Purification and Characterization of Ginsenoside R_<b1>-Metabolizing β-Glucosidase from Fusobacterium K-60,a Human Intestinal Anaerobic Bacterium

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Fusobacterium K-60,a ginsenoside R_<b1>-metabolizing bacterium, was isolated from human intestinal feces. From this Fusodobacterium K-60,a ginsenoside R_<b1>-metabolizing enzyme, β-glucosidase, has been purified. The enzyme was purified to apparent homogeneity by a combination of butyl-Toyopearl, hydroxyapatite ultragel, Q-Sepharose, and Sephacryl S-300 HR column chromatographies with a final specific activity of 1.52μmol/min/mg. It had optimal activity at pH 7.0 and 40℃. The molecular mass of this purified enzyme was 320 kDa, with 4 identical subunits (80 kDa). The purified enzyme activity was inhibited by Ba^<++>, Fe^<++>, and some agents that modify cysteine residues. This enzyme strongly hydrolyzed sophorose, followed by pnitrophenyl β-D-glucopyranoside, esculin, and ginsenoside R_<b1>. However, this enzyme did not change 20-O-β-D-glucopyranosyl-20(S)-protopanaxadiol (IH-901) to 20(S)-protopanaxadiol, while it weakly changed ginsenoside R_<b1> to IH-901. These findings suggest that the Fusobacterial β-glucosidase is a novel enzyme transforming ginsenoside R_<b1>.
社団法人日本農芸化学会の論文
2001-05-23