Antimicrobial Substance Produced by Pseudomonas aeruginosa Isolated from Slaughterhouse Sediment: Physicochemical Characterization, Purification, and Identification

This study aimed to produce the novel bacteriocin from Pseudomonas aeruginosa 43. The bacteriocin was purified through 80% ammonium sulfate precipitation, cation exchange chromatography, and gel filtration, and the specific antimicrobial activity was 400 AU/ml of protein. The molecular weight of purified bacteriocin was 10 kDa determined by SDS-PAGE. It was shown to be heat stable at 121 °C for 30 min and functioned well at low pH in a range of 3–7. Reduction of activity was shown after treatment with proteinase K, trypsin, papain, and α-amylase that confirmed its proteinaceous nature. Bacteriocin also showed its stability against various organic solvents and chemical reagents. Scanning electron microscope analysis indicated that bacteriocin from P. aeruginosa 43 damaged the morphology of methicillin-resistant Staphylococcus aureus (MRSA). Also, the novel bacteriocin exhibited an enhanced ability to impair biofilm formation and to reduce the density of established biofilms. LC–MS analysis study showed elastase is a novel peptide produced by P. aeruginosa 43 which has broad spectrum of inhibition against MRSA. The study suggested that bacteriocin from P. aeruginosa 43 could be developed as a antimicrobial agent for skin infection.