The glucansucrases transfer a D-glucosyl residue from sucrose to a glucan chain. They are classified based on the linkage of the transferred glucosyl residue. The enzyme, characterized from the lactic acid bacterium Limosilactobacillus reuteri strain 121, catalyses the hydrolysis of sucrose and the transfer of the D-glucose moiety to suitable acceptors (inclduing sucrose), forming the glucan reuteran, which is typical for these strains. The enzyme forms mostly alpha(1->4) glucosidic linkages, but also alpha(1->6) linkages. The presence of maltose significantly accelerate the initial rate of the reaction. See EC 2.4.1.5, dextransucrase.
Kralj S, van Geel-Schutten GH, Rahaoui H, Leer RJ, Faber EJ, van der Maarel MJ, Dijkhuizen L.
Title
Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1-->4) and alpha-(1-->6) glucosidic bonds.
