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Antibacterial activity and its mechanisms of a recombinant Funme peptide against Cronobacter sakazakii in powdered infant formula
- Chen, Yong, Zhang, Yifan, Wang, Xiaohou, Ling, Jianqun, He, Guanghua, Shen, Lirong
- Food research international 2019 v.116 pp. 258-265
- Cronobacter sakazakii, ampicillin, antibacterial properties, antimicrobial peptides, bacteria, beta-galactosidase, biofilm, cell walls, cesium, cytotoxicity, erythrocytes, food processing plants, infant formulas, minimum inhibitory concentration, permeability, scanning electron microscopy, transmission electron microscopy
- Cronobacter sakazakii (Cs) is a typical foodborne bacterium that infect powdered infant formula (PIF) worldwide. In this study, a recombinant antimicrobial peptide, branded as Funme peptide (FP)was applied to protect PIF from Cs contamination. The result from the antimicrobial activity assay showed that the minimum inhibitory concentration (MIC) of BMAP-27 peptide, FP and Ampicillin against Cs were 250.0, 125.0 and 15.6 μg/mL, respectively, indicating FP possessed higher MIC than that of Ampicillin, and lower MIC than that of BMAP-27. The minimum biofilm eradication concentration (MBEC) assay showed that FP at 2 × MIC (250.0 μg/mL) could completely eradicated Cs biofilms. The antibacterial activity of FP might be due to the increasing permeability and the release of cytoplasmic β-galactosidase of Cs. The results acquired from transmission electron microscopy and scanning electron microscopy indicated that FP induced the disruption and dysfunction of cell walls and membranes. Moreover, safety assay showed that FP had low cytotoxicity to human erythrocytes. The present study investigated the antibacterial effects and mechanisms of FP against Cs, providing promising evidence to apply this novel antimicrobial agent against Cs contamination in foods and food processing facilities.