Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH

Autores
Cian, Raúl Esteban; Vioque, Javier; Drago, Silvina Rosa
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The aims of this study were to assess bioactive properties (ACE inhibition and antioxidant capacity) from wheat gluten hydrolysate peptides fractionated by pH (4.0, 6.0 and 9.0), to determine peptide action mechanism, and to relate it to the secondary structure and functional groups of peptides. Gluten hydrolysate extracts (GHE) were enriched in peptideswith mediumhydrophobicity and molecularweight (≈60%MH and 5.5 kDa, respectively). Gluten peptides inhibited ACE I by uncompetitive mechanism and a direct relationship between α-helix structure and IC50% value was obtained (r = 0.9127). TEAC and cooper chelating activity from GHE 6.5 were the highest and directly correlated with MH peptides. GHE 9.0 had high carotene bleaching inhibition (47.5± 0.3%) and reducing power activity (163.1±2.9 mg S2O3 2 − equivalent g−1 protein), which were directly related to disulfide bonds content of peptides (r=0.9982 and 0.9216, respectively). pHwas a good alternative to select bioactive peptides from wheat gluten hydrolysate.
Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vioque, Javier. Consejo Superior de Investigaciones Cientificas; España
Fil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Secondary Structure
Gluten Peptides
Ace Inhibition
Antioxidant Properties
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:11336/16041
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/16041
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pHCian, Raúl EstebanVioque, JavierDrago, Silvina RosaSecondary StructureGluten PeptidesAce InhibitionAntioxidant Propertieshttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2The aims of this study were to assess bioactive properties (ACE inhibition and antioxidant capacity) from wheat gluten hydrolysate peptides fractionated by pH (4.0, 6.0 and 9.0), to determine peptide action mechanism, and to relate it to the secondary structure and functional groups of peptides. Gluten hydrolysate extracts (GHE) were enriched in peptideswith mediumhydrophobicity and molecularweight (≈60%MH and 5.5 kDa, respectively). Gluten peptides inhibited ACE I by uncompetitive mechanism and a direct relationship between α-helix structure and IC50% value was obtained (r = 0.9127). TEAC and cooper chelating activity from GHE 6.5 were the highest and directly correlated with MH peptides. GHE 9.0 had high carotene bleaching inhibition (47.5± 0.3%) and reducing power activity (163.1±2.9 mg S2O3 2 − equivalent g−1 protein), which were directly related to disulfide bonds content of peptides (r=0.9982 and 0.9216, respectively). pHwas a good alternative to select bioactive peptides from wheat gluten hydrolysate.Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Vioque, Javier. Consejo Superior de Investigaciones Cientificas; EspañaFil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier2015-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16041Cian, Raúl Esteban; Vioque, Javier; Drago, Silvina Rosa; Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH; Elsevier; Food Research International; 69; 3-2015; 216-2230963-9969enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2014.12.036info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:10:25Zoai:ri.conicet.gov.ar:11336/16041instacron: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:34982025-10-22 12:10:26.1CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
title Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
spellingShingle Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
Cian, Raúl Esteban
Secondary Structure
Gluten Peptides
Ace Inhibition
Antioxidant Properties
title_short Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
title_full Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
title_fullStr Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
title_full_unstemmed Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
title_sort Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH
dc.creator.none.fl_str_mv Cian, Raúl Esteban
Vioque, Javier
Drago, Silvina Rosa
author Cian, Raúl Esteban
author_facet Cian, Raúl Esteban
Vioque, Javier
Drago, Silvina Rosa
author_role author
author2 Vioque, Javier
Drago, Silvina Rosa
author2_role author
author
dc.subject.none.fl_str_mv Secondary Structure
Gluten Peptides
Ace Inhibition
Antioxidant Properties
topic Secondary Structure
Gluten Peptides
Ace Inhibition
Antioxidant Properties
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The aims of this study were to assess bioactive properties (ACE inhibition and antioxidant capacity) from wheat gluten hydrolysate peptides fractionated by pH (4.0, 6.0 and 9.0), to determine peptide action mechanism, and to relate it to the secondary structure and functional groups of peptides. Gluten hydrolysate extracts (GHE) were enriched in peptideswith mediumhydrophobicity and molecularweight (≈60%MH and 5.5 kDa, respectively). Gluten peptides inhibited ACE I by uncompetitive mechanism and a direct relationship between α-helix structure and IC50% value was obtained (r = 0.9127). TEAC and cooper chelating activity from GHE 6.5 were the highest and directly correlated with MH peptides. GHE 9.0 had high carotene bleaching inhibition (47.5± 0.3%) and reducing power activity (163.1±2.9 mg S2O3 2 − equivalent g−1 protein), which were directly related to disulfide bonds content of peptides (r=0.9982 and 0.9216, respectively). pHwas a good alternative to select bioactive peptides from wheat gluten hydrolysate.
Fil: Cian, Raúl Esteban. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vioque, Javier. Consejo Superior de Investigaciones Cientificas; España
Fil: Drago, Silvina Rosa. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Tecnología de los Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The aims of this study were to assess bioactive properties (ACE inhibition and antioxidant capacity) from wheat gluten hydrolysate peptides fractionated by pH (4.0, 6.0 and 9.0), to determine peptide action mechanism, and to relate it to the secondary structure and functional groups of peptides. Gluten hydrolysate extracts (GHE) were enriched in peptideswith mediumhydrophobicity and molecularweight (≈60%MH and 5.5 kDa, respectively). Gluten peptides inhibited ACE I by uncompetitive mechanism and a direct relationship between α-helix structure and IC50% value was obtained (r = 0.9127). TEAC and cooper chelating activity from GHE 6.5 were the highest and directly correlated with MH peptides. GHE 9.0 had high carotene bleaching inhibition (47.5± 0.3%) and reducing power activity (163.1±2.9 mg S2O3 2 − equivalent g−1 protein), which were directly related to disulfide bonds content of peptides (r=0.9982 and 0.9216, respectively). pHwas a good alternative to select bioactive peptides from wheat gluten hydrolysate.
publishDate 2015
dc.date.none.fl_str_mv 2015-03
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/11336/16041
Cian, Raúl Esteban; Vioque, Javier; Drago, Silvina Rosa; Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH; Elsevier; Food Research International; 69; 3-2015; 216-223
0963-9969
url http://hdl.handle.net/11336/16041
identifier_str_mv Cian, Raúl Esteban; Vioque, Javier; Drago, Silvina Rosa; Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH; Elsevier; Food Research International; 69; 3-2015; 216-223
0963-9969
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2014.12.036
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
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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
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score 12.982451

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