Characterization of a thermostable alkaline protease from Staphylococcus aureus S-2 isolated from chicken waste.

In this study, the protease producing bacterium was isolated from chicken waste and characterized as Staphylococcus aureus through 16S rRNA ribotyping. The protease from S. aureus S-2 showed maximum activity of 360 U/mL. S. aureus S-2 showed optimum growth at 37 degrees C and pH 7. S. aureus S-2 was able to grow in 1% gram pulse, mung beans and hydrolyzed casein but the maximum growth of the organism was supported by 1% hydrolyzed casein. A comparison of intracellular and extracellular enzyme activity showed that the predominant form of the enzyme was extracellular. The optimal pH and temperature for the protease activity were 8.0 and 50 degrees C, respectively. The enzyme was active at a broad range of pH (5-9) and temperatures (30-90 degrees C). The molecular mass of the enzyme was found to be 30 kDa in SDS-polyacrylamide gel electrophoresis. S. aureus S-2 can be exploited for biotechnological and industrial applications.