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KMID : 0364819870250010001
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Korean Journal of Microbiology
1987 Volume.25 No. 1 p.1 ~ p.8
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Purification and Properties of β-1. 3-Glucanase from Pseudomonas stutzeri KF13
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Bang, K.W./方光雄
Song, H.I./Kim, J.K./Yu, T.S./Chung, K.T./宋亨翼/金在根/兪大植/程基澤
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Abstract
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1
An extracellular P-1, 3-glucanase from Pseudomonas stutzeri KF 13 was purified about 390 fold 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´C, respectively. The activation energy was calculated to be 16,130 cal per mole. The Km value for laminarin was found to be 3 mg 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. 0 mM of Hg´ +, and strongly inhibited by 1.0 mM of p-chloromercuribenzoic acid. KEY WORDS 0 Pseud. stutzeri KF 13, 8 -1, 3-glucanase.
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KEYWORD
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