Title Pseudomonas-stutzeri KF13의 β-1, 3-glucanase 精製 및 性質
Author 方光雄 · 宋亨翼 · 金在根 · 兪大植 * · 鄭基澤
Address 경북대학교 식품가공학과; *계명대학교 생물학과
Bibliography Korean Journal of Microbiology, 25(1),1-8, 1987
DOI
Key Words Pseud. stutzeri KF13, β-1,3-glucanase
Abstract An extracellular β-1, 3-glucanase from Pseudomonas stutzeri KF 13 was purified about 390 with 26% recovery. The purified enzyme revealed a single band by polyacrylamide gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The enzyme was stable in a pH 6.0 to 9.0, and relatively thermostable. The optimal pH and temperature on the enzyme activity were found to be 5.8 and 45℃, respectively. The activation energy was calculated to be 16,130 cal per mole. The Km value for laminarin was found to be 3ng per ml and the molecular weight was determined to be 28,000 by gel filtration and 26,000 daltons by SDS-acrylamide gel electrophoresis. The enzyme was inhibited by 1.0mM of Hg^2+, and strongly inhibited by 1.0mM of p-chloromercuribenzoic acid.
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