Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation

In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10....

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Autores principales: Hidalgo, María Eugenia, Folmer Côrrea, Ana Paula, Mancilla Canales, Manuel Arturo, Daroit, Daniel, Brandelli, Adriano, Risso, Patricia Hilda
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: Elsevier 2018
Materias:
Acceso en línea:http://hdl.handle.net/2133/10477
http://hdl.handle.net/2133/10477
Aporte de:
id I15-R121-2133-10477
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
orig_language_str_mv eng
topic Bacillus sp. P7
Bovine Sodium Caseinate
Hydrolysates
Bioactivity
Acid Aggregation and Gelation
Microstructure
spellingShingle Bacillus sp. P7
Bovine Sodium Caseinate
Hydrolysates
Bioactivity
Acid Aggregation and Gelation
Microstructure
Hidalgo, María Eugenia
Folmer Côrrea, Ana Paula
Mancilla Canales, Manuel Arturo
Daroit, Daniel
Brandelli, Adriano
Risso, Patricia Hilda
Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
topic_facet Bacillus sp. P7
Bovine Sodium Caseinate
Hydrolysates
Bioactivity
Acid Aggregation and Gelation
Microstructure
description In this work, we aimed at the production of bovine sodium caseinate (NaCAS) hydrolysates by means of an extracellular protease from Bacillus sp. P7. Mass spectrometry was carried out to evaluate peptide mass distribution and identified sequences of peptides with a signal/noise ratio higher than 10. Antioxidant and antimicrobial properties of hydrolysates were evaluated. An acid-induced aggregation process of the hydrolysates and their corresponding mixtures with NaCAS were also analyzed. The results showed that the enzymatic hydrolysis produced peptides, mostly lower than 3 kDa, with different bioactivities depending on the time of hydrolysis (ti). These hydrolysates lost their ability to aggregate by addition of glucono-delta-lactone, and their incorporation into NaCAS solutions alter the kinetics of the process. Also, the degree of compactness of the NaCAS aggregates, estimated by the fractal dimension of aggregates, was not significantly altered by the incorporation of hydrolysates. However, at higher protein concentrations, when the decrease in pH leads to the formation of NaCAS acid gels, the presence of hydrolysates alters the microstructure and rheological behavior of these gels.
format article
artículo
publishedVersion
author Hidalgo, María Eugenia
Folmer Côrrea, Ana Paula
Mancilla Canales, Manuel Arturo
Daroit, Daniel
Brandelli, Adriano
Risso, Patricia Hilda
author_facet Hidalgo, María Eugenia
Folmer Côrrea, Ana Paula
Mancilla Canales, Manuel Arturo
Daroit, Daniel
Brandelli, Adriano
Risso, Patricia Hilda
author_sort Hidalgo, María Eugenia
title Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
title_short Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
title_full Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
title_fullStr Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
title_full_unstemmed Biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
title_sort biological and physicochemical properties of bovine sodium caseinate hydrolysates obtained by a bacterial protease preparation
publisher Elsevier
publishDate 2018
url http://hdl.handle.net/2133/10477
http://hdl.handle.net/2133/10477
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