Antimicrobial Substance Produced by Pseudomonas aeruginosa Isolated from Slaughterhouse Sediment: Physicochemical Charac
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Antimicrobial Substance Produced by Pseudomonas aeruginosa Isolated from Slaughterhouse Sediment: Physicochemical Characterization, Purification, and Identification Dhanam Selvam1 · Arumugam Thangarasu1 · Douglas J. H. Shyu2 · Rameshkumar Neelamegam3 · Krishnan Muthukalingan4 · Kayalvizhi Nagarajan1 Accepted: 28 October 2020 © Springer Nature B.V. 2020
Abstract 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. Keywords Pseudomonas aeruginosa · Methicillin-resistant Staphylococcus aureus (MRSA) · Cation exchange chromatography · Biofilm
Introduction A group of small antimicrobial peptides produced from bacteriocins was shown to have the ability to inhibit the growth of competitive bacterial strains (Hassan et al. 2012). The relatively narrow killing spectrum of bacteriocins and their antimicrobial mechanisms are distinct from traditional * Kayalvizhi Nagarajan [email protected] 1
Regenerative Medicine Laboratory, Department of Zoology, School of Life Sciences, Periyar University, Salem, Tamil Nadu 636011, India
2
Functional Genomics Lab, Department of Biological Science and Technology, National Pingtung University of Science and Technology, Neipu, Pingtung 91201, Taiwan
3
School of Life Sciences, Central University of Tamil Nadu, Thiruvarur, Tamil Nadu 610005, India
4
Madurai Kamaraj University, Madurai, Tamil Nadu 625 021, India
broad-spectrum antibiotics and the fact means that they may be used to replace traditional antibiotics (Cavera et al. 2015; Kaskoniene et al. 2017). For example, bacteriocins epidermin and gallidermin have been used to effectively treat skin infections (Kellner et al. 1988). The mechanism of action is classified into two classes for antimicrobial peptides. The first class of mechanism is divided into two types of membrane disruption. (1) Barrel stave or toroidal mechanism for transm
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