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Title

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

AuthorsPalma-Albino, Cleni; Intiquilla, Arturo; Jiménez-Aliaga, Karim; Rodríguez-Arana, Nathaly; Solano, Estela; Flores, Eduardo CSIC ORCID; Zavaleta, Amparo I.; Izaguirre, Víctor; Hernández-Ledesma, Blanca CSIC ORCID
KeywordsErythrina edulis
Multifunctional peptides
Legume proteins
Sequential enzymatic digestion
Issue Date2021
PublisherMultidisciplinary Digital Publishing Institute
CitationAntioxidants 10(11): 1722 (2021)
AbstractMultifunctional peptides, capable of acting on different body systems through multiple mechanisms of action, offer many advantages over monofunctional peptides, including lower adverse 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 antioxidant, 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.
DescriptionThis article belongs to the Special Issue Anti-Inflammatory and Antioxidant Advances on Bioactive Compounds Derived from Plants and Foods in Honor of Professor Carlo Franchini on the Occasion of His Retirement.
Publisher version (URL)https://doi.org/10.3390/antiox10111722
URIhttp://hdl.handle.net/10261/262570
DOI10.3390/antiox10111722
E-ISSN2076-3921
Appears in Collections:(CIAL) Artículos




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