Abstract
Crude enzymes (En(C)) which hydrolyze insoluble glucan produced by Streptococcus mutans FA-1 were extracted from Bacteroides oralis obtained from human dental plaque. Extracellular insoluble glucan of S. mutans (IsG) and the one which was partially modified by Smith degradation (M-IsG) were used as substrates. Commercial dextran (M.W. 2,000,000) was used as control. Composition of the types of glucosidic linkages of the glucans was determined by methylation analysis. The ratio of the α-(1-6) linkage and α-(1-3) linkage was 96.3% and 0.5% for dextran, 29.2% and 55.1% for IsG and 11.9% and 84.9% for M-IsG.
En(C) was extracted by salting out of the culture of B. oralis with 60% saturation of ammonium sulfate. En(C) hydrolyzed IsG, M-IsG and dextran, whereas commercial dextranase (α-1,6 glucanase) hydrolyzed only dextran. IsG was treated with the commercial dextranase until no glucose was detected in the medium, and the remaining material was used for the substrate of enzymes. Release of glucose was detected from the substrate by treatment with En(C), but not with commercial dextranase. These results indicated that En(C) of Bacteroides oralis contained at least two types of glucanase, one being dextranase which hydrolyzes the α-(1-6) linkage and the other the so-called mutanase which hydrolyzes the α-(1-3) linkage.
