Erythrina edulis (pajuro) seed protein: A new source of antioxidant peptides

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

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


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.

Original languageEnglish
Pages (from-to)781-786
Number of pages6
JournalNatural Product Communications
Issue number6
StatePublished - Jun 2016


  • Antioxidant activity
  • Enzymatic hydrolysis
  • Erythrina edulis
  • Peptide
  • Radical scavenging activity


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