Isolation and some properties of the two components of an Arthrobacter β-1, 3 glucanase (glucanase II-1 and glucanase II-2) are described. Both of these glucanases hydrolyzed various β-1, 3 glucans, accumulating as final products, glucose and laminaribiose. They resembled each other in instability at acidic pH values, lability at temperature above 55°C, having an optimal pH range of 5.5_??_6.5 and requirement of the presence of glucanase I for the effective hydrolysis of yeast glucan. Glucanase II-1 showed a high lytic activity for isolated yeast cell wall, while the activity of glucanase II-2 was low. Culture fluids of early cultures contained glucanase II-1 predominantly, while those of late cultures contained glucanase II-2, predominantly.

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