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

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 pre...

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Autores principales: Cimino, Cecilia Verónica, Liggieri, Constanza Silvina, Priolo de Lufrano, Nora Silvia, Bruno, Mariela Anahí, Vairo Cavalli, Sandra Elizabeth
Formato: Articulo
Lenguaje:Inglés
Publicado: 2010
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/67028
http://www.idecefyn.com.ar/MMC21PDF/MMCV2104FIN.pdf
Aporte de:
id I19-R120-10915-67028
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Asteraceae
Péptidos
aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity
spellingShingle Ciencias Exactas
Asteraceae
Péptidos
aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity
Cimino, Cecilia Verónica
Liggieri, Constanza Silvina
Priolo de Lufrano, Nora Silvia
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
<i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
topic_facet Ciencias Exactas
Asteraceae
Péptidos
aspartic proteases, Asteraceae, whey hydrolyzates, ACE inhibitory activity
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.
format Articulo
Articulo
author Cimino, Cecilia Verónica
Liggieri, Constanza Silvina
Priolo de Lufrano, Nora Silvia
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author_facet Cimino, Cecilia Verónica
Liggieri, Constanza Silvina
Priolo de Lufrano, Nora Silvia
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author_sort Cimino, Cecilia Verónica
title <i>Arctium minus</i> (Hill) Bernh. (Asteraceae) aspartylendopeptidases with potential application in the formulation of nutraceutical products
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
publishDate 2010
url http://sedici.unlp.edu.ar/handle/10915/67028
http://www.idecefyn.com.ar/MMC21PDF/MMCV2104FIN.pdf
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