Purification, cDNA cloning and homology modeling of endo-1,3-beta-D-glucanase from scallop Mizuhopecten yessoensis.

The retaining endo-1,3-beta-D-glucanase (LV) with molecular mass of 36 kDa was purified to homogeneity from the crystalline styles of scallop Mizuhopecten yessoensis. The purified enzyme catalyzed hydrolysis of laminaran as endo-enzyme forming glucose, laminaribiose and higher oligosaccharides as products (Km approximately 600 microg/mL). The 1,3-beta-D-glucanase effectively catalyzed transglycosylation reaction that is typical of endo-enzymes too.