STUDIES ON DEXTRANSUCRASE

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Abstract
A strain of L. mesenteroides secretes an extracellular enzyme for riboflavinylglucoside formation from sucrose and riboflavin. The enzyme was isolated from the cell-free culture fluid by precipitation with (NH4)2SO4 and reprecipitation with acetone. Maximum activity of the enzyme was observed at pH 5.0[long dash]5.6 and 25[long dash]30[degree]. The enzyme was fairly sensitive to heat, even at pH 5.3. The enzyme revealed high specificity on sucrose, since any other sugars did not act as the glucosyl donor for the formation of riboflavinyl-glucoside. The enzyme formation was observed only in a sucrose medium. Maltose showed a strong inhibitory effect on the formation of riboflavinylglucoside; and Cu2+, Fe2+ and Fe3+ also acted as powerful inhibitors.

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