The Action Modes of an Extracellular β-1, 3-Glucanase Isolated from Bacillus clausii NM-1 on β-1, 3-Glucooligosaccharides (ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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The mode of action of an extracellular β-1, 3-glucanase from Bacillus clausii NM-1 on β-1, 3-glucooligosaccharides and their alditols was studied. The enzyme could not hydrolyze laminaribiose or laminaritriose. β-1, 3-Glucooligosaccharides higher than laminarihexaose were rapidly hydrolyzed, while laminaritetraose was slowly hydrolyzed. The k_<cat>/K_m ratios for a series of β-1, 3-glucooligosaccharides from laminaritetraose to laminariheptaose showed that the substrate binding site of the enzyme covered a wide range of β-1, 3-glucooligosaccharides having six glucose residues. The action pattern of the enzyme on the alditols corresponding to each laminarioligosaccharide suggested that the catalytic site of the enzyme existed between the third and fourth glucose residue from the non-reducing terminal. The value of k_<cat>/K_m also suggested that the sixth binding position contributed to the catalytic efficiency and stability.
社団法人日本生物工学会の論文
2003-07-25