The identification of novel natural sources of bioactive peptides with multifunctional health-promoting properties remains a major challenge for the development of nutraceutical and therapeutic agents. Prosopis laevigata (mesquite), a plant of economic, medicinal, and nutritional relevance in Mexico, has been poorly explored as a source of protein-derived bioactive molecules. Therefore, this study evaluated the antioxidant, antimicrobial, cytotoxic, and enzymatic inhibitory activities of peptides obtained from the enzymatic hydrolysis of P. laevigata cotyledon proteins. The resulting hydrolysates exhibited significant antioxidant activity, for peptide fractions smaller and larger than 5 kDa, in the ABTS and FRAP assays. Cytotoxic activity against HepG2 liver cancer cells was observed at high peptide concentrations (8 mg/mL). Additionally, the peptides inhibited the growth of Staphylococcus aureus but showed no activity against Escherichia coli. The peptides also displayed partial inhibition of α-amylase activity, with peptides 5 kDa showing a mixed inhibition pattern. Overall, these findings highlight P. laevigata seeds as a promising source of multifunctional bioactive peptides with potential applications in functional foods and health-related biotechnological developments.
Sanchez-Jimenez et al. (Fri,) studied this question.