Characterization of novel amylase-sensitive, anti-listerial Class IId bacteriocin, agilicin C7 produced by Ligilactobacillus agilis C7

Among various biological agents, bacteriocins are important candidates to control which is a foodborne pathogen. In this study, a novel bacteriocin, named agilicin C7, was isolated from C7 showing inhibitory activity against . Agilicin C7 biosynthesis gene was characterized by bioinformatics analyses and heterologously expressed in for further study. The anti-listeria activity of recombinant agilicin C7 (r-agilicin C7) was lost by proteases and α-amylase, suggesting that agilicin C7 is a glycoprotein. r-Agilicin C7 has wide pH and thermal stability and is also stable in various organic solvents. It destroyed by damaging the integrity of the cell envelope. These properties of r-agilicin C7 indicate that agilicin C7 is a novel amylase-sensitive anti-listerial Class IId bacteriocin. Physicochemical stability and inhibitory activity against of r-agilicin C7 suggest that it can be applied to control in the food industry, including dairy and meat products.