An extracellular glucosyltransferase synthesizing water-insoluble glucan (GTF-I) was purified from the culture supernatant of strain BHT (mutans serotype ) by hydroxylapatite chromatography, DEAE-Toyopearl chromatography and preparative isoelectric focusing. The of GTF-I was 155000 by SDS-PAGE and the isoelectric point was pH 4.9. The specific activity, the optimum pH and the value for sucrose were 10.0 i.u. (mg protein), 6.5 and 2.4 m, respectively. The enzyme synthesized a water-insoluble glucan consisting of 69.4 mol% 1,3-α-linked glucose, 23.6 mol% 1,6-α-linked glucose, 2.4 mol% 1,3,6-α-branched glucose and 4.4 mol% non-reducing terminal glucose, and also a small amount (3% of the total glucan) of soluble glucan with 82.4 mol% 1,6-α-linked glucose. The and pI values of purified GTF-I were identical with those of the enzyme in the culture supernatant.


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