides of phenolic compounds such as phenolphthalein mono-.beta.-D-glucoronide. Gl-hydrolyzing activity was recovered in the supernatant fraction after disruption of this bacterium with a French press and was partially purified by means of ammonium sulfate fractionation, and Sephadex G-200 and octyl-Sepharose column chromatographies. GL-hydrolyzing enzyme was separated from the .beta.-D-glucuronidase which hydrolyzes .beta.-D-glucuronides of phenolic compounds by octyl-Sepharose column chromatography, indicating that the GL-hydrolyzing enzyme is a novel type of .beta.-D-glucuronidase.