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 $1.5{ imes}10^{-4}M,;5.5{ imes}10^{-4}M;and;2.75{ imes}10^{-5}M$ and Vmax values $1.66{ imes}10^{-4}mM/min,;3.33{ imes}10^{-4}mM/min;and;1.14{ imes}10^{-4}mM/min$, respectively.