Partial Purification and Characterization of a Haloalkaline Protease from Pseudomonas aeruginosa

A study was conducted to partially purify and characterize a haloalkaline protease isolated from Pseudomonas aeruginosa. The enzyme was purified in a two-step procedure involving acetone precipitation and chromatography. The enzyme was shown to have a relatively low molecular weight of 30 kDa. The haloalkaline protease enzyme was purified 2.2-fold with a relative activity of 67.25%. The maximum activity of the enzyme was noticed at 35°C at pH 9, with casein as a substrate. The partially purified enzyme was almost 100% stable at 5% sodium chloride supplemented medium even after 1hr of incubation. The effect of sodium dodecyl sulphate on partially purified protease activity revealed that the maximum activity was found to be at 50 mM. The impact of ethylene diamine tetra acetic acid on the partially purified protease activity revealed that the maximum activity was found to be at 50 mM. The compatibility of the enzyme was studied with commercial and local detergents. The partially purified enzyme has improved the sanitization power of the detergents tested.