KMID : 0903519840270030174
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Journal of the Korean Society of Agricultural Chemistry and Biotechnology 1984 Volume.27 No. 3 p.174 ~ p.179
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Studies on the Characterization of Protease Produced by Streptomyces alboniger
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Abstract
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Some physico-chemical properties of proteolytic enzyme produced from Streptomyces alboniger Hesseltine were characterized.
The optimal pH and temperature of the enzyme; were around pH 9.0 and 40¡É, respectively. The enzyme was stable between pH 6.0¡10.8 and the enzyme activity was not inactivated by heat treatment in lower temperature than 40¡É. However the enzyme activity decreased by 70% of the initial activity for 10minutes at 70¡É. The Km value was 7.1¥ìM with Hammarsten casein and 333.3¥ìM with cytochrom C. The activity of enzyme was inhibited by metal ions in the order of Fe^(+++)$gt;Hg^(++)$gt;Cu^(++$gt;Pb^(++)$gt;Zn^(++), whereas Ca++ increased the enzyme activity. There was no effect of Mg^(++) and Co+t on the enzyme activity. The enzyme was inhibited by EDTA strongly. When Ca^(++) was added to the EDTA-denaturated enzyme, the activity of enzyme was restored.
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