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....
Autores principales: | , , , , , |
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Formato: | article artículo publishedVersion |
Lenguaje: | Inglés |
Publicado: |
Elsevier
2018
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Materias: | |
Acceso en línea: | http://hdl.handle.net/2133/10477 http://hdl.handle.net/2133/10477 |
Aporte de: |
id |
I15-R121-2133-10477 |
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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 |
work_keys_str_mv |
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bdutipo_str |
Repositorios |
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1764820408406638594 |