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dc.provenanceUniversidad Nacional de Rosario.RepHipUNR-
dc.creatorLombardi, Julia-
dc.creatorSpelzini, Darío-
dc.creatorFolmer Côrrea, Ana Paula-
dc.creatorBrandelli, Adriano-
dc.creatorRisso, Patricia Hilda-
dc.creatorBoeris, Valeria-
dc.date2015-12-27-
dc.date2015-12-27-
dc.date.accessioned2019-07-15T19:04:55Z-
dc.date.available2019-07-15T19:04:55Z-
dc.date.issued2015-12-27-
dc.date.issued2015-12-27-
dc.identifier0927-7765-
dc.identifierhttp://hdl.handle.net/2133/11426-
dc.identifierhttp://hdl.handle.net/2133/11426-
dc.identifier.urihttp://rodna.bn.gov.ar/jspui/handle/bnmm/570830-
dc.descriptionStructural 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.-
dc.descriptionFil: Lombardi, Julia. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.-
dc.descriptionFil: Lombardi, Julia. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina.-
dc.descriptionFil: Spelzini, Darío. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.-
dc.descriptionFil: Spelzini, Darío. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina.-
dc.descriptionFil: Folmer Côrrea, Ana Paula. Universidade Federal de Rio Grande do Sul. Instituto de Ciência e Tecnologia de Alimentos. Laboratório de Bioquimica e Microbiologia Aplicada; Brasil.-
dc.descriptionFil: Brandelli, Adriano. Universidade Federal de Rio Grande do Sul. Instituto de Ciência e Tecnologia de Alimentos. Laboratório de Bioquimica e Microbiologia Aplicada; Brasil.-
dc.descriptionFil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Física Rosario (IFIR-CONICET); Argentina.-
dc.descriptionFil: Risso, Patricia Hilda. Universidad Nacional de Rosario. Facultad de Ciencias Veterinarias; Argentina.-
dc.descriptionFil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas; Argentina.-
dc.descriptionFil: Boeris, Valeria. Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; Argentina.-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherElsevier-
dc.relationhttps://www.sciencedirect.com/science/article/pii/S092777651530401X?via%3Dihub-
dc.relationhttp://dx.doi.org/10.1016/j.colsurfb.2015.12.052-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.sourcereponame:RepHipUNR (UNR)-
dc.sourceinstname:Universidad Nacional de Rosario-
dc.sourceinstacron:UNR-
dc.source.urihttp://hdl.handle.net/2133/11426-
dc.subjectBacterial Enzyme-
dc.subjectCasein Micelle Aggregation-
dc.subjectStructural Changes-
dc.subjectDivalent Cations-
dc.titleMilk protein suspensions enriched with three essential minerals: Physicochemical characterization and aggregation induced by a novel enzymatic pool-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeartículo-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: Universidad Nacional de Rosario. RepHipUNR

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