SUMMARY: Ingbritt (serotype ) was shown to have a significant amount of cell-associated glucosyltransferase activity which synthesizes water-insoluble glucan from sucrose. The enzyme was extracted from the washed cells with SDS, renatured with Triton X-100, adsorbed to 1,3-α--glucan gel, and then eluted with SDS. The enzyme preparation was electrophoretically homogeneous, and the specific activity was 7·3 i.u. (mg protein). The enzyme had an of 158000 as determined by SDS-PAGE, and was a strongly hydrophilic protein, as judged by its amino acid composition. The enzyme gradually aggregated in the absence of SDS. The enzyme had an optimum pH of 6·5 and a value of 16·3 mM for sucrose. Activity was stimulated 1·7-fold by dextran T10, but was not stimulated by high concentrations of ammonium sulphate. Below a sodium phosphate buffer concentration of 50 mM, activity was reduced by 75%. This enzyme synthesized an insoluble -glucan consisting of 76 mol% 1,3-α-linked glucose and 24 mol% 1,6-α-linked glucose.


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