SPECIFIC ACTIVITY AND MOLECULAR CHARACTERIZATION OF PROTEASE OF BOTH WILD AND MUTANT STRAINS OF BACILLUS SUBTILISJ. KASTHURI AND K. DHANALAKSHMI
The Bacillus subtilis isolated from the soil samples was grown in LB broth. The enzyme protease was recovered and assayed for its protein content and specific activity at various levels of purification. Of which, the ion exchange chromatographic sample seemed to be a highly purified form when compared to the other two samples. On further experimentation it showed an optimal activity at 65°C and pH 7. Further, Ca, Mg ++ and EDTA seemed to activate the specific activity of protease at optimized temperature and pH; whereas HgC1, and FeCl, showed inhibitory effect. The strain was then improved by UV exposure and the one exposed to 15 min showed the highest activity (0.186 U/mL). Besides, the protease of both wild and mutant strains revealed the molecular weight 28,000 and 38,000 D respectively. Thus the mutant strain seemed to be the superior.
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