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The intestinal microflora of humans is an extraordinarily complex mixture of microorganisms, the majority of which are anaerobic bacteria. Amongst them, most prevalent bacteria are Bacteroides, Eubacterium, Peptococcus, Bifidobacteria. We isolated a Bacteroides fragilis strain from a Korean adult and examined various glycosidase activities of this strain. The activities of N-acetyl-β-glucosaminidase, afucosidase, β-glucuronidase, chitobiase and PNPCase were stronger in Bacteroides fragilis Roid 8 than in other intestinal anaerobic bacteria. N-acetyl-β-glucosaminidase was strongest, followed by α-fucosidase, β-glucuronidase and PNPCase. The activities of a galactosidase, β-xylosidase, α-arabinofuranosidase were not present or very low. The activities of α-glucosidase, β-glucosidase and α-galactosidase were present but at a lower level than in Bifidobacterium. The effect of the carbon sources on the production of N-acetyl-β-glucosaminidase, α-fucosidase, β-glucuronidase and PNPCase of Bacteroides fragilis Roid 8 was investigated. .actose and glucose lowered the production of the varous glycosidase enzymes studied in this work. In addition, we investigated the optimum temperature and pH of each glycosidase from Bacteroides fragilis Roid-8 using crude enzyme preparations.
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