The extracellular protease APSm1 was purified to homogeneity from m>Stenocarpella maydism>.

The molecular weight of enzyme was estimated to be 56.8 kDa.

Enzymatic activity toward hemoglobin was optimal at pH 2.0 and at 25 °C.

Pepstatin A inhibited APSm1 activity, as the protein is in fact an aspartyl protease.

The Km and m>Vm>_max values obtained were 0.514 mg/mL and 0.222 μmol/min, respectively, using hemoglobin as the substrate.