The extracellular protease APSm1 was purified to homogeneity from Stenocarpella maydis.
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 Vmax values obtained were 0.514 mg/mL and 0.222 μmol/min, respectively, using hemoglobin as the substrate.