Purification and Some Properties of p-Nitrophenyl-β-D-glucoside-hydrolyzing Enzymes in Culture Filtrate of Bacillus circulans KA-304 Grown on Cell-wall Preparation of Schizophyllum commune

概要

論文の詳細を見る
Hydrolyzing activities toward p-nitrophenyl (p-NP)-β-D-glucoside and laminarin in a culture filtrate of Bacillus circulans KA-304, which has been observed to form protoplasts from Schizophyllum commune mycelia, increased when the bacterium was grown on a cell-wall preparation (CWP) of S. commune or laminarin as a carbon source. An analysis of the filtrate with the CWP suggested occurrence of two major p-NPβ-D-glucoside-hydrolyzing enzymes (β-D-glucosidases I and II) and a laminarin-hydrolyzing enzyme. After separation by DEAE-cellulose column chromatography, β-D-glucosidases I and II were isolated (β-D-glucosidases I: 13-fold purification with 34% yield; β-D-glucobidases II: 26-fold with 8%). The enzymes resembled each other in their properties except for their molecular weight, subunit structure (β-D-glucosidase I: 200,000, tetramer; II: 100,000, dimer), and susceptibility to such substandes as p-chloromercuribenzoic acid and Ag^+ ion. β-D-Glucosidases I and II hydrolyzed gentiobiose (β-1, 6 glucosidic linkage; Km=3.6 mM, β-D-glucosidase I; 4.6 mM, β-D-glucosidase II) and laminaribiose (β-1, 3 glucosidic linkage; Km=6.1 mM, β-D-glucosidase I; 6.7 mD β-D-glucosidase II), and showed a certain reactivity toward laminarin as well.
社団法人日本農芸化学会の論文
1998-01-23