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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/241720
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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 Técnicas2025-09-29T09:34:55Zoai: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:34982025-09-29 09:34:55.276CONICET 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 |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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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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1844613084173303808 |
score |
13.070432 |