An enzyme from Streptococcus mutans forms branches on dextran in the absence of sucrose.

摘要: Abstract An enzyme in glucosyltransferase preparations from Streptococcus mutans catalyzed the transfer of [14C]glucopyranoside purified isomaltosaccharides, each containing at its non-reducing terminus, to acceptor dextran, absence sucrose. Half radioactivity present resulting [14C]dextrans was resistant hydrolysis by amylo-1,6-glucosidase. Treatment with endodextranase resulted extensive and produced [14C]-labeled limit oligosaccharides branch sites. Acetolysis yielded [14C]nigerose, thus indicating formation sites on dextran The catalyzing this reaction has not been identified but appears be independent major extracellular glucosyltransferases S. .