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Cellulase components, CMCase(Cx) and Avicelase(C₁), were partially purified, from the culture extract of a strain of Trichoderma koningii by column chromatography on DEAE-Sephadex A-50 and the step of gel filtration through Sphadex G-150, Optimum pH of CMCase was 5.2 and Avicelase showed the highest activity at pH 5.6 in acetate buffer. Optimal temperatures for activities of CMCase and Avicelase were 50℃ and 60℃ respectively. More than 70% of the activities of two enzymes were remained after heating at 60℃ for 30 min and Avicelase is more stable than any other fungal enzymes. The Michaelis constants, Km, of CMCase and Avicelase were 0.116% of CMC and 0.281% of avicel. And also the values of maximum velocity, Vmax, of CMCase and Avicelase, Cu^++, Hg^++, and Pb^++ are remarkably effective inhibitors. The molecular weights of Cx and C₁component were estimated to be about 47,000 and 61,000 by gel filtration method.
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