Erythrina edulis (Pajuro) seed protein: a new source of antioxidant peptides.

Intiquilla, Arturo; Jiménez-Aliaga, Karim; Zavaleta, Amparo Iris; Arnao, Inés; Peña, Carmen; Chávez-Hidalgo, Elizabeth L; Hernández-Ledesma, Blanca

Natural Products Communications 11,781-786.

Resumen
Erythrina edulis Triana ex Micheli is a protein-enriched legume traditionally used for both dietary and medicinal purposes. In this paper, protein concentrate was obtained from the seed flour. SDS-PAGE analysis revealed a high number and intensity of bands in the range between 10 and 90 kDa. Neutrase, Flavourzyme, and Alcalase were used to hydrolyze the protein concentrate at different times. By SDS-PAGE, the lower resistance of proteins to Alcalase action was observed, providing
hydrolyzates with higher radical scavenging activity. The 120 min-hydrolyzate showed ORAC and TEAC values of 2.51 and 0.91 μmol Trolox equivalents/mg of protein, respectively. A fraction lower than 3 kDa and rich in hydrophobic and aromatic amino acids was demonstrated to be mainly responsible for the observed activity. E. edulis could be a new alternative in the formulation of functional foods not only for its high protein content but also for the potential biological properties
of its hydrolyzates.