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KMID : 0903519840270030174
Journal of the Korean Society of Agricultural Chemistry and Biotechnology
1984 Volume.27 No. 3 p.174 ~ p.179
Studies on the Characterization of Protease Produced by Streptomyces alboniger



Abstract
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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