A mutant (S19) of Sreptococcus mutans strain 6715 which produces elevated levels of dextransucrase (EC 2.4.1.5) was isolated. Soluble enzyme in culture supernatant solutions from S19 polymerized the glucosyl moiety of sucrose into alcohol-insoluble and water-insoluble glucans at a rate three to six times greater than that of the parent strain. Washed-cell suspensions of S19 also contained increased amounts of cell-associated enzyme. Adherence of S19 to glass in the presence of sucrose occurred at twice the rate of strain 6715. The Km values for sucrose and primer dextran were similar for the mutant and parent enzymes. Mutant S19 should facilitate studies on the mechanism of adherence of S. Mutans and the control of dextransucrase production by this bacterium.
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