Role of primers in glucan synthesis by glucosyltransferases from Streptococcus mutans strain OMZ176.

The effects of isomaltosaccharides of various molecular weights (isomaltose to dextran T2000) on glucan synthesis by a water-soluble glucan-synthesizing glucosyltransferase enzyme (GTase-S) and a water-insoluble glucan-synthesizing enzyme (GTase-I), both from Streptococcus mutans OMZ176, were examined. The activity of GTase-S was not affected by the addition of the isomaltosaccharides, but GTase-I was stimulated increasingly by isomaltosaccharides with degrees of polymerization more than 10. The GTase-I activity first increased and thereafter decreased slightly with increasing amounts of a soluble dextran. Maximal stimulation occurred at concentrations in the range 0.1 to 0.2 mg ml-1, when dextran T10 was used as a primer. The rate of glucan synthesis was highly enhanced by the combined action of GTase-S and GTase-I. The profile of the net activity of GTase-I in the presence of various amounts of GTase-S was similar to that of GTase-I in the presence of increasing amounts of an exogenous dextran. These results collectively suggest that soluble glucan produced by GTase-S from sucrose acts as an intrinsic primer for the glucan synthesis by GTase-I, indicating the contribution of autopriming in glucan synthesis by crude GTase of S. mutans.