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KMID : 0379119870150010029
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Korean Journal of Mycology
1987 Volume.15 No. 1 p.29 ~ p.37
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Studies on the cellulase properties of Aspergillus clavatus from the Cellulose - Cultural Properties
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Abstract
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Cellulolytic mocrooganisms were isolated from the cellulose-cultural properties. Among them, Aspergillus clavatus with the highest cellulase activity was identified by the morphological characteristics and it´s enzyme activities were compared on the various cultural conditions. It was found that the induction of carboxymethylcellulase(CMCase), avicelase and salicinase in CMC liquid media showed the highest enzyme activity on five day´s cultivation at 30℃ and thereafter their activities were gradually decreased with time. After crude extracellular enzymes precipitated with the 70% saturated ammonium sulfate solution were dialyzed with 20 mM acetate buffer pH 6.0, each crude enzyme was examined. The optimal activities of CMCase and avicelase were both found to be at 50℃ and pH 6.0. Their thermal stability was appeared at the 50℃. CMCase and avicelase had the maxima activities with 1.5% and 2.2% substrate concentration, respectively. The concentration of 5 mM Mg^(++) or Ca^(++) was found to have a maximum cellulase activity and its activity was inhibited with more than 5 mM Cu^(++) and Zn^(++) concentration. Cellulase activity was also inhibited sensitively by the inhibitors such as 2-mercaptoethanol, iodine and sodium azide.
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