PURIFICATION AND CHARACTERIZATION OF A LIPOLYTIC ENZYME ACTIVE AT LOW-TEMPERATURE FROM NORWEGIAN TYPHULA-ISHIKARIENSIS GROUP-III STRAIN

An extracellular lipolytic enzyme active at low temperature was purifi ed from the culture filtrate of the snow mold fungus, Typhula ishikari ensis group III, strain 6-1-1. The molecular mass of enzyme was approx imately 83 kDa (SDS-PAGE). The lipolytic enzyme was most active for p- nitrophenyl palmitate at 30 degrees C (pH 9.0). The lipolytic activity was 23.4% of the maximum at 4 degrees C, the temperature of culture. Thus, the isolated ir: ishikariensis lipolytic enzyme is thought to re present a new member of a group of enzymes active at low temperature.