Isolation, Purification and Characterization of New Cold Active Subtilisin-like Protease from Bacillus sp. strain EL-GU1

Abstract

One of the important hydrolytic enzymes are proteases that slice peptide bonds between amino acid residues.Proteases have various industrial applications including detergent, food, pharmaceutical, leather and diagnosticreagent industries. Among them, the most commercialized enzymes are alkaline proteases in the industry. Due totheir potential applications in the detergent industry as cleaning additives, they are of particular interest. In thisstudy, a novel protease from Bacillus sp. strain EL-GU1 was reported showing highest activity at pH 6 and20°C. The novel protease was purified by using ammonium sulfate precipitation and identified by 16S rDNAsequencing. Highest activity was observed as 3300 µmol/min-1mg-1 when casein used as a substrate. Kineticparameters of the enzyme were determined; KM, Vmax, kcat and catalytic efficiency values were calculated as 1.4mM, 1 mM/s, 2.10-7s-1, 0.14 10-7s-1M-1, respectively. These results indicated that the novel cold active proteasefrom Bacillus sp. strain EL- GU1 can be a good candidate for the detergent industry.