Kinetic and Thermal Characterization of Alkaline Protease Produced by a New Alkalophilic Isolate of Bacillus subtilis

Present studies involve the production and purification of alkaline protease from a new isolate of Bacillus subtilis. The purified enzyme was characterized and described kinetically. It was found that the enzyme was highly active at a temperature of 55 degrees C and a reaction pH of 8.5 however, it was active in a wide range of pH from 5-12. The optimum substrate/ enzyme ratio and reaction period were found to be 150 and 40 min respectively. The enzyme showed optimum values of KM and Vmax when it was used to hydrolyze casein so it was inferred that the enzyme was a caseinase type of protease. The enthalpy (ΔHD) and entropy of activation (ΔS) for alkaline protease activity were recorded as 34.5 ± 4 kJ/mol and -160 ± 12 J/ mol/ K respectively.