Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis

Autores
Tironi, Valeria Anahi; Añon, Maria Cristina
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The antioxidant activity of peptides present in the phosphate buffer-soluble fraction of: – Amaranthus mantegazzianus protein isolates (Is), – protein fractions (Albs, Globs, GlobPs and Gluts), alcalase hydrolysates of isolates (hydrolysis degree –HD-: 2.4% (IHls) and 30% (IHhs) and protein fractions (AlbHs, GlobHs, GlobPHs, and GlutHs) was investigated. Fractions separated by molecular exclusion chromatography were also analyzed. ABTS+. scavenging method showed the presence of antioxidant peptides in Is, Albs, Globs, and Gluts, being the last the one with the highest activity. No activity was detected in the GlobPs. After hydrolysis, the scavenging activity of all samples increased, especially at high HD. The GlobPs fraction presented the highest scavenging capacity after hydrolysis. Naturally-occurring peptides and polypeptides presented also the capacity to inhibit the linoleic acid oxidation, which was partially lost after hydrolysis. FPLC fractionation evidenced the appearance of <0.5 kDa active peptides due to the hydrolysis process. Results suggest the presence in the Is and IHhs of several peptides and polypeptides which can act as antioxidants by different mechanisms.
Fil: Tironi, Valeria Anahi. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Materia
AMARANTH
ANTIOXIDANT ACTIVITY
HYDROLYSIS
PEPTIDES
PROTEINS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/135305
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Amaranth proteins as a source of antioxidant peptides: Effect of proteolysisTironi, Valeria AnahiAñon, Maria CristinaAMARANTHANTIOXIDANT ACTIVITYHYDROLYSISPEPTIDESPROTEINShttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2The antioxidant activity of peptides present in the phosphate buffer-soluble fraction of: – Amaranthus mantegazzianus protein isolates (Is), – protein fractions (Albs, Globs, GlobPs and Gluts), alcalase hydrolysates of isolates (hydrolysis degree –HD-: 2.4% (IHls) and 30% (IHhs) and protein fractions (AlbHs, GlobHs, GlobPHs, and GlutHs) was investigated. Fractions separated by molecular exclusion chromatography were also analyzed. ABTS+. scavenging method showed the presence of antioxidant peptides in Is, Albs, Globs, and Gluts, being the last the one with the highest activity. No activity was detected in the GlobPs. After hydrolysis, the scavenging activity of all samples increased, especially at high HD. The GlobPs fraction presented the highest scavenging capacity after hydrolysis. Naturally-occurring peptides and polypeptides presented also the capacity to inhibit the linoleic acid oxidation, which was partially lost after hydrolysis. FPLC fractionation evidenced the appearance of <0.5 kDa active peptides due to the hydrolysis process. Results suggest the presence in the Is and IHhs of several peptides and polypeptides which can act as antioxidants by different mechanisms.Fil: Tironi, Valeria Anahi. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaElsevier Science2010-01info: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/11336/135305Tironi, Valeria Anahi; Añon, Maria Cristina; Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis; Elsevier Science; Food Research International; 43; 1; 1-2010; 315-3220963-99691873-7145CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://bit.ly/3qEIgfoinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2009.10.001info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:34:47Zoai:ri.conicet.gov.ar:11336/135305instacron: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:34982025-10-15 15:34:48.194CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
title Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
spellingShingle Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
Tironi, Valeria Anahi
AMARANTH
ANTIOXIDANT ACTIVITY
HYDROLYSIS
PEPTIDES
PROTEINS
title_short Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
title_full Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
title_fullStr Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
title_full_unstemmed Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
title_sort Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis
dc.creator.none.fl_str_mv Tironi, Valeria Anahi
Añon, Maria Cristina
author Tironi, Valeria Anahi
author_facet Tironi, Valeria Anahi
Añon, Maria Cristina
author_role author
author2 Añon, Maria Cristina
author2_role author
dc.subject.none.fl_str_mv AMARANTH
ANTIOXIDANT ACTIVITY
HYDROLYSIS
PEPTIDES
PROTEINS
topic AMARANTH
ANTIOXIDANT ACTIVITY
HYDROLYSIS
PEPTIDES
PROTEINS
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 antioxidant activity of peptides present in the phosphate buffer-soluble fraction of: – Amaranthus mantegazzianus protein isolates (Is), – protein fractions (Albs, Globs, GlobPs and Gluts), alcalase hydrolysates of isolates (hydrolysis degree –HD-: 2.4% (IHls) and 30% (IHhs) and protein fractions (AlbHs, GlobHs, GlobPHs, and GlutHs) was investigated. Fractions separated by molecular exclusion chromatography were also analyzed. ABTS+. scavenging method showed the presence of antioxidant peptides in Is, Albs, Globs, and Gluts, being the last the one with the highest activity. No activity was detected in the GlobPs. After hydrolysis, the scavenging activity of all samples increased, especially at high HD. The GlobPs fraction presented the highest scavenging capacity after hydrolysis. Naturally-occurring peptides and polypeptides presented also the capacity to inhibit the linoleic acid oxidation, which was partially lost after hydrolysis. FPLC fractionation evidenced the appearance of <0.5 kDa active peptides due to the hydrolysis process. Results suggest the presence in the Is and IHhs of several peptides and polypeptides which can act as antioxidants by different mechanisms.
Fil: Tironi, Valeria Anahi. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Añon, Maria Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
description The antioxidant activity of peptides present in the phosphate buffer-soluble fraction of: – Amaranthus mantegazzianus protein isolates (Is), – protein fractions (Albs, Globs, GlobPs and Gluts), alcalase hydrolysates of isolates (hydrolysis degree –HD-: 2.4% (IHls) and 30% (IHhs) and protein fractions (AlbHs, GlobHs, GlobPHs, and GlutHs) was investigated. Fractions separated by molecular exclusion chromatography were also analyzed. ABTS+. scavenging method showed the presence of antioxidant peptides in Is, Albs, Globs, and Gluts, being the last the one with the highest activity. No activity was detected in the GlobPs. After hydrolysis, the scavenging activity of all samples increased, especially at high HD. The GlobPs fraction presented the highest scavenging capacity after hydrolysis. Naturally-occurring peptides and polypeptides presented also the capacity to inhibit the linoleic acid oxidation, which was partially lost after hydrolysis. FPLC fractionation evidenced the appearance of <0.5 kDa active peptides due to the hydrolysis process. Results suggest the presence in the Is and IHhs of several peptides and polypeptides which can act as antioxidants by different mechanisms.
publishDate 2010
dc.date.none.fl_str_mv 2010-01
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/11336/135305
Tironi, Valeria Anahi; Añon, Maria Cristina; Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis; Elsevier Science; Food Research International; 43; 1; 1-2010; 315-322
0963-9969
1873-7145
CONICET Digital
CONICET
url http://hdl.handle.net/11336/135305
identifier_str_mv Tironi, Valeria Anahi; Añon, Maria Cristina; Amaranth proteins as a source of antioxidant peptides: Effect of proteolysis; Elsevier Science; Food Research International; 43; 1; 1-2010; 315-322
0963-9969
1873-7145
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://bit.ly/3qEIgfo
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.foodres.2009.10.001
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv 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
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score 13.22299

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