蜡样芽孢杆菌
抗菌剂
肽
单核细胞增生李斯特菌
枯草芽孢杆菌
抗菌肽
微生物学
大肠杆菌
化学
金黄色葡萄球菌
肠沙门氏菌
细菌
生物化学
生物
遗传学
基因
作者
Elahe Omidbakhsh Amiri,Jamshid Farmani,Zeynab Raftani Amiri,Ali Dehestani,Mojtaba Mohseni
标识
DOI:10.1016/j.ijfoodmicro.2021.109403
摘要
αs165-181 is a peptide derived from αs2-casein of ovine milk. Herein, we report the antimicrobial activity and mechanism, and food application of the peptide. αs165-181 showed antimicrobial activity against Escherichia coli, Staphylococcus aureus, Bacillus subtilis, Listeria monocytogenes, Bacillus cereus, and Salmonella enterica serovar Enteritidis in a dose-dependent manner. The minimum inhibitory concentration of the peptide was 3.9 mg/ml for E. coli and 7.8 mg/ml for the other bacteria. The peptide did not show antimicrobial activity against Lactobacillus plantarum up to 3.9 mg/ml concentration. The minimum bactericidal concentration of αs165-181 peptide was 7.8 mg/ml for E. coli, S. aureus, L. monocytogenes, and B. cereus. The peptide was sensitive to monovalent and divalent cations, pH, and high temperatures. Transmission electron microscopy, cytoplasmic β-galactosidase leakage, and DNA electrophoresis analyses showed that αs165-181 peptide affects bacteria by damaging cell membrane and binding to the genomic DNA. When αs165-181 peptide was applied to minced beef or UHT cream, the antimicrobial activity (7.8 mg/g) was almost the same as or even better than nisin (0.5 mg/g). This study helps understand the antimicrobial mode of action of αs165-181 peptide and develop strategies for application in food products.
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