Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool

Structural changes of casein micelles and their aggregation induced by a novel enzymatic pool isolatedfrom Bacillus spp. in the presence of calcium, magnesium or zinc were investigated. The effect of cationson milk protein structure was studied using fluorescence and dynamic light scattering. In the...

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Autores principales: Lombardi, Julia, Spelzini, Darío, Folmer Côrrea, Ana Paula, Brandelli, Adriano, Risso, Patricia Hilda, Boeris, Valeria
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: Elsevier 2018
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Acceso en línea:http://hdl.handle.net/2133/11426
http://hdl.handle.net/2133/11426
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id I15-R121-2133-11426
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 Bacterial Enzyme
Casein Micelle Aggregation
Structural Changes
Divalent Cations
spellingShingle Bacterial Enzyme
Casein Micelle Aggregation
Structural Changes
Divalent Cations
Lombardi, Julia
Spelzini, Darío
Folmer Côrrea, Ana Paula
Brandelli, Adriano
Risso, Patricia Hilda
Boeris, Valeria
Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
topic_facet Bacterial Enzyme
Casein Micelle Aggregation
Structural Changes
Divalent Cations
description Structural changes of casein micelles and their aggregation induced by a novel enzymatic pool isolatedfrom Bacillus spp. in the presence of calcium, magnesium or zinc were investigated. The effect of cationson milk protein structure was studied using fluorescence and dynamic light scattering. In the presenceof cations, milk protein structure rearrangements and larger casein micelle size were observed. Theinteraction of milk proteins with zinc appears to be of a different nature than that with calcium ormagnesium. Under the experimental conditions assayed, the affinity of each cation for some groupspresent in milk proteins seems to play an important role, besides electrostatic interaction. On the otherhand, the lowest aggregation times were achieved at the highest calcium and zinc concentrations (15 mMand 0.25 mM, respectively). The study found that the faster the aggregation of casein micelles, the lesscompact the gel matrix obtained. Cation concentrations affected milk protein aggregation kinetics andthe structure of the aggregates formed.
format article
artículo
publishedVersion
author Lombardi, Julia
Spelzini, Darío
Folmer Côrrea, Ana Paula
Brandelli, Adriano
Risso, Patricia Hilda
Boeris, Valeria
author_facet Lombardi, Julia
Spelzini, Darío
Folmer Côrrea, Ana Paula
Brandelli, Adriano
Risso, Patricia Hilda
Boeris, Valeria
author_sort Lombardi, Julia
title Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
title_short Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
title_full Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
title_fullStr Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
title_full_unstemmed Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
title_sort milk protein suspensions enriched with three essential minerals: physicochemical characterization and aggregation induced by a novel enzymatic pool
publisher Elsevier
publishDate 2018
url http://hdl.handle.net/2133/11426
http://hdl.handle.net/2133/11426
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