Lactoferrin and Its Enzymatic Hydrolysates as Natural Antimicrobial and Antioxidant Agents for Food Preservation

Lactoferrin (Lf) and Lf-derived peptides are multifunctional milk components with potential applications in food preservation due to their antibacterial and antioxidant properties. In this study, the antibacterial and antioxidant activities of bovine lactoferrin and Lf-derived peptides obtained by enzymatic hydrolysis with pepsin, trypsin, and chymotrypsin were evaluated. Antibacterial activity was assessed against four foodborne pathogens and spoilage microorganisms (Escherichia coli, Listeria monocytogenes, Staphylococcus epidermidis, and Latilactobacillus sakei), while antioxidant activity was determined using four complementary assays. Lf showed stronger antibacterial activity than the corresponding hydrolysates against all tested strains, while the hydrolysates notably inhibited Listeria monocytogenes and Latilactobacillus sakei. Both Lf and its peptides showed lower antioxidant capacity than Trolox, although native Lf and its peptides markedly inhibited lipid peroxidation. Lf peptides demonstrated greater antioxidant activity in the superoxide scavenging and FRAP assays. Low-molecular-weight peptides (<10 kDa) contributed most to antioxidant activity, while mass spectrometry analysis revealed peptide sequences rich in hydrophobic and electron-donating amino acid residues, providing mechanistic insight into the observed activities. Overall, these findings highlight the potential of lactoferrin and its enzymatic hydrolysates as natural antimicrobial and antioxidant agents for food preservation.