Abstract
Cellulase components, CMCase(Cx) and Avicelase$(C_1)$, were partially prueified, 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^{\circ}C\;and\;60^{\circ}C, $ respectively. More than 70% of the activities of two enzymes were remained after heating at $60^{\circ}C$ 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 were $23.20{\mu}g\;and\;2.54{\mu}g$ of reducing sugar per min. Of the metal ions tested against the activites of CMCase and Avicelase, $Cu^{++}, \; Hg^{++}, \;and\;Pb^{{++}$ are remarkably effective inhibitors. The molecular weights of Cx and $C_1$ component were estimated to be about 47, 000 and 61, 000 by gel filtration method.
