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C-Glucosides, in which sugars are attached to the aglycone by carbon-carbon bonds, are generally resistant to acid and enzyme hydrolysis. The C-glucosyl bond of mangiferin, a xanthone C-glucoside, was cleaved by anaerobic incubation with a human intestinal bacterium, Bacteroides sp. MANG, to give norathyriol. A cell-free extract obtained by sonication of B. sp. MANG demonstrated cleaving activity for mangiferin to norathyriol by adding NADH, diaphorase, and dithiothreitol. Both high molecular weight (&gt;10 k) and low molecular weight (&lt;10 k) fractions obtained from the cell-free extract were required for the activity. MnCl2 was necessary for the activity, but other metal ions were not. By purification of the high molecular weight fraction using DEAE-cellulose and Phenyl Sepharose column chromatography, two fractions, designated as proteins A and B, were separated and required for the activity. Neither protein A nor protein B alone showed any activity. This is the first report describing a C-glucosyl-cleaving enzyme from human intestinal bacterium that seems to involve a novel enzyme mechanism.

Two Proteins, Mn2+, and Low Molecular Cofactor Are Required for C-Glucosyl-Cleavage of Mangiferin