Purification and Properties of Mycodextranase from Streptomyces sp. J-13-3

概要

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An enzyme hydrolyzing nigeran (alternating α-1,3-and α-1,4-linked glucan) was purified from the culture filtrate of Streptomyces sp. J-13-3,which lysed the cell wall of Aspergillus niger, by precipitation with ammonium sulfate and column chromatographies on DEAE-Sephadex A-50,CM-Sephadex C-50,chromatofocusing, and Sephadex G-100. The final preparation was homogenous in polyacrylamide gel electrophoresis (PAGE). The molecular weight of the enzyme was 68,000 by SDS-PAGE and gel filtration. The optimum pH and temperature for the enzyme activity were 6.0 and 50℃, respectively. The enzyme was stable in the pH range from 6.0 to 8.0 and up to 50℃. The enzyme activity was inhibited significantly by Hg^+, Hg^<2+>, and p-chloromercuribenzoic acid. The K_m (mg/ml) for nigeran was 3.33. The enzyme specifically hydrolyzed nigeran into nigerose and nigeran tetrasaccharide by an endo-type of action, indicating it to be a mycodextranase (EC 3.2.1.61) that splits only the α-1,4-glucosidic linkages in nigeran.
社団法人日本農芸化学会の論文
1992-09-23