Design, expression and characterization of lactiscin—A novel broad-spectrum peptidic bacteriocin

Bacteria-derived antimicrobial peptides known as peptidic bacteriocins offer a promising alternative to traditional antibiotics in the face of emergence multidrug-resistant bacteria. Here, nucleotide sequence gene encoding Lactococcus lactis-derived bacteriocin designated lactiscin selectively identified from GenBank® database was synthesized with an added 6⋅His and cloned into Escherichia coli. Upon low-temperature expression at 16 °C, His-tagged peptide could be produced both soluble form insoluble inclusions. Efficient purification achieved via immobilized-Ni2+ affinity chromatography (IMAC) its estimated molecular mass ∼13.4 kDa determined by tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified highly active against Gram-positive Gram-negative bacteria it exhibited minimal inhibitory concentration 0.45 mg/mL, 0.15 0.35 mg/mL against. coli, Vibrio parachemolyticus, Staphylococcus aureus Micrococcus luteus, respectively. In addition, still retained activity over pH range 3.0–12.0 heat stability 100 °C for 30 min. A membrane integrity study revealed that this able induce E. coli permeabilization concentration-dependent manner, albeit showed negligible toxic effect on erythrocytic cells. Gel retardation assay demonstrated suppress migration genomic DNA extracted pathogenic bacteria, suggesting presence bacteriocin-responsive binding genomic. Our findings lactiscin—a novel broad-spectrum would valuable additive application food industry potential bio-preservative.