Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products

Autores
Cimino, Cecilia Verónica; Liggieri, Constanza Silvina; Priolo, Nora Silvia; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Food proteins encrypt bioactive peptides that can be released during gastrointestinal digestion or food processing by enzymatic proteolysis. Flowers of Carduae tribe, family Asteraceae, contain aspartic proteinases with milk clotting activity. Crude enzyme extracts with proteolytic activity were prepared from flowers of Arctium minus at pH 7.0, and were partially purified and characterized. Optimun bovine milk clotting activity was achieved with CaCl2 30 mM at 35 ºC. Inhibition of milk clotting activity was only promoted by pepstatin A, a highly selective inhibitor for aspartic peptidases. Analysis of crude extract by isoelectric focusing and zymogram showed an unique active band (pI 5.0). Molecular exclusion chromatography (Sephadex G-25 Fine) was employed to eliminate pigments and phenolic compounds, in order to obtain the partially purified extract (EE). Whey bovine hydrolyzates were performed with EE and analyzed by SDS-PAGE. Hydrolyzed whey was ultrafiltrated, and low molecular fractions (peptide mass ≤ 3000 Da) showed angiotensin-converting enzyme (ACE) inhibitory activity. Therefore, these peptides with antihypertensive activity could be potentially used in food industry for formulation of nutraceutical products.
Fil: Cimino, Cecilia Verónica. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Materia
ASPARTIC PROTEASE
ASTERACEAE
WHEY HYDROLYZATE
ACE INHIBITORY ACTIVITY
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:11336/241720
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical productsCimino, Cecilia VerónicaLiggieri, Constanza SilvinaPriolo, Nora SilviaBruno, Mariela AnahíVairo Cavalli, Sandra ElizabethASPARTIC PROTEASEASTERACEAEWHEY HYDROLYZATEACE INHIBITORY ACTIVITYhttps://purl.org/becyt/ford/3.4https://purl.org/becyt/ford/3Food proteins encrypt bioactive peptides that can be released during gastrointestinal digestion or food processing by enzymatic proteolysis. Flowers of Carduae tribe, family Asteraceae, contain aspartic proteinases with milk clotting activity. Crude enzyme extracts with proteolytic activity were prepared from flowers of Arctium minus at pH 7.0, and were partially purified and characterized. Optimun bovine milk clotting activity was achieved with CaCl2 30 mM at 35 ºC. Inhibition of milk clotting activity was only promoted by pepstatin A, a highly selective inhibitor for aspartic peptidases. Analysis of crude extract by isoelectric focusing and zymogram showed an unique active band (pI 5.0). Molecular exclusion chromatography (Sephadex G-25 Fine) was employed to eliminate pigments and phenolic compounds, in order to obtain the partially purified extract (EE). Whey bovine hydrolyzates were performed with EE and analyzed by SDS-PAGE. Hydrolyzed whey was ultrafiltrated, and low molecular fractions (peptide mass ≤ 3000 Da) showed angiotensin-converting enzyme (ACE) inhibitory activity. Therefore, these peptides with antihypertensive activity could be potentially used in food industry for formulation of nutraceutical products.Fil: Cimino, Cecilia Verónica. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaInstituto de Investigación de las Ciencias Exactas Físicas y Naturales2010-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/241720Cimino, Cecilia Verónica; Liggieri, Constanza Silvina; Priolo, Nora Silvia; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth; Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products; Instituto de Investigación de las Ciencias Exactas Físicas y Naturales; Molecular Medicinal Chemistry; 21; 6-2010; 11-161666-888XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.idecefyn.com.ar/MMC21PDF/vol_21__january.htminfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:02:57Zoai:ri.conicet.gov.ar:11336/241720instacron: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 11:02:57.394CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
title Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
spellingShingle Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
Cimino, Cecilia Verónica
ASPARTIC PROTEASE
ASTERACEAE
WHEY HYDROLYZATE
ACE INHIBITORY ACTIVITY
title_short Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
title_full Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
title_fullStr Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
title_full_unstemmed Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
title_sort Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
dc.creator.none.fl_str_mv Cimino, Cecilia Verónica
Liggieri, Constanza Silvina
Priolo, Nora Silvia
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author Cimino, Cecilia Verónica
author_facet Cimino, Cecilia Verónica
Liggieri, Constanza Silvina
Priolo, Nora Silvia
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author_role author
author2 Liggieri, Constanza Silvina
Priolo, Nora Silvia
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author2_role author
author
author
author
dc.subject.none.fl_str_mv ASPARTIC PROTEASE
ASTERACEAE
WHEY HYDROLYZATE
ACE INHIBITORY ACTIVITY
topic ASPARTIC PROTEASE
ASTERACEAE
WHEY HYDROLYZATE
ACE INHIBITORY ACTIVITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Food proteins encrypt bioactive peptides that can be released during gastrointestinal digestion or food processing by enzymatic proteolysis. Flowers of Carduae tribe, family Asteraceae, contain aspartic proteinases with milk clotting activity. Crude enzyme extracts with proteolytic activity were prepared from flowers of Arctium minus at pH 7.0, and were partially purified and characterized. Optimun bovine milk clotting activity was achieved with CaCl2 30 mM at 35 ºC. Inhibition of milk clotting activity was only promoted by pepstatin A, a highly selective inhibitor for aspartic peptidases. Analysis of crude extract by isoelectric focusing and zymogram showed an unique active band (pI 5.0). Molecular exclusion chromatography (Sephadex G-25 Fine) was employed to eliminate pigments and phenolic compounds, in order to obtain the partially purified extract (EE). Whey bovine hydrolyzates were performed with EE and analyzed by SDS-PAGE. Hydrolyzed whey was ultrafiltrated, and low molecular fractions (peptide mass ≤ 3000 Da) showed angiotensin-converting enzyme (ACE) inhibitory activity. Therefore, these peptides with antihypertensive activity could be potentially used in food industry for formulation of nutraceutical products.
Fil: Cimino, Cecilia Verónica. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Liggieri, Constanza Silvina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Bruno, Mariela Anahí. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Vairo Cavalli, Sandra Elizabeth. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
description Food proteins encrypt bioactive peptides that can be released during gastrointestinal digestion or food processing by enzymatic proteolysis. Flowers of Carduae tribe, family Asteraceae, contain aspartic proteinases with milk clotting activity. Crude enzyme extracts with proteolytic activity were prepared from flowers of Arctium minus at pH 7.0, and were partially purified and characterized. Optimun bovine milk clotting activity was achieved with CaCl2 30 mM at 35 ºC. Inhibition of milk clotting activity was only promoted by pepstatin A, a highly selective inhibitor for aspartic peptidases. Analysis of crude extract by isoelectric focusing and zymogram showed an unique active band (pI 5.0). Molecular exclusion chromatography (Sephadex G-25 Fine) was employed to eliminate pigments and phenolic compounds, in order to obtain the partially purified extract (EE). Whey bovine hydrolyzates were performed with EE and analyzed by SDS-PAGE. Hydrolyzed whey was ultrafiltrated, and low molecular fractions (peptide mass ≤ 3000 Da) showed angiotensin-converting enzyme (ACE) inhibitory activity. Therefore, these peptides with antihypertensive activity could be potentially used in food industry for formulation of nutraceutical products.
publishDate 2010
dc.date.none.fl_str_mv 2010-06
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/11336/241720
Cimino, Cecilia Verónica; Liggieri, Constanza Silvina; Priolo, Nora Silvia; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth; Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products; Instituto de Investigación de las Ciencias Exactas Físicas y Naturales; Molecular Medicinal Chemistry; 21; 6-2010; 11-16
1666-888X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/241720
identifier_str_mv Cimino, Cecilia Verónica; Liggieri, Constanza Silvina; Priolo, Nora Silvia; Bruno, Mariela Anahí; Vairo Cavalli, Sandra Elizabeth; Arctium minus (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products; Instituto de Investigación de las Ciencias Exactas Físicas y Naturales; Molecular Medicinal Chemistry; 21; 6-2010; 11-16
1666-888X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.idecefyn.com.ar/MMC21PDF/vol_21__january.htm
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Instituto de Investigación de las Ciencias Exactas Físicas y Naturales
publisher.none.fl_str_mv Instituto de Investigación de las Ciencias Exactas Físicas y Naturales
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 13.229304

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