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dc.contributor.author
Lombardi, Julia
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Spelzini, Darío
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Corrêa, Ana Paula Folmer
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Brandelli, Adriano
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Risso, Patricia Hilda
dc.contributor.author
Boeris, Valeria
dc.date.available
2018-03-15T17:05:46Z
dc.date.issued
2015-12
dc.identifier.citation
Lombardi, Julia; Spelzini, Darío; Corrêa, Ana Paula Folmer ; Brandelli, Adriano; Risso, Patricia Hilda; et al.; Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 140; 12-2015; 452-459
dc.identifier.issn
0927-7765
dc.identifier.uri
http://hdl.handle.net/11336/38908
dc.description.abstract
Structural changes of casein micelles and their aggregation induced by a novel enzymatic pool isolated from Bacillus spp. in the presence of calcium, magnesium or zinc were investigated. The effect of cations on milk protein structure was studied using fluorescence and dynamic light scattering. In the presence of cations, milk protein structure rearrangements and larger casein micelle size were observed. The interaction of milk proteins with zinc appears to be of a different nature than that with calcium or magnesium. Under the experimental conditions assayed, the affinity of each cation for some groups present in milk proteins seems to play an important role, besides electrostatic interaction. On the other hand, the lowest aggregation times were achieved at the highest calcium and zinc concentrations (15 mM and 0.25 mM, respectively). The study found that the faster the aggregation of casein micelles, the less compact the gel matrix obtained. Cation concentrations affected milk protein aggregation kinetics and the structure of the aggregates formed.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Bacterial Enzyme
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Casein Micelle Aggregation
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Structural Changes
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Divalent Cations
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Otras Ciencias Químicas
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Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
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Astronomía
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Ciencias Físicas
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CIENCIAS NATURALES Y EXACTAS
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Biotecnología Industrial
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Biotecnología Industrial
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Milk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-05T20:46:17Z
dc.journal.volume
140
dc.journal.pagination
452-459
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Lombardi, Julia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Spelzini, Darío. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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Fil: Corrêa, Ana Paula Folmer. Universidade Federal do Rio Grande do Sul; Brasil
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Fil: Brandelli, Adriano. Universidade Federal do Rio Grande do Sul; Brasil
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Fil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Física de Rosario. Universidad Nacional de Rosario. Instituto de Física de Rosario; Argentina
dc.description.fil
Fil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Química e Ingeniería-Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.journal.title
Colloids and Surfaces B: Biointerfaces
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S092777651530401X
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.colsurfb.2015.12.052