Isolation, properties and amino acid sequences of two 1,3-β-D-glucanases from gastropoda Lambis sp.
Keywords:
1,3-β-D-glucanase, hepatopancreas, laminaran, marine mollusk, Lambis sp., transglycosylationAbstract
Two 1,3-β-D-glucanases from hepatopancreas of marine gastropoda Lambis sp. from the South China Sea with molecular weights of 44 and 51 kDa were isolated and characterized. The properties of these two enzymes appeared to be similar to endo-1,3-β-D-glucanases (EC 3.2.1.39) of tropical sea mollusks: temperature optimum was 60 °C, pH range was from 3.0 to 6.0, Km for laminaran hydrolysis was 0.30–0.35 mg/ml. In both cases, glucose was the main product of complete hydrolysis. The both enzymes catalyzed hydrolysis of laminaran with retention of configuration of anomeric carbon atom and formation of transglycosylation products with DP 2 and 3. There were determined full cDNA sequences, coding these 1,3-β-D-glucanases. Both enzymes were classified to O-glycoside hydrolase structural family 16 (GH16).