Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides

The aim of this work is to establish the most suitable proteolysis conditions to obtain bovine casein hydrolysates containing peptides with antioxidant and antihypertensive capacity. To this end, the proteolytic activity of Cynara scolymus L. flower extracts was characterized on whole bovine casein,...

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Autores: Abellán, Adela, Bermejo, María Soledad, Salazar, Eva, Cayuela, José Maria, Tejada Portero, Luis, Bueno Gavilá, Estefanía, Prieto Merino, David
Tipo de recurso: artículo
Fecha de publicación:2020
País:España
Institución:Universidad Católica San Antonio de Murcia (UCAM)
Repositorio:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
OAI Identifier:oai:repositorio.ucam.edu:10952/9082
Acceso en línea:http://hdl.handle.net/10952/9082
Access Level:acceso abierto
Palabra clave:Artichoke
Antioxidant
Bovine casein
Proteolysis
Angiotensin converting enzyme (ACE)
Cinarases
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spelling Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive PeptidesAbellán, AdelaBermejo, María SoledadSalazar, EvaCayuela, José MariaTejada Portero, LuisBueno Gavilá, EstefaníaPrieto Merino, DavidArtichokeAntioxidantBovine caseinProteolysisAngiotensin converting enzyme (ACE)CinarasesThe aim of this work is to establish the most suitable proteolysis conditions to obtain bovine casein hydrolysates containing peptides with antioxidant and antihypertensive capacity. To this end, the proteolytic activity of Cynara scolymus L. flower extracts was characterized on whole bovine casein, evaluating the effect of several factors (pH, temperature, substrate concentration, enzyme concentration, and hydrolysis time). The optimal conditions to carry out the hydrolysis with the C. scolymus L. extract were as follows: pH 6.2, 50 ◦C, and 0.023 mg·mL−1 of extract-protein concentration. A Michaelis constant (Km) value of 5.66 mg·mL−1 and a maximum rate of reaction (Vmax) of 8.47 mUAbs·min−1 were observed. The optimal hydrolysis time was 17 h. The casein hydrolysates obtained with these conditions contained peptides with antioxidant activity (1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity: 30.89%; Trolox equivalent antioxidant capacity (TEAC) against 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) free radical (ABTS•+): 4.43 mM Trolox equivalent·mg−1 peptide) and antihypertensive activity, showing 55.05% angiotensin-converting enzyme-I inhibition in vitro.El objetivo de este trabajo es establecer las condiciones de proteólisis más adecuadas para obtener hidrolizados de caseína bovina que contengan péptidos con capacidad antioxidante y antihipertensiva. Para ello, se caracterizó la actividad proteolítica de los extractos de la flor de Cynara scolymus L. sobre la caseína bovina completa, evaluando el efecto de varios factores (pH, temperatura, concentración del sustrato, concentración de la enzima y tiempo de hidrólisis). Las condiciones óptimas para llevar a cabo la hidrólisis con el extracto de C. scolymus L. fueron las siguientes: pH 6.2, 50 °C y una concentración de proteína en el extracto de 0.023 mg·mL⁻¹. Se observó un valor de la constante de Michaelis (Km) de 5.66 mg·mL⁻¹ y una velocidad máxima de reacción (Vmax) de 8.47 mUAbs·min⁻¹. El tiempo óptimo de hidrólisis fue de 17 horas. Los hidrolizados de caseína obtenidos en estas condiciones contenían péptidos con actividad antioxidante (capacidad de eliminación del radical 1,1-difenil-2-picrilhidrazilo (DPPH): 30.89%; capacidad antioxidante equivalente a Trolox (TEAC) frente al radical libre 2,2’-azino-bis(3-etilbenzotiazolina-6-ácido sulfónico) (ABTS•+): 4.43 mM de equivalentes de Trolox·mg⁻¹ de péptidos) y actividad antihipertensiva, mostrando una inhibición del 55.05% de la enzima convertidora de angiotensina-I (ECA) in vitro.Ciencias de la AlimentaciónFarmacia y Nutrición2020info:eu-repo/semantics/articlehttp://hdl.handle.net/10952/9082reponame:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murciainstname:Universidad Católica San Antonio de Murcia (UCAM)Inglésinfo:eu-repo/semantics/openAccessoai:repositorio.ucam.edu:10952/90822026-06-07T18:35:21Z
dc.title.none.fl_str_mv Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
title Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
spellingShingle Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
Abellán, Adela
Artichoke
Antioxidant
Bovine casein
Proteolysis
Angiotensin converting enzyme (ACE)
Cinarases
title_short Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
title_full Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
title_fullStr Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
title_full_unstemmed Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
title_sort Characterization of Proteolytic Activity of Artichoke (Cynara scolymus L.) Flower Extracts on Bovine Casein to Obtain Bioactive Peptides
dc.creator.none.fl_str_mv Abellán, Adela
Bermejo, María Soledad
Salazar, Eva
Cayuela, José Maria
Tejada Portero, Luis
Bueno Gavilá, Estefanía
Prieto Merino, David
author Abellán, Adela
author_facet Abellán, Adela
Bermejo, María Soledad
Salazar, Eva
Cayuela, José Maria
Tejada Portero, Luis
Bueno Gavilá, Estefanía
Prieto Merino, David
author_role author
author2 Bermejo, María Soledad
Salazar, Eva
Cayuela, José Maria
Tejada Portero, Luis
Bueno Gavilá, Estefanía
Prieto Merino, David
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Artichoke
Antioxidant
Bovine casein
Proteolysis
Angiotensin converting enzyme (ACE)
Cinarases
topic Artichoke
Antioxidant
Bovine casein
Proteolysis
Angiotensin converting enzyme (ACE)
Cinarases
description The aim of this work is to establish the most suitable proteolysis conditions to obtain bovine casein hydrolysates containing peptides with antioxidant and antihypertensive capacity. To this end, the proteolytic activity of Cynara scolymus L. flower extracts was characterized on whole bovine casein, evaluating the effect of several factors (pH, temperature, substrate concentration, enzyme concentration, and hydrolysis time). The optimal conditions to carry out the hydrolysis with the C. scolymus L. extract were as follows: pH 6.2, 50 ◦C, and 0.023 mg·mL−1 of extract-protein concentration. A Michaelis constant (Km) value of 5.66 mg·mL−1 and a maximum rate of reaction (Vmax) of 8.47 mUAbs·min−1 were observed. The optimal hydrolysis time was 17 h. The casein hydrolysates obtained with these conditions contained peptides with antioxidant activity (1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity: 30.89%; Trolox equivalent antioxidant capacity (TEAC) against 2,2’-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) free radical (ABTS•+): 4.43 mM Trolox equivalent·mg−1 peptide) and antihypertensive activity, showing 55.05% angiotensin-converting enzyme-I inhibition in vitro.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10952/9082
url http://hdl.handle.net/10952/9082
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
instname:Universidad Católica San Antonio de Murcia (UCAM)
instname_str Universidad Católica San Antonio de Murcia (UCAM)
reponame_str RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
collection RIUCAM. Repositorio Institucional de la Universidad Católica San Antonio de Murcia
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869422982655377408
score 15,811543

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