(1⇾2)-β-_D-Glucan-Hydrolyzing Enzymes in Cytophaga arvensicola : Patrial Purification and Some Properties of Endo-(1⇾2)-β-_D-Glucanase and β-_D-Glucosidase Specific for (1⇾2)-and(1⇾3)-Linkages

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Cytophaga arvensicola A21L, a bacterium isolated from soil, produces an intracellular enzyme degrading cyclic(1⇾2)-β-_D-glucan. The enzyme was highly inducible and was released from the cells by sonication. The inducible cell bound enzyme was found to be a mixture of two enzymes acting together in the complete degradation of cyclic (1⇾2)-β-_D-glucan. These two enzymes could be separated by CM-cellulose chromatography into an endo(1⇾2)-β-_D-glucanase and β-_D-glucosidase. These enzyme were purified about 5-fold and 260-fold, respectively. The glucosidase had high activity towards sophoro-oligosaccharides, laminarabiose, and p-nitrophenyl-β-_D-glucoside. Some properties of the enzyme were examined. The endo(1⇾2)-β-_D-glucanase was further purified on Sephadex G-150 and its activities on cyclic(1⇾2)-β-_D-glucan and sophoro-oligosaccharides were checked by paper chromatography. It hydrolyzed cyclic (1⇾2)-β-_D-glucan in a random manner releasing β-(1⇾2)-linked oligosaccharides with a small amount of glucose. The enzyme showed a preference for longer chain substrates and hydrolyzed only sophorohexaose well among the oligosaccharides tested.
公益社団法人日本生物工学会の論文
1983-10-25