Bacillus cereus is a common foodborne pathogen that can not only contaminate various foods and cause diseases, but is also hard to eliminate during production and processing, necessitating effective methods to inhibit it.This study aimed to investigate the biological characteristics of the antimicrobial peptide Temporin L and its antibacterial activity and mechanism against B.cereus.Firstly, the biological characteristics of Temporin L were predicted using online bioinformatics software.Then, the antibacterial activity and stability of B.cereus under different conditions were determined by the microbroth method.Finally, scanning electron microscope and molecular docking analysis revealed the mechanism of action against B.cereus.Results showed that Temporin L was a small molecule, positively charged, stable, and non-toxic hydrophobic polypeptide with extended chains.Temporin L did not have transmembrane regions or signal peptides, and 11 proteases could cleave it.In addition, Temporin L exhibited strong antibacterial activity against B.cereus, with minimum inhibitory concentration (MIC) and minimum bactericidal concentration of 8 μmol/L and 16 μmol/L, respectively.Temporin L maintained its antibacterial efficacy (MIC remained at 8 μmol/L) under varying environmental conditions (temperature, ultraviolet rays, pH, metal ions).Further analysis revealed that Temporin L could change the morphology of B.cereus.At the same time, Temporin L could produce good binding energy to DNA and phospholipase C through the formation of hydrogen bonds and hydrophobicity.In summary, Temporin L not only exhibits good biological properties, but also effectively inhibits the growth of B.cereus, and its excellent stability makes it expected to become a new type of food preservative.
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