KMID : 0379119820100020067
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Korean Journal of Mycology 1982 Volume.10 No. 2 p.67 ~ p.73
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Studies on the Isolation , Purification and Characterization of a Cx Enzyme Produced by Pyricularia oryzae , C-7+t
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Abstract
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The (NH©þ)©ü SO©þ, (70%) treated crude enzymes from the culture filtrates of the C-7^(+1) strain of Pyricularia oryzae which was grown on 2% CMC (carboxymethyl cellulose) for 8 days at 28¡É, were chromatographied on Sephadex G-150 and DEAE-Sephadex A-25 columns. From the chromatography, three fractions of CMCase(C_x) was examined using Na-CMC as substrate. The C_x enzyme activity was optimal at pH 6.0 and 40¡É, stable up to 40¡É. The values of Km and Vmax of the enzyme were 2.8 ¡¿ 10 mM and 5.9m moles/hour, respectively. The molecular weight determined by Sephadex G-150 column chromatography was around 80,000. Approximately sevenfold purified C_x enzyme gave a single protein band on the polyacrylamide gel electrophoresis.
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