Abstract |
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℃ and that of CMCase, salicinase were pH4.5-5.5, 45-60℃ and pH 4.5-6.0, 45-60℃ 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 × 10^-4M and 2.75 × 10^-5M and Vmax values 1.66 × 10^-4 mM/min, 3.33 × 10^-4 mM/min and 1.14 * 10^-4mM/min, respectively. |