Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein
Oxidative reactions are responsible for the changes in quality during food processing and storage. [Background] Oxidative stress is also involved in multiple chronic diseases, such as cardiovascular and neurodegenerative disorders, diabetes, cancer, and aging. The consumption of dietary antioxidants has been demonstrated to help to reduce the oxidative damage in both the human body and food systems. In this study, the potential of Erythrina edulis (pajuro) protein as source of antioxidant peptides was evaluated.
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Format: | artículo biblioteca |
Language: | English |
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John Wiley & Sons
2019
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Subjects: | Erythrina edulis, Alcalase hydrolysis, Antioxidant activity, Bioactive peptides, |
Online Access: | http://hdl.handle.net/10261/193618 http://dx.doi.org/10.13039/501100003329 |
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dig-cial-es-10261-1936182019-10-29T02:15:51Z Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein Intiquilla, Arturo Jiménez-Aliaga, Karim Guzmán, Fanny Alvarez, Claudio A. Zavaleta, Amparo I. Izaguirre, Víctor Hernández-Ledesma, Blanca Ministerio de Economía y Competitividad (España) Fondo Nacional de Desarrollo Científico, Tecnológico y de Información Tecnológica (Perú) Jiménez-Aliaga, Karim [0000-0001-8234-8358] Hernández-Ledesma, Blanca [0000-0001-7192-6044] Erythrina edulis Alcalase hydrolysis Antioxidant activity Bioactive peptides Oxidative reactions are responsible for the changes in quality during food processing and storage. [Background] Oxidative stress is also involved in multiple chronic diseases, such as cardiovascular and neurodegenerative disorders, diabetes, cancer, and aging. The consumption of dietary antioxidants has been demonstrated to help to reduce the oxidative damage in both the human body and food systems. In this study, the potential of Erythrina edulis (pajuro) protein as source of antioxidant peptides was evaluated. [Results] Pajuro protein concentrate hydrolyzed by alcalase for 120 min showed potent ABTS·+ and peroxyl radical scavenging activity with Trolox equivalent antioxidant capacity (TEAC) and oxygen radical absorbance capacity (ORAC) values of 1.37 ± 0.09 µmol TE mg-1 peptide and 2.83 ± 0.07 µmol TE mg-1 peptide, respectively. Fractionation of the hydrolyzate to small peptides resulted in increased antioxidant activity. De novo sequencing of most active fractions collected by chromatographic analysis enabled 30 novel peptides to be identified. Of these, ten were synthesized and their radical activity evaluated, demonstrating their relevant contribution to the antioxidant effects observed for pajuro protein hydrolyzate. [Conclusions] The sequences identified represent an important advance in the molecular characterization of the pajuro protein, demonstrating its potential as a source of antioxidant peptides for food and nutraceutical applications. This work has received financial support from projects 186-FINCyT-IA-2013 (Programa Nacional de Innovación para la Competividad y Productividad) (Innovate-Peru), N∘ 007-FONDECYT-2014 (Fondo Nacional de Desarrollo Científico, Tecnológico y de Innovación Tecnológica-Peru), and AGL2015-66886-R (Ministry of Economy and Competitiveness, MINECO, Spain). Peer reviewed 2019-10-28T13:57:25Z 2019-10-28T13:57:25Z 2019 artículo http://purl.org/coar/resource_type/c_6501 Journal of the Science of Food and Agriculture 99(5): 2420-2427 (2019) 0022-5142 http://hdl.handle.net/10261/193618 10.1002/jsfa.9449 1097-0010 http://dx.doi.org/10.13039/501100003329 30362128 en #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2015-66886-R https://doi.org/10.1002/jsfa.9449 Sí none John Wiley & Sons |
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Erythrina edulis Alcalase hydrolysis Antioxidant activity Bioactive peptides Erythrina edulis Alcalase hydrolysis Antioxidant activity Bioactive peptides |
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Erythrina edulis Alcalase hydrolysis Antioxidant activity Bioactive peptides Erythrina edulis Alcalase hydrolysis Antioxidant activity Bioactive peptides Intiquilla, Arturo Jiménez-Aliaga, Karim Guzmán, Fanny Alvarez, Claudio A. Zavaleta, Amparo I. Izaguirre, Víctor Hernández-Ledesma, Blanca Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein |
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Oxidative reactions are responsible for the changes in quality during food processing and storage. [Background] Oxidative stress is also involved in multiple chronic diseases, such as cardiovascular and neurodegenerative disorders, diabetes, cancer, and aging. The consumption of dietary antioxidants has been demonstrated to help to reduce the oxidative damage in both the human body and food systems. In this study, the potential of Erythrina edulis (pajuro) protein as source of antioxidant peptides was evaluated. |
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Ministerio de Economía y Competitividad (España) |
author_facet |
Ministerio de Economía y Competitividad (España) Intiquilla, Arturo Jiménez-Aliaga, Karim Guzmán, Fanny Alvarez, Claudio A. Zavaleta, Amparo I. Izaguirre, Víctor Hernández-Ledesma, Blanca |
format |
artículo |
topic_facet |
Erythrina edulis Alcalase hydrolysis Antioxidant activity Bioactive peptides |
author |
Intiquilla, Arturo Jiménez-Aliaga, Karim Guzmán, Fanny Alvarez, Claudio A. Zavaleta, Amparo I. Izaguirre, Víctor Hernández-Ledesma, Blanca |
author_sort |
Intiquilla, Arturo |
title |
Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein |
title_short |
Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein |
title_full |
Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein |
title_fullStr |
Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein |
title_full_unstemmed |
Novel antioxidant peptides obtained by alcalase hydrolysis of Erythrina edulis (pajuro) protein |
title_sort |
novel antioxidant peptides obtained by alcalase hydrolysis of erythrina edulis (pajuro) protein |
publisher |
John Wiley & Sons |
publishDate |
2019 |
url |
http://hdl.handle.net/10261/193618 http://dx.doi.org/10.13039/501100003329 |
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