A new bacillolycin with serin-protease nature is inhibited by cupper

In this study, it is aimed to search for new proteases with novel properties from bacteria and to characterise the properties of the enzyme. The best protease producing microorganisms was isolated from soil and characterised by 16 s rDNA sequence analysis. A 33 kDa molecular weight bacillolycin metallo–serine protease from newly isolated Bacillus sp. BHC01 was purified 2.6–fold with a final 38,617.0 ± 1013.7 U/mg protein specific activity. Optimum reaction temperature and pH of the enzyme was found to be 50° C and pH 7.5, respectively. Fe2+, N+, Co2+ and Mg2+ ions were detected as activators, and Cu2+ metal ions was observed as inhibitors. The kinetic constants of the enzyme Km and Vmax is measured as 0.574 mg/mL, 338.1 mmol/ml.min, respectively. Because ethylenediaminetetraacetic acid (EDTA) and phenylmethylsulfonyl fluoride (PMSF), both inhibit the enzyme, it is concluded that this enzyme is a mixed catalytic type peptidase which has metals in active site and also has some serine residues in order to reach an active folding.