Enzymic Studies on the Animal and Intestinal Bacterial Metabolism of Geniposide.

Abstract

Geniposide, a main iridoid glucoside of Gardenia fruit, is transformed to genipin, a genuine choleretic, in vivo in rats (Aburada et al., J. Pharmacobio-Dyn., 1, 81 (1978)). As geniposide was not hydrolyzed to any metabolite by rat liver homogenate, which has beta-D-glucosidase and esterase activities, beta-D-glucosidases in intestinal bacteria seem to be required for an exhibition of its choleretic action. The crude extract of Eubacterium sp. A-44, a human intestinal anaerobe, hydrolyzed geniposide, but that of Ruminococcus sp. PO1-3, another human anaerobe, did not, though both extracts had beta-D-glucosidase activities for p-nitrophenyl beta-D-glucopyranoside. Only one of three beta-D-glucosidases from E. sp. A-44 and none of two from R. sp. PO1-3 hydrolyzed geniposide to genipin. However, carboxylesterases from E. sp. A-44 and pig liver were unable to hydrolyze geniposide to geniposidic acid, but hydrolyzed genipin to an aglycone of geniposidic acid, indicating that geniposide is first hydrolyzed to genipin by beta-D-glucosidases and subsequently to the aglycone of geniposidic acid by esterases. Thus, when geniposide is orally administered, genipin seems to be effectively produced in the intestine and then absorbed to act as a genuine choleretic.