The aim of this experimental study was to isolate and partially purify extracellular protease from Hypocrea virens and Trichoderma koenigii. The species were inoculated in a protease fermentation medium. The supernatants were collected after 92 hours. The partial purification was realized by applying respectively, ammonium sulfate precipitation, dialysis and DEAE-Cellulose ion exchange chromatography to the supernatant. Effect of pH and temperature on enzyme activity and stability were determined. In addition, the molecular mass of the obtained enzyme was investigated by Sodium Dodecyl Sulphate-Polyacrylamide gel elecrophoresis (SDS-PAGE). The specific activity of partially purified enzyme from Hypocrea virens and Trichoderma koenigii were determined to the 63U/mg and 16U/mg respectively. The final enzyme preparation from Hypocrea virens and Trichoderma koenigii were 9.3 and 3.1 fold more pure than the crude homogenate respectively. The molecular mass of the partially purified enzyme from Hypocrea virens and Trichoderma koenigii were found to be 33kDa and 52kDa respectively by using SDS-PAGE.