INDUCED BETA-1,3-GLUCANASE FROM MARINE BACTERIUM ALTEROMONAS SP

A laminarin-induced beta-1,3-glucanase with molecular weight 40 kD, te mperature optimum 45 degrees C, and pH optimum 5.5 was isolated from t he marine bacterium Alteromonas sp. The products of laminarin hydrolys is by the beta-1,3-glucanase are laminarin oligosaccharides and glucos e. Near the beginning of the reaction the accumulation of reducing sug ars markedly exceeds the accumulation of glucose. The enzyme has trans gry-cosylating activity. The beta-1,3-glucanase is endo-specific. Chem ical modification indicates that tryptophan, histidine, and dicarboxyl ic acid residues are important for enzymatic activity.