Albumin from erythrina edulis (Pajuro) as a promising source of multifunctional peptides

Cleni Palma-Albino, Arturo Intiquilla, Karim Jiménez-Aliaga, Nathaly Rodríguez-Arana, Estela Solano, Eduardo Flores, Amparo Iris Zavaleta, Víctor Izaguirre, Blanca Hernández-Ledesma

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Multifunctional peptides, capable of acting on different body systems through multiple mechanisms of action, offer many advantages over monofunctional peptides, including lower ad-verse side effects and costs. Erythrina edulis (pajuro) is a legume with a large number of high-quality proteins, of which their potential as a source of antioxidant peptides has been recently reported. In this study, the behavior of these proteins under a sequential enzymatic hydrolysis with digestive and microbial enzymes was investigated by evaluating the multi-functionality of the hydrolyzates. The albumin hydrolyzates obtained after the action of pepsin, pancreatin, and Alcalase showed an-tioxidant, angiotensin-converting enzyme (ACE), α-amylase, α-glucosidase, and dipeptidyl peptidase (DPP)-IV inhibitory activities. The radical scavenging properties of the hydrolyzate could be responsible for the potent protective effects observed in FeSO4-induced neuroblastoma cells. The findings support the role of pajuro protein as an ingredient of functional foods or nutraceuticals for health promotion and the prevention of oxidative stress, hypertension, and metabolic alteration-associated chronic diseases.

Original languageEnglish
Article number1722
Issue number11
StatePublished - Nov 2021
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.


  • Erythrina edulis
  • Legume proteins
  • Multifunctional peptides
  • Sequential enzymatic digestion


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