Properties of Dextransucrase from Leuconostoc mesenteroides Isolated from Sikhae

Studies on the optimum conditions for dextran production and the properties of dextransucrase (DS) were performed with Leuconostoc mesenteroides from Sikhae and Leuconostoc mesenteroides NRRL B-512(F). Dextransucrases were partially purified by lyophilization of the culture supernatant and subsequent gel chromatography on Bio-Gel A-5(m). The storage stabilities of Sikhae DS and B-512(F) DS were decreaed by the addition of dextranase. The optimum conditions for the enzyme stability were pH 5 and below $30^{\circ}C$. The B-512(F) DS lost the activity at pH 4, while Sikhae DS had 30% of the activity at the same pH. The activity of DS was decreased by EDTA. confirming the metalloprotein character of the enzymes, and was restored by the addition of calcium ions. Concanavalin A completely removed the activity of DSs, confirming the glycoprotein character of the enzymes.