Isolation and characterization of a protease from Bacillus sps

Abstract

Abstract Proteases are highlighted group of enzymes which corresponds to approximately 60% of enzymes used globally in commercial applications. Present study describes isolation of a new protease from TSA5 strain. Sequencing of 16SrRNA revealed identity to Bacillus sps with common five restriction sites (Acc651, Btscl, Fok1, Plel, Kpnl). The enzyme from TSA5 strain partial purified by, salting and dialysis which resulted a homogeneity of 6-fold with the yield of 34%. Enzyme activity was characterised for a broad range of pH (4–10.5) and temperature (0–120 °C). Optimum activity was observed at pH 8.5 and 80 °C. The enzyme showed substrate specificity to casein. The effect of different solvents and chemicals were assayed. It is found to be more active in presence of polar solvents. EDTA (Ethylenediaminetetraacetic acid) and β-mercaptoethanol shows potent inhibition. The purified fraction showed silver recovery from X-ray films. The protease also exhibited detergent activity and antibacterial property suggesting the use of enzymes for enzyme hydrolysis in industries for commercial applications.