<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
- Autores
- Cimino, Cecilia Verónica; Liggieri, Constanza Silvina; Priolo de Lufrano, 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.
Facultad de Ciencias Exactas - Materia
-
Ciencias Exactas
Asteraceae
Péptidos
aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-nd/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/67028
Ver los metadatos del registro completo
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<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical productsCimino, Cecilia VerónicaLiggieri, Constanza SilvinaPriolo de Lufrano, Nora SilviaBruno, Mariela AnahíVairo Cavalli, Sandra ElizabethCiencias ExactasAsteraceaePéptidosaspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activityFood 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.Facultad de Ciencias Exactas2010-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf11-16http://sedici.unlp.edu.ar/handle/10915/67028enginfo:eu-repo/semantics/altIdentifier/url/http://www.idecefyn.com.ar/MMC21PDF/MMCV2104FIN.pdfinfo:eu-repo/semantics/altIdentifier/issn/1666-888Xinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:10:10Zoai:sedici.unlp.edu.ar:10915/67028Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:10:10.491SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products |
title |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products |
spellingShingle |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products Cimino, Cecilia Verónica Ciencias Exactas Asteraceae Péptidos aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity |
title_short |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products |
title_full |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products |
title_fullStr |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products |
title_full_unstemmed |
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products |
title_sort |
<i>Arctium minus</i> (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 de Lufrano, Nora Silvia Bruno, Mariela Anahí Vairo Cavalli, Sandra Elizabeth |
author |
Cimino, Cecilia Verónica |
author_facet |
Cimino, Cecilia Verónica Liggieri, Constanza Silvina Priolo de Lufrano, Nora Silvia Bruno, Mariela Anahí Vairo Cavalli, Sandra Elizabeth |
author_role |
author |
author2 |
Liggieri, Constanza Silvina Priolo de Lufrano, Nora Silvia Bruno, Mariela Anahí Vairo Cavalli, Sandra Elizabeth |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Ciencias Exactas Asteraceae Péptidos aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity |
topic |
Ciencias Exactas Asteraceae Péptidos aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity |
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. Facultad de Ciencias Exactas |
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 |
2010-04 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo 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://sedici.unlp.edu.ar/handle/10915/67028 |
url |
http://sedici.unlp.edu.ar/handle/10915/67028 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
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openAccess |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) |
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