Trichoderma koningii로 부터 추출한 섬유소분해효소의 부분정제 및 그의 효소학적 성질

Partial Purification and some Properties of Cellulase Components from Trichoderma koningii

Cellulase components, CMCase(Cx) and Avicelase<TEX>$(C_1)$</TEX>, 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 <TEX>$50^{circ}C;and;60^{circ}C, $</TEX> respectively. More than 70% of the activities of two enzymes were remained after heating at <TEX>$60^{circ}C$</TEX> 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 <TEX>$23.20{mu}g;and;2.54{mu}g$</TEX> of reducing sugar per min. Of the metal ions tested against the activites of CMCase and Avicelase, <TEX>$Cu^{++}, ; Hg^{++}, ;and;Pb^{{++}$</TEX> are remarkably effective inhibitors. The molecular weights of Cx and <TEX>$C_1$</TEX> component were estimated to be about 47, 000 and 61, 000 by gel filtration method.