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Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides
Multifunctional 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 whic...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8615073/ https://www.ncbi.nlm.nih.gov/pubmed/34829593 http://dx.doi.org/10.3390/antiox10111722 |
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author | Palma-Albino, Cleni Intiquilla, Arturo Jiménez-Aliaga, Karim Rodríguez-Arana, Nathaly Solano, Estela Flores, Eduardo Zavaleta, Amparo Iris Izaguirre, Víctor Hernández-Ledesma, Blanca |
author_facet | Palma-Albino, Cleni Intiquilla, Arturo Jiménez-Aliaga, Karim Rodríguez-Arana, Nathaly Solano, Estela Flores, Eduardo Zavaleta, Amparo Iris Izaguirre, Víctor Hernández-Ledesma, Blanca |
author_sort | Palma-Albino, Cleni |
collection | PubMed |
description | Multifunctional 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 FeSO(4)-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. |
format | Online Article Text |
id | pubmed-8615073 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-86150732021-11-26 Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides Palma-Albino, Cleni Intiquilla, Arturo Jiménez-Aliaga, Karim Rodríguez-Arana, Nathaly Solano, Estela Flores, Eduardo Zavaleta, Amparo Iris Izaguirre, Víctor Hernández-Ledesma, Blanca Antioxidants (Basel) Article Multifunctional 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 FeSO(4)-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. MDPI 2021-10-28 /pmc/articles/PMC8615073/ /pubmed/34829593 http://dx.doi.org/10.3390/antiox10111722 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Palma-Albino, Cleni Intiquilla, Arturo Jiménez-Aliaga, Karim Rodríguez-Arana, Nathaly Solano, Estela Flores, Eduardo Zavaleta, Amparo Iris Izaguirre, Víctor Hernández-Ledesma, Blanca Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides |
title | Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides |
title_full | Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides |
title_fullStr | Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides |
title_full_unstemmed | Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides |
title_short | Albumin from Erythrina edulis (Pajuro) as a Promising Source of Multifunctional Peptides |
title_sort | albumin from erythrina edulis (pajuro) as a promising source of multifunctional peptides |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8615073/ https://www.ncbi.nlm.nih.gov/pubmed/34829593 http://dx.doi.org/10.3390/antiox10111722 |
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