Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal dig...

Autores
Cian, Raúl Esteban; Garzón, Antonela Guadalupe; Betancur, Ancona, David; Chel Guerrero, Luis; Drago, Silvina Rosa
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aim of this work was to evaluate the bio-accessibility of bioactive peptides with ACE I inhibition, antioxidant and antiplatelet aggregation activity obtained by enzymatic hydrolysis of Pyropia columbina proteins. Two hydrolyzates were produced (A and AF). Bio-accesibility was determined using a gastrointestinal digestion (pepsin and pancreatin) and membrane dialysis system. Hydrolyzates had peptides with medium molecular weight (2300 Da), and Asp, Glu and Ala were the most abundant amino acids. Additionally, AF presented small peptides with 287 Da. Peptides from A showed the highest angiotensin-converting enzyme activity (ACE I) inhibition by uncompetitive mechanism (IC50%, 1.2 ± 0.1 g L−1), and β-carotene bleaching inhibition. Peptides from AF presented the lower IC50% value for ABTS+• and DPPH radical inhibition, the highest copper-chelating activity (CCA), and antiplatelet aggregation activity. In vitro gastrointestinal digestion increased ABTS+• and DPPH scavenging and CCA of both hydrolyzates. Antiplatelet aggregation activity of A peptides was increased after simulated digestion process (≈157%). Peptides from both hydrolyzates were potentially bio-accessible, maintaining overall the bioactivity after gastrointestinal diges
Fil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Betancur, Ancona, David. Universidad Autónoma de Yucatán; México
Fil: Chel Guerrero, Luis. Universidad Autónoma de Yucatán; México
Fil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Materia
Accessibility
Gastrointestinal Digestion
Bioactive Peptides
Red Seaweeds
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/78248
Acceder
id CONICETDig_e3b91d0dc33bf73f081c9dcea1cead3c
oai_identifier_str oai:ri.conicet.gov.ar:11336/78248
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestionCian, Raúl EstebanGarzón, Antonela GuadalupeBetancur, Ancona, DavidChel Guerrero, LuisDrago, Silvina RosaAccessibilityGastrointestinal DigestionBioactive PeptidesRed Seaweedshttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The aim of this work was to evaluate the bio-accessibility of bioactive peptides with ACE I inhibition, antioxidant and antiplatelet aggregation activity obtained by enzymatic hydrolysis of Pyropia columbina proteins. Two hydrolyzates were produced (A and AF). Bio-accesibility was determined using a gastrointestinal digestion (pepsin and pancreatin) and membrane dialysis system. Hydrolyzates had peptides with medium molecular weight (2300 Da), and Asp, Glu and Ala were the most abundant amino acids. Additionally, AF presented small peptides with 287 Da. Peptides from A showed the highest angiotensin-converting enzyme activity (ACE I) inhibition by uncompetitive mechanism (IC50%, 1.2 ± 0.1 g L−1), and β-carotene bleaching inhibition. Peptides from AF presented the lower IC50% value for ABTS+• and DPPH radical inhibition, the highest copper-chelating activity (CCA), and antiplatelet aggregation activity. In vitro gastrointestinal digestion increased ABTS+• and DPPH scavenging and CCA of both hydrolyzates. Antiplatelet aggregation activity of A peptides was increased after simulated digestion process (≈157%). Peptides from both hydrolyzates were potentially bio-accessible, maintaining overall the bioactivity after gastrointestinal digesFil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaFil: Betancur, Ancona, David. Universidad Autónoma de Yucatán; MéxicoFil: Chel Guerrero, Luis. Universidad Autónoma de Yucatán; MéxicoFil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; ArgentinaElsevier Science2015-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/78248Cian, Raúl Esteban; Garzón, Antonela Guadalupe; Betancur, Ancona, David; Chel Guerrero, Luis; Drago, Silvina Rosa; Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion; Elsevier Science; LWT - Food Science and Technology; 64; 2; 12-2015; 881-8880023-6438CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2015.06.043info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643815004703info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:18:59Zoai:ri.conicet.gov.ar:11336/78248instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:18:59.609CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
title Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
spellingShingle Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
Cian, Raúl Esteban
Accessibility
Gastrointestinal Digestion
Bioactive Peptides
Red Seaweeds
title_short Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
title_full Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
title_fullStr Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
title_full_unstemmed Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
title_sort Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion
dc.creator.none.fl_str_mv Cian, Raúl Esteban
Garzón, Antonela Guadalupe
Betancur, Ancona, David
Chel Guerrero, Luis
Drago, Silvina Rosa
author Cian, Raúl Esteban
author_facet Cian, Raúl Esteban
Garzón, Antonela Guadalupe
Betancur, Ancona, David
Chel Guerrero, Luis
Drago, Silvina Rosa
author_role author
author2 Garzón, Antonela Guadalupe
Betancur, Ancona, David
Chel Guerrero, Luis
Drago, Silvina Rosa
author2_role author
author
author
author
dc.subject.none.fl_str_mv Accessibility
Gastrointestinal Digestion
Bioactive Peptides
Red Seaweeds
topic Accessibility
Gastrointestinal Digestion
Bioactive Peptides
Red Seaweeds
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The aim of this work was to evaluate the bio-accessibility of bioactive peptides with ACE I inhibition, antioxidant and antiplatelet aggregation activity obtained by enzymatic hydrolysis of Pyropia columbina proteins. Two hydrolyzates were produced (A and AF). Bio-accesibility was determined using a gastrointestinal digestion (pepsin and pancreatin) and membrane dialysis system. Hydrolyzates had peptides with medium molecular weight (2300 Da), and Asp, Glu and Ala were the most abundant amino acids. Additionally, AF presented small peptides with 287 Da. Peptides from A showed the highest angiotensin-converting enzyme activity (ACE I) inhibition by uncompetitive mechanism (IC50%, 1.2 ± 0.1 g L−1), and β-carotene bleaching inhibition. Peptides from AF presented the lower IC50% value for ABTS+• and DPPH radical inhibition, the highest copper-chelating activity (CCA), and antiplatelet aggregation activity. In vitro gastrointestinal digestion increased ABTS+• and DPPH scavenging and CCA of both hydrolyzates. Antiplatelet aggregation activity of A peptides was increased after simulated digestion process (≈157%). Peptides from both hydrolyzates were potentially bio-accessible, maintaining overall the bioactivity after gastrointestinal diges
Fil: Cian, Raúl Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Garzón, Antonela Guadalupe. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
Fil: Betancur, Ancona, David. Universidad Autónoma de Yucatán; México
Fil: Chel Guerrero, Luis. Universidad Autónoma de Yucatán; México
Fil: Drago, Silvina Rosa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina
description The aim of this work was to evaluate the bio-accessibility of bioactive peptides with ACE I inhibition, antioxidant and antiplatelet aggregation activity obtained by enzymatic hydrolysis of Pyropia columbina proteins. Two hydrolyzates were produced (A and AF). Bio-accesibility was determined using a gastrointestinal digestion (pepsin and pancreatin) and membrane dialysis system. Hydrolyzates had peptides with medium molecular weight (2300 Da), and Asp, Glu and Ala were the most abundant amino acids. Additionally, AF presented small peptides with 287 Da. Peptides from A showed the highest angiotensin-converting enzyme activity (ACE I) inhibition by uncompetitive mechanism (IC50%, 1.2 ± 0.1 g L−1), and β-carotene bleaching inhibition. Peptides from AF presented the lower IC50% value for ABTS+• and DPPH radical inhibition, the highest copper-chelating activity (CCA), and antiplatelet aggregation activity. In vitro gastrointestinal digestion increased ABTS+• and DPPH scavenging and CCA of both hydrolyzates. Antiplatelet aggregation activity of A peptides was increased after simulated digestion process (≈157%). Peptides from both hydrolyzates were potentially bio-accessible, maintaining overall the bioactivity after gastrointestinal diges
publishDate 2015
dc.date.none.fl_str_mv 2015-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/78248
Cian, Raúl Esteban; Garzón, Antonela Guadalupe; Betancur, Ancona, David; Chel Guerrero, Luis; Drago, Silvina Rosa; Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion; Elsevier Science; LWT - Food Science and Technology; 64; 2; 12-2015; 881-888
0023-6438
CONICET Digital
CONICET
url http://hdl.handle.net/11336/78248
identifier_str_mv Cian, Raúl Esteban; Garzón, Antonela Guadalupe; Betancur, Ancona, David; Chel Guerrero, Luis; Drago, Silvina Rosa; Hydrolyzates from Pyropia columbina seaweed have antiplatelet aggregation, antioxidant and ACE I inhibitory peptides which maintain bioactivity after simulated gastrointestinal digestion; Elsevier Science; LWT - Food Science and Technology; 64; 2; 12-2015; 881-888
0023-6438
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.lwt.2015.06.043
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0023643815004703
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844614157665566720
score 13.070432

Publicaciones similares