Abstract
In this study, the antimicrobial activity of milk-derived peptide αS2-casein151-181 against Bacillus subtilis ATCC6633 was evaluated. The minimum inhibitory concentration of αS2-casein151-181 against B. subtilis was between 3.10 and 6.67 μm and the minimum bactericidal concentration was below 16.00 μm. Peptide αS2-casein151-181 generated pores in the cytoplasmic membrane of B. subtilis and resulted in PI uptake and leakage of cell constituents. Treatment with αS2-casein151-181 also caused a loss of membrane potential as measured by DiOC2 fluorescence. These data suggest that αS2-casein151-181 kills B. subtilis through the disruption of cell membrane, allowing cell constituents to leak out of the cell, which is followed by a loss of membrane potential and cell death. Furthermore, αS2-casein151-181 also acted against B. subtilis spores (1 × 106 spores mL−1) with an IC50 and an IC90 of 8.07 μm and 16.22 μm, respectively.
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