Proteases are the most important groups of industrial enzymes, with considerable application in the food industry. The aim of this work was to characterize protease from Aspergillus sp UCP1287 produced by submerged fermentation. Optimum temperature for enzyme activity in the crude extract was 50°C and the optimum pH was 11.0. The studies on pH stability showed that the enzyme was stable in a range of pH 7.0–10.0 and the effect of the inhibitors showed it to be a serine protease because of PMSF (Phenyl Methyl Sulphonyl Fluoride) showed 89.06% inhibition of activity. Thermostability revealed temperatures 30-40°C showed 81.5% residual activity at 180 minutes. The activity was reduced in the presence of Cu2+(35.18%), Fe2+(36.45%) and Na2+(39.9%) ions. The biochemical properties found with this enzyme assure that it could be a potential candidate for industrial applications. The high activity in alkaline pH make these proteases an ideal choice for application in detergent formulations.