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 K-M and V-max when it was used to hydrolyze casein so it was inferred that the enzyme was a caseinase type of protease. The enthalpy (Delta H-D) and entropy of activation (Delta S) for alkaline protease activity were recorded as 34.5 +/- 4 kJ/mol and -160 +/- 12 J/mol/K respectively.