1990 Volume 54 Issue 8 Pages 2107-2114
A nonlytic endo-β-1, 3-glucanase I (1, 3-β-D-glucan glucanohydrolase, EC 22.214.171.124) was purified from the culture broth of Flavobacterium dormitator var. glucanolyticae, which produced several species of endo-β-1, 3-glucanases. The purified enzyme decomposed various β-1, 3-glucans such as laminarin, yeast glucan, and pachyman to yield glucose, laminaribiose, and laminaritriose as the main products; the enzyme is a smaller oligosaccharide-producing type of endo-β-1, 3-glucanase. The molecular weight and isoelectric point of the enzyme were 27, 000 and 5.8, respectively. The substrate specificity, the conditions for the maximum reactivity, stability, and immunochemical properties of the enzyme resembled those of the lytic endo-β-1, 3-glucanase II, but there were some differences in isoelectric points, molecular weights, and the lytic activity on viable yeast cells between β-1, 3-glucanases I and II. By addition of yeast cells to the culture medium, the secretion of nonlytic β-1, 3-glucanase I was induced with a lag period, following the secretion of lytic β-1, 3-glucanases II and IV. From the results of the enzymological, immunological, and limited proteolytic experiments, it is concluded that β-1, 3-glucanase I was formed by a proteolytic digestion of β-1, 3-glucanase II during the cultivation of the organism.
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