[Streptococcus mutans glucosyltransferase: isolation and its ability to synthesize polysaccharides].

The extracellular glucosyltransferases (GTF, EC 2.4.1.5) were extracted from trypticase yeast L-cystine culture supernatant of streptococcus mutans strains SSMC 167(g), 6715(g), SSMC 100 (c) and Ingbritt (c) by 60% saturated ammonium sulphate precipitation. The yield was more than 50%. All the enzyme preparations could synthesize both water-soluble and insoluble glucans. The results of polyacrylamide gel electrophoresis of enzyme preparations illustrated the complexity and multicomponent nature of the GTF of S. mutans. The abilities of synthesizing polysaccharides were different between S. mutans serotype g and serotype c. The ability of synthesizing water-soluble glucan was almost the same as that of synthesizing water-insoluble glucan for GTFs from the two S. mutans strains of serotype g, but the ability of synthesizing water-soluble glucan was 10-fold to that of synthesizing water-insoluble glucan for GTFs from other two strains serotype c. No frucotosyltransferase activity was found.