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- W4366998346 abstract "Antibacterial peptides can be released from yak milk casein. To date, the amino acid sequences and mechanism of action of yak casein-derived antibacterial peptides remain unknown. The current study identified antibacterial peptides from yak casein and their molecular mechanism of action. Our results showed that yak α-casein, β-casein, and κ-casein could be effectively hydrolyzed by Flavourzyme (Solarbio Science and Technology Co. Ltd.), and the 2-h hydrolysate showed the highest antibacterial rate of 43.07 ± 2.59% against Staphylococcus aureus. The 1,000 to 3,000 Da fraction accounted for 23.61% of the 2-h hydrolysate and had an antibacterial rate of 62.64 ± 4.40%. Three novel peptides with antibacterial activity were identified from this fraction, and the β-casein-derived peptide APKHKEMPFPKYP showed the strongest antibacterial effect (half-maximal inhibitory concentration = 0.397 mg/mL). Molecular docking predicted that APKHKEMPFPKYP interacted with 2 important enzymes of Staph. aureus, dihydrofolate reductase and DNA gyrase, through hydrophobic, hydrogen bonding, salt bridge, and π-π stacking interactions. Our findings suggest that the yak casein-derived peptides may serve as a potential source of natural preservatives to inhibit Staph. aureus." @default.
- W4366998346 created "2023-04-27" @default.
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- W4366998346 date "2023-06-01" @default.
- W4366998346 modified "2023-10-09" @default.
- W4366998346 title "Identification and molecular mechanism of action of antibacterial peptides from Flavourzyme-hydrolyzed yak casein against Staphylococcus aureus" @default.
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- W4366998346 doi "https://doi.org/10.3168/jds.2022-22823" @default.
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