STABILITY AND ACTIVITY PROFILE OF ALKALINE PROTEASE, PRODUCED FROM BACILLUS SUBTILIS

The present study gives an insight into the effect of different activators and inhibitors on the activity and stability of alkaline proteases produced by Bacillus subtilis IH-72. The alkaline protease was strongly activated both by bivalent and monovalent cations such as Mg2+, Mn2+, Na+ and K+. The enzyme activity was considerably enhanced in the presence of fructose, galactose, glucose and mannitol. The enzyme was stabilized up to 10 days by immobilization on activated charcoal and was efficiently stabilized up to 2 months by lyophilization. The enzyme remained stable up to 19 days both at 4 degrees C and 30 degrees C in the presence of Mn2+. However, it exhibited significant stability up to 22 days at 4 degrees C and 30 degrees C in the presence of fructose, galactose and polyethylene glycol.