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

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 fraction...

Full description

Bibliographic Details
Authors: Tironi, Valeria Anahi, Añon, Maria Cristina
Format: article
Status:Published version
Publication Date:2010
Country:Argentina
Institution:Consejo Nacional de Investigaciones Científicas y Técnicas
Repository:CONICET Digital (CONICET)
Language:English
OAI Identifier:oai:ri.conicet.gov.ar:11336/135305
Online Access:http://hdl.handle.net/11336/135305
Access Level:Open access
Keyword:AMARANTH
ANTIOXIDANT ACTIVITY
HYDROLYSIS
PEPTIDES
PROTEINS
https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
id AR_f3df7f3f93e1a3e1a4e1e06c852078f5
oai_identifier_str oai:ri.conicet.gov.ar:11336/135305
network_acronym_str AR
network_name_str Argentina
repository_id_str
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 Técnicas2024-05-08T14:20:56Zoai: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:34982024-05-08 14:20:57.179CONICET 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
https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
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
https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
topic AMARANTH
ANTIOXIDANT ACTIVITY
HYDROLYSIS
PEPTIDES
PROTEINS
https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
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
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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_ 1799196265776414720
score 15,812429