The objective of the present study was to evaluate the stability of low-molecular-weight peptides after their incorporation into fermented sausages. Peptide fractions were produced from the bovine liver peptides (BLP) by enzymatic hydrolysis. Optimal conditions were identified as hydrolysis at 45 °C for 24 h, resulting in the generation of <3 kDa and <10 kDa peptide fractions exhibiting the highest antioxidant activity. The antioxidant potential of fermented sausages made from beef meat containing BLPs at 0.5% and 1% concentrations was assessed during manufacturing and storage. The initial antioxidant activity values of the sausages containing BLPs were higher than that of the control. Furthermore, the stability of the peptides in the sausages was demonstrated by their preserved antioxidant activity for 102 days. Peptides extracted from 1% of <10 kDa-peptide containing sausages possessed two-fold higher radical scavenging activity than control. The highest peptide concentration in the sausages containing 1% of <10 kDa-peptides (79.32±1.34–101.56±1.22 μg peptide/mg) was maintained from day 0 to day 102. The SDS-PAGE profile of myofibrillar proteins and peptide extracts revealed the degradation of proteins were delayed in <10 kDa of peptide added sausages, suggesting that the protein oxidation was slowed down. These results contribute to the advancement of peptide commercialization as functional ingredients in fermented food products. Furthermore, our research sheds light on the enduring impact of fermentation on the stability of the added peptides and the synergistic interactions between naturally produced peptides during fermentation and those introduced externally.
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