PURIFICATION AND PROPERTIES OF SECRETORY ASPARTIC PROTEINASE FROM CANDIDA ALBICANS / 微生物学通报

An extracellular proteinase from Candida albicans WD27 was purified by (NH4)2SO4 fractionation and DEAE-Sephacel ion-exchange chromatography with 25.4 fold and 5.2% yield. This enzyme appeared to be aspartic proteinase since the enzyme activity could be inhibited by pepstatin which was specific inhibitor of this class of proteinase. The enzyme had an acidic proteolytic activity profile with the optimum pH of 4.0. The optimum temperature of the enzyme activity was 37℃. The proteinase had a broad substrate specificity with the highest susceptibility to bovine hemoglobin. The Km for bovine hemoglobin was determined to be 0.814mmol/L.