Catalytic properties of endo-1,3-beta-D-glucanase from the Vietnamese edible mussel Perna viridis

A beta-1,3-glucanase with a molecular mass of 33 kDa was isolated in the homogeneous state from a crystalline stalk of the commercially available Vietnamese edible mussel Perna viridis. It hydrolyzes beta-1,3-bonds in glucans and is capable of catalyzing the transglycosylation reaction. The beta-1,3-glucanase has a K (m) value of 0.3 mg/ml for the hydrolysis of laminaran and shows a maximum activity in the pH range from 4 to 6.5 and at 45A degrees C. Its half-inactivation time is 180 min at 45A degrees C and 20 min at 50A degrees C. The enzyme was ascribed to glucan-endo-(1 -> 3)-beta-D-glucosidases (EC 3.2.1.39). The enzyme could be used in the structure determination of beta-1,3-glucans and enzymatic synthesis of new carbohydrate-containing compounds.