Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis

Autores
Cimino, Cecilia V.; Colombo, Maria Laura; Liggieri, Constanza; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this article, we report the cloning of an aspartic protease (AP) from flowers of Arctium minus (Hill) Bernh. (Asteraceae) along with the use of depigmented aqueous flower extracts, as a source of APs, for the hydrolysis of whey proteins. The isolated cDNA encoded a protein product with 509 amino acids called arctiumisin, with the characteristic primary structure organization of typical plant APs. Bovine whey protein hydrolysates, obtained employing the enzyme extracts of A. minus flowers, displayed inhibitory angiotensin-converting enzyme (ACE) and antioxidant activities. Hydrolysates after 3 and 5 h of reaction (degree of hydrolysis 2.4 and 5.6, respectively) and the associated peptide fraction with molecular weight below 3 kDa were analyzed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization/time of flight mass spectrometry, and reverse phase-high-performance liquid chromatography. The results obtained in this study demonstrate the viability of using proteases from A. minus to increase the antioxidant and inhibitory ACE capacity of whey proteins.
Fil: Cimino, Cecilia V.. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Colombo, Maria Laura. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Liggieri, Constanza. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Ace-Inhibitory Activity
Antioxidant Capacity
Arctiumisin
Cloning
Milk Protein
Typical Plant Aspartic Protease
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:11336/13643
Acceder
id CONICETDig_55d6a25dc347149bbd3f40b8e474b163
oai_identifier_str oai:ri.conicet.gov.ar:11336/13643
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysisCimino, Cecilia V.Colombo, Maria LauraLiggieri, ConstanzaBruno, Mariela AnahíVairo Cavalli, Sandra ElizabethAce-Inhibitory ActivityAntioxidant CapacityArctiumisinCloningMilk ProteinTypical Plant Aspartic Proteasehttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3In this article, we report the cloning of an aspartic protease (AP) from flowers of Arctium minus (Hill) Bernh. (Asteraceae) along with the use of depigmented aqueous flower extracts, as a source of APs, for the hydrolysis of whey proteins. The isolated cDNA encoded a protein product with 509 amino acids called arctiumisin, with the characteristic primary structure organization of typical plant APs. Bovine whey protein hydrolysates, obtained employing the enzyme extracts of A. minus flowers, displayed inhibitory angiotensin-converting enzyme (ACE) and antioxidant activities. Hydrolysates after 3 and 5 h of reaction (degree of hydrolysis 2.4 and 5.6, respectively) and the associated peptide fraction with molecular weight below 3 kDa were analyzed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization/time of flight mass spectrometry, and reverse phase-high-performance liquid chromatography. The results obtained in this study demonstrate the viability of using proteases from A. minus to increase the antioxidant and inhibitory ACE capacity of whey proteins.Fil: Cimino, Cecilia V.. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Colombo, Maria Laura. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Liggieri, Constanza. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; ArgentinaFil: Bruno, Mariela Anahí. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaMary Ann Liebert Inc2015-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13643Cimino, Cecilia V.; Colombo, Maria Laura; Liggieri, Constanza; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth; Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis; Mary Ann Liebert Inc; Journal Of Medicinal Food; 18; 8; 1-2015; 856-8641096-620X1557-7600enginfo:eu-repo/semantics/altIdentifier/doi/10.1089/jmf.2014.0101info:eu-repo/semantics/altIdentifier/url/http://online.liebertpub.com/doi/10.1089/jmf.2014.0101info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:25:36Zoai:ri.conicet.gov.ar:11336/13643instacron: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 11:25:36.924CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
title Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
spellingShingle Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
Cimino, Cecilia V.
Ace-Inhibitory Activity
Antioxidant Capacity
Arctiumisin
Cloning
Milk Protein
Typical Plant Aspartic Protease
title_short Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
title_full Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
title_fullStr Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
title_full_unstemmed Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
title_sort Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis
dc.creator.none.fl_str_mv Cimino, Cecilia V.
Colombo, Maria Laura
Liggieri, Constanza
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author Cimino, Cecilia V.
author_facet Cimino, Cecilia V.
Colombo, Maria Laura
Liggieri, Constanza
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author_role author
author2 Colombo, Maria Laura
Liggieri, Constanza
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ace-Inhibitory Activity
Antioxidant Capacity
Arctiumisin
Cloning
Milk Protein
Typical Plant Aspartic Protease
topic Ace-Inhibitory Activity
Antioxidant Capacity
Arctiumisin
Cloning
Milk Protein
Typical Plant Aspartic Protease
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv In this article, we report the cloning of an aspartic protease (AP) from flowers of Arctium minus (Hill) Bernh. (Asteraceae) along with the use of depigmented aqueous flower extracts, as a source of APs, for the hydrolysis of whey proteins. The isolated cDNA encoded a protein product with 509 amino acids called arctiumisin, with the characteristic primary structure organization of typical plant APs. Bovine whey protein hydrolysates, obtained employing the enzyme extracts of A. minus flowers, displayed inhibitory angiotensin-converting enzyme (ACE) and antioxidant activities. Hydrolysates after 3 and 5 h of reaction (degree of hydrolysis 2.4 and 5.6, respectively) and the associated peptide fraction with molecular weight below 3 kDa were analyzed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization/time of flight mass spectrometry, and reverse phase-high-performance liquid chromatography. The results obtained in this study demonstrate the viability of using proteases from A. minus to increase the antioxidant and inhibitory ACE capacity of whey proteins.
Fil: Cimino, Cecilia V.. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Colombo, Maria Laura. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Liggieri, Constanza. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de la Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biologicas. Laboratorio de Investigacion de Proteinas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description In this article, we report the cloning of an aspartic protease (AP) from flowers of Arctium minus (Hill) Bernh. (Asteraceae) along with the use of depigmented aqueous flower extracts, as a source of APs, for the hydrolysis of whey proteins. The isolated cDNA encoded a protein product with 509 amino acids called arctiumisin, with the characteristic primary structure organization of typical plant APs. Bovine whey protein hydrolysates, obtained employing the enzyme extracts of A. minus flowers, displayed inhibitory angiotensin-converting enzyme (ACE) and antioxidant activities. Hydrolysates after 3 and 5 h of reaction (degree of hydrolysis 2.4 and 5.6, respectively) and the associated peptide fraction with molecular weight below 3 kDa were analyzed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, matrix-assisted laser desorption ionization/time of flight mass spectrometry, and reverse phase-high-performance liquid chromatography. The results obtained in this study demonstrate the viability of using proteases from A. minus to increase the antioxidant and inhibitory ACE capacity of whey proteins.
publishDate 2015
dc.date.none.fl_str_mv 2015-01
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/11336/13643
Cimino, Cecilia V.; Colombo, Maria Laura; Liggieri, Constanza; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth; Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis; Mary Ann Liebert Inc; Journal Of Medicinal Food; 18; 8; 1-2015; 856-864
1096-620X
1557-7600
url http://hdl.handle.net/11336/13643
identifier_str_mv Cimino, Cecilia V.; Colombo, Maria Laura; Liggieri, Constanza; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth; Partial molecular characterization of Arctium minus Aspartylendopeptidase and preparation of bioactive peptides by Whey protein hydrolysis; Mary Ann Liebert Inc; Journal Of Medicinal Food; 18; 8; 1-2015; 856-864
1096-620X
1557-7600
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1089/jmf.2014.0101
info:eu-repo/semantics/altIdentifier/url/http://online.liebertpub.com/doi/10.1089/jmf.2014.0101
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
dc.publisher.none.fl_str_mv Mary Ann Liebert Inc
publisher.none.fl_str_mv Mary Ann Liebert Inc
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_ 1846781806710358016
score 12.982451

Publicaciones similares