In recent years, several studies have shown the antioxidant and antihypertensive potential of bioactive peptides. Thus, bioactive peptides are likely to be a valuable substance for the development of functional foods. There are a wide variety of sources of these peptides, including several cereals. Teff is an Ethiopian-rooted cereal with an interesting nutritional profile, mainly due to its high amount of protein. In this study, teff flour was subjected to a defatting process for optimizing the protein extraction. Such extraction was performed by precipitation from its isoelectric point, a crucial step that separates the protein from other components based on their charge. The protein obtained was subjected to enzymatic hydrolysis by pepsin and Cynara cardunculus L. The antihypertensive (angiotensin-I-converting enzyme ―ACE-I― inhibitory activity) and antioxidant activity (2,2-diphenyl-1-picrylhydrazyl ―DPPH― radical scavenging activity) of the peptides were determined. According to the IC₅₀ values, the results obtained showed that the peptides from teff flour show promising bioactivity compared to other cereals. Furthermore, the peptides from teff flour obtained from C. cardunculus L. showed higher antioxidant activity (defatted teff flour ―DTF―: 0.59 ± 0.05; protein extract ―EP― : 1.04 ± 0.11) than those obtained with pepsin (DTF: 0.87 ± 0.09; EP: 1.73 ± 0.11). However, C. cardunculus L. hydrolyzate peptides showed lower inhibitory activity of ACE-I (DTF: 0.59 ± 0.07; EP: 0.61 ± 0.05) than the pepsin hydrolyzate (DTF: 0.15 ± 0.02; EP: 0.33 ± 0.05).

The bioactive potential of dairy-derived peptides has attracted increasing interest due to their capacity to exert antioxidant and antihypertensive effects. This study investigated three artisanal cheeses manufactured with animal rennet (CTRL), Onopordum platylepis extract (OP), or a mixture of both coagulants (AR/OP) to compare their peptide profiles and associated bioactivities. Water-soluble extracts were analyzed to identify precursors and released bioactive peptides, and in vitro assays were performed to assess antioxidant activity and angiotensin-converting enzyme (ACE) inhibition. The analysis of precursors suggested a predominance of antioxidant sequences in CTRL and ACE-inhibitory precursors in OP, with AR/OP showing intermediate values. However, direct peptide identification confirmed that the AR/OP mixture produced a wider range of peptides with antioxidant activity, while OP and AR/OP exhibited similarly high levels of ACE-inhibiting peptides. These results were consistent with in vitro assays, which confirmed AR/OP as the most active sample for antioxidant potential and OP, closely followed by AR/OP, as the strongest for ACE inhibitory activity. Overall, the integration of precursor analysis, peptide identification, and experimental validation highlights the influence of the coagulant on the generation of bioactive peptides, suggesting that the use of Onopordum platylepis Murb. (O. platylepis) alone or in combination with animal rennet may enhance the functional properties of cheese.