Bacillus Protein as AntimicrobialCompounds: A Novel Strategy for Combating Pathogenic Bacteria

Abstract

Everywhere in the world, MRSA infections are increasing in frequency. As a result, antibiotics need to be replenished frequently in order to combat the illness. Previously operational members of Bacillus amyloliquefaciens have been reclassified using GyrB. The antibacterial activity of cell-free supernatants from the strains was tested using the spontaneous emulsification method (CFS).The CFS was examined for its MIC, MBC, and physical and chemical properties. The GyrB housekeeping gene was used to re-identify previously identified Bacillus-Amyloliquefaciens operational group members. The strains' cell-free supernatant (CFS) was evaluated using an agar well diffusion experiment. MIC, MBC, and physicochemical properties, as well as minimal inhibitory concentration, have all been assessed and confirmed (MIC). Results confirmed the accuracy of the MIC and MBC values at 125 l/ml When tested at various temperatures, pH levels, surfactants, and metal ions, the crude antibacterial extract proved bactericidal (MgCI2, NaCI2, ZnNO3, and CuSO4). After being the treated with peptidase K, the crude extract was found to be unstable. Peptides, which are small molecules, share several of these characteristics. The antibacterial component of the chosen strain was extracted using solvent extraction and silica gel column chromatography. High Performance Liquid Chromatography (HPLC) was used to analyse the purified anti-MRSA compound, which revealed a single peak. SDS-PAGE and a zymogram were used to determine the anti-MRSA drug's molecular weight. The antimicrobial peptide's molecular weight was estimated to be around 5 kDa. It may be possible to prevent MRSA infection in the future by using antimicrobial peptides produced by B. velezensis strain PD9.