Partial Molecular Characterization of Arctium minus Aspartylendopeptidase and Preparation of Bioactive Peptides by Whey Protein Hydrolysis

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...

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Autores principales: Cimino, Cecilia Verónica, Colombo, María Laura, Liggieri, Constanza Silvina, Bruno, Mariela Anahí, Vairo Cavalli, Sandra Elizabeth
Formato: Articulo
Lenguaje:Inglés
Publicado: 2015
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Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/74527
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id I19-R120-10915-74527
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
Biología
angiotensin-converting enzyme, inhibitory activity, antioxidant capacity, arctiumisin, cloning, milk protein, typical plant aspartic protease
spellingShingle Ciencias Exactas
Biología
angiotensin-converting enzyme, inhibitory activity, antioxidant capacity, arctiumisin, cloning, milk protein, typical plant aspartic protease
Cimino, Cecilia Verónica
Colombo, María Laura
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
Partial Molecular Characterization of Arctium minus Aspartylendopeptidase and Preparation of Bioactive Peptides by Whey Protein Hydrolysis
topic_facet Ciencias Exactas
Biología
angiotensin-converting enzyme, inhibitory activity, antioxidant capacity, arctiumisin, cloning, milk protein, typical plant aspartic protease
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.
format Articulo
Articulo
author Cimino, Cecilia Verónica
Colombo, María Laura
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author_facet Cimino, Cecilia Verónica
Colombo, María Laura
Liggieri, Constanza Silvina
Bruno, Mariela Anahí
Vairo Cavalli, Sandra Elizabeth
author_sort Cimino, Cecilia Verónica
title Partial Molecular Characterization of Arctium minus Aspartylendopeptidase and Preparation of Bioactive Peptides by Whey Protein Hydrolysis
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
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/74527
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