Isolation, Purification and enzymatic characterization of the Cellulase produced by Aspergillus Phoenicis

Aspergillus phoenices K.U. 175이 생성하는 셀루라아제의 분리, 정제 및 효소학적 성질

Avicelase, CMCase and salicinase of A.phoenicis K.U. 175 were purified from wheat bran culture by salting out with ammonium sulfate, dialysis and successive column chromatography Sephadex G-100. Optimum pH and temperature of avicelase were pH 3.8-4.8, $35-55^{\circ}C$ and that of CMCase, salicinase were pH4.5-5.5, $45-60^{\circ}C$ and pH 4.5-6.0, $45-60^{\circ}C$ respectively. These enzymes were relatively thermostable, alkali unstable and inhibited by $Ca^{++},\;Mn^{++},\;Cu^{++},\;and\;Hg^{++}$. Km values of avicelase, CMCase and salicinase were calculated to be $1.5{\times}10^{-4}M,\;5.5{\times}10^{-4}M\;and\;2.75{\times}10^{-5}M$ and Vmax values $1.66{\times}10^{-4}mM/min,\;3.33{\times}10^{-4}mM/min\;and\;1.14{\times}10^{-4}mM/min$, respectively.