Purification and properties of lytic .BETA.-1, 3-glucanase from Flavobacterium dormitator var. glucanolyticae.

Abstract

An endo β-1, 3-glucanase which is able to disrupt the cells of living yeast has been purified in homogeneous state from the culture filtrate of Flavobacterium dormitator var. glucanolyticae. The molecular weight of the enzyme was estimated to be 17,000 ~ 22,000. The mode of enzyme action has been suggested to be a “random” type of β-1, 3-glucanase. The enzyme preferes larger chains saccharides as substrate for its action, however, smaller oligosaccharides such as laminaritriose and laminaribiose are also decomposed by the enzyme. The Km values of the enzyme for laminarin, laminarihexaose, and laminaritetraose were determined to be 0.26, 1.18, and 2.00 g/liter, respectively. The ability of this enzyme to disrupt the cells of living yeast is its remarkable point, since endo β-1, 3-glucanase of a smaller oligosaccharide-producing type from most sources has been recognized to be inactive (or very weakly active) on living yeast cells.