Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates

Whey is a highly polluting by-product of cheese processing. However, it has valuable nutritional properties since it is a rich and balanced source of proteins and amino acids. Therefore, it has a broad range of functional properties that can be exploited for diverse applications. Research has shown...

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Autores principales: Tovar-Jiménez, Xochitl, Téllez-Jurado, Alejandro, Gómez-Aldapa, Carlos Alberto, Mercado-Flores, Yuridia, Arana-Cuenca, Ainhoa
Formato: Online
Lenguaje:eng
Publicado: Universidad de Sonora 2021
Acceso en línea:https://biotecnia.unison.mx/index.php/biotecnia/article/view/1321
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spelling biotecnia-article-13212022-05-31T17:19:20Z Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates Hidrolizados enzimáticos con actividad antioxidante y antihipertensiva obtenidos del concentrado proteíco del suero lácteo bovino Tovar-Jiménez, Xochitl Téllez-Jurado, Alejandro Gómez-Aldapa, Carlos Alberto Mercado-Flores, Yuridia Arana-Cuenca, Ainhoa antioxidant peptides; antihypertensive peptides; protein concentrate from bovine whey; aspartyl protease of Sporisorium reilianum; commercial enzymes. péptidos antioxidantes, péptidos antihipertensivos, concentrado proteico del suero lácteo bovino, aspartil proteasa de Sporisorium reilianum, enzimas comerciales. Whey is a highly polluting by-product of cheese processing. However, it has valuable nutritional properties since it is a rich and balanced source of proteins and amino acids. Therefore, it has a broad range of functional properties that can be exploited for diverse applications. Research has shown how the enzymatic hydrolysis of whey proteins releases bioactive peptides. In the present study, the hydrolysis of whey protein concentrate (WCP) was performed using purified Sporisorium reilianum aspartyl protease (Eap1), commercial enzymes chymotrypsin (C) and trypsin (T), as well as different enzymatic combinations in order to determine which enzyme or combination allowed for the release of peptides presenting the highest antioxidant and antihypertensive activity levels; our results indicated that hydrolysis with Eap1 releases the best-performing peptides in comparison with individual enzymes and their combinations. El suero lácteo a pesar de ser considerado un desecho altamente contaminante de la industria quesera cuenta con importantes propiedades nutrimentales, ya que es una fuente rica y equilibrada en aminoácidos que presentan propiedades funcionales que pueden ser aprovechadas. Algunos estudios indican que la hidrólisis enzimática de las proteínas séricas permite liberar péptidos bioactivos. En este estudio se realizó la hidrólisis del concentrado proteico del suero lácteo (WCP) por acción de la aspartil proteasa purificada Sporisorium reilianum (Eap1), las enzimas comerciales quimotripsina (C), tripsina (T) y de la combinación enzimática de estas, con la finalidad de determinar que enzima permite liberar péptidos con mejor actividad antioxidante y antihipertensiva. Los resultados de la actividad biológica indicaron que la Eap1 libera péptidos con mejor actividad en comparación con las enzimas individuales y sus combinaciones. Universidad de Sonora 2021-02-19 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Original peer-reviewed articles Artículos originales evaluados por pares application/pdf text/xml https://biotecnia.unison.mx/index.php/biotecnia/article/view/1321 10.18633/biotecnia.v23i1.1321 Biotecnia; Vol. 23 No. 1 (2021): Enero-Abril; 161-169 Biotecnia; Vol. 23 Núm. 1 (2021): Enero-Abril; 161-169 1665-1456 1665-1456 eng https://biotecnia.unison.mx/index.php/biotecnia/article/view/1321/500 https://biotecnia.unison.mx/index.php/biotecnia/article/view/1321/541 Derechos de autor 2021 https://creativecommons.org/licenses/by-nc-sa/4.0
institution Biotecnia
collection OJS
language eng
format Online
author Tovar-Jiménez, Xochitl
Téllez-Jurado, Alejandro
Gómez-Aldapa, Carlos Alberto
Mercado-Flores, Yuridia
Arana-Cuenca, Ainhoa
spellingShingle Tovar-Jiménez, Xochitl
Téllez-Jurado, Alejandro
Gómez-Aldapa, Carlos Alberto
Mercado-Flores, Yuridia
Arana-Cuenca, Ainhoa
Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
author_facet Tovar-Jiménez, Xochitl
Téllez-Jurado, Alejandro
Gómez-Aldapa, Carlos Alberto
Mercado-Flores, Yuridia
Arana-Cuenca, Ainhoa
author_sort Tovar-Jiménez, Xochitl
title Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
title_short Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
title_full Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
title_fullStr Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
title_full_unstemmed Antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
title_sort antioxidant and antihypertensive activity of bovine whey protein concentrate enzymatic hydrolysates
description Whey is a highly polluting by-product of cheese processing. However, it has valuable nutritional properties since it is a rich and balanced source of proteins and amino acids. Therefore, it has a broad range of functional properties that can be exploited for diverse applications. Research has shown how the enzymatic hydrolysis of whey proteins releases bioactive peptides. In the present study, the hydrolysis of whey protein concentrate (WCP) was performed using purified Sporisorium reilianum aspartyl protease (Eap1), commercial enzymes chymotrypsin (C) and trypsin (T), as well as different enzymatic combinations in order to determine which enzyme or combination allowed for the release of peptides presenting the highest antioxidant and antihypertensive activity levels; our results indicated that hydrolysis with Eap1 releases the best-performing peptides in comparison with individual enzymes and their combinations.
publisher Universidad de Sonora
publishDate 2021
url https://biotecnia.unison.mx/index.php/biotecnia/article/view/1321
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