Anti-inflammatory activity of a serine protease produced from Bacillus pumilus SG2

Proteases have appreciable anti-inflammatory activity and proteolytic enzymes from diverse sources have been studied for their anti-inflammatory potential. This study investigated the anti-inflammatory activity of a protease isolated from Bacillus pumilus SG2 using in-vitro models such as heat and hypotonicity induced hemolysis and protein denaturation. The activity exhibited by SG2 protease was comparable to that exhibited by the standard drug diclofenac. The IC 50 value of SG2 protease for inhibition of heat induced hemolysis was calculated to be 226 μg while that of diclofenac was 215 μg The IC 50 value for both protease and diclofenac for the inhibition of hypotonicity induced hemolysis was 85 μg. The IC 50 value of SG2 protease for the inhibition of protein denaturation was 247 μg while that of diclofenac was 181 μg. The structure of SG2 protease was deduced using online tools. The enzyme had a signal peptide of 31 amino acids and a pro-peptide of 77 amino acids. The mature protein consisted of 298 amino acids. The catalytic triad, oxyanion hole and secondary structure of SG2 protease was also studied. Thus a protease with anti-inflammatory potential was studied and was structurally characterized, the details of which may help in engineering the enzyme.