Dextran Sucrase from Leuconostoc mesenteroides

Dextran Sucrase from Leuconostoc mesenteroides belongs to glycoside hydrolase family 70 (GH70). It functions through a retaining mechanism and uses two catalytic acidic residues. Dextran sucrase has a dextran binding site in the C-terminal domain.

Dextran Sucrase from Leuconostoc mesenteroides has been used:

• in immobilization on shirasu porous membrane (SPG) for dextran production
• in the enzymatic synthesis of dextran nanoparticles at various pH range
• in the immobilization with hydroxyapatite for dextran production

The enzyme from Sigma has been used to prepare immobilized sphere for the production of dextran from sucrose.

Dextran sucrase from Leuconostoc mesenteroides has been used in a study to investigate the functional and structural characterization of α-(1→2) branching sucrase derived from DSR-E glucansucrase. Dextran sucrase from Leuconostoc mesenteroides has also been used in a study to investigate the bioengineering of Leuconostoc mesenteroides glucansucrases.

Dextransucrases are glucansucrases that are able to produce dextran, a glucose polymer linked mainly through α1-6 bonds. However, α1-3, α1-6, α1-4 and α1-2 bonds are also found, in both the main chain and the branching linkages. The peptide has approximately 1600 amino acids. The aspartic acid in position 551 is essential for catalytic activity, while glutamic acid 589 and aspartic acid 662 complement the catalytic triad. The activity of dextransucrase is decreased by EDTA, and is restored by the addition of calcium ions. Zinc, cadmium, lead, mercury and copper ions are inhibitory to various degrees.

Lyophilized powder containing dextran, MES buffer salts and CaCl₂

Chromatographically purified

One unit will liberate 1.0 μmole of fructose per min at 37 °C, pH 5.4.