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L. casei HZ1 was identified from Chinese traditional fermented milk, and angiotensin converting enzyme inhibitory peptide was separated from its culture in our previous work. Here, LGH2 was a novel AMP, identified from the genome of L. casei HZ1. Altogether, roughly 52.76% of LGH2 was α-helical, with the remainder in β-strand and random coil in 50% TFE solution tested by CD. The peptide was also an amphipathic and cationic molecule, which was composed of 20 amino acid residues. The similarity of the amino acid sequence between LGH2 and Temporin-RN3 was highest. Then, the peptide successfully expressed in E. coli Rossetta (DE3) pLysS using the SUMO fusion expression system and purified by chromatography technologies. The molecular weight of the peptide was 2448 Da determined by MALDI-TOF MS. Antimicrobial tests showed that the peptide has strong activities against G+ bacteria, special for S. aureus (MIC = 4 μM). The toxicity assay showed that the peptide exhibits a low hemolytic activity against sheep red blood cells. The antimicrobial mechanisms of LGH2 against pathogens were further investigated by dye leakage, CLSM, SEM, and FCM assays. We found that LGH2 can bind to the cell membrane, and destroy its integrity. These significant results indicate that LGH2 has great potential to treat the infections caused by pathogenic bacteria such as S. aureus, and it provides a new template to improve antimicrobial peptides targeting antibiotic-resistant pathogenic bacteria.

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