PURIFICATION AND CHARACTERIZATION OF ANTI-BACTERIAL BACTERIOCIN ISOLATED FROM HOSPITAL ACQUIRED MULTI DRUG RESISTANT Staphylococcus aureus

Concerns for public health have been raised all over the world as a result of a significant increase in bacterial resistance to the antibiotics that are currently available. As a result, antimicrobial peptides (AMPs) have emerged as a promisingly novel class of infectious disease treatment options. The current study focuses on the isolation and purification of a bacteriocin from clinically Multi-Drug Resistant Staphylococcus aureus (HA MRSA_1) that was acquired in a hospital including characterization. The ribosomally synthesized peptides have significant potential as an anti-bacterial peptide, and it was demonstrated that the bacteriocin has strong antagonistic activity against many pathogenic organisms. Ammonium sulfate precipitation, dialysis, Gel filtration chromatography, RP-HPLC, and SDS-PAGE were the initial methods used to purify it. A combination of LCMS analysis and Mass matrix-assisted laser desorption/ionization-mass spectrometry (MALDI TOF/MS) was used. The physio-chemical characterization of purified bacteriocin was studied using FT-IR, and XRD. The LCMS analysis of the RP-HPLC-collected active component revealed the amino acid sequence of the purified peptide (bacteriocin). After being subjected to high-performance liquid chromatography, a peak was discovered with a retention time of 5.330 minutes. The amino acid of bacteriocin was identified by LCMS, and the query sequence shared a match with the Staphylococcus aureus protein. In-silico molecular docking study investigated the significant evidence for the role of bacteriocin identified from Multi-Drug Resistant Staphylococcus aureus as an anti-bacterial agent. In conclusion, the bacteriocin found in this study may be a promising agent that should be further investigated for it’s cytotoxicity and in-vivo anti-bacterial activity in the future.