dc.creatorHuck-Iriart
dc.creatorCristian; Montes-de-Oca-Avalos
dc.creatorJuan; Lidia Herrera
dc.creatorMaria; Jorge Candal
dc.creatorRoberto; Pinto-de-Oliveira
dc.creatorCristiano Luis; Linares-Torriani
dc.creatorIris
dc.date2016
dc.datenov
dc.date2017-11-13T13:13:01Z
dc.date2017-11-13T13:13:01Z
dc.date.accessioned2018-03-29T05:51:06Z
dc.date.available2018-03-29T05:51:06Z
dc.identifierFood Research International. Elsevier Science Bv, v. 89, p. 338 - 346, 2016.
dc.identifier0963-9969
dc.identifier1873-7145
dc.identifierWOS:000388775500033
dc.identifier10.1016/j.foodres.2016.08.026
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S0963996916303519
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/326981
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1364006
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFlocculation process was studied in emulsions formulated with 10 wt.% sunflower oil, 2, 5 or 7.5 wt.% NaCas, and with or without addition of sucrose (0, 5, 10, 15, 20 or 30 wt.%). Two different processing conditions were used to prepare emulsions: ultraturrax homogenization or further homogenization by ultrasound. Emulsions with droplets with diameters above (coarse) or below (fine) 1 pm were obtained. Emulsions were analyzed for droplet size distribution by static light scattering (SLS), stability by Turbiscan, and structure by confocal laser scanning microscopy (CLSM) and small angle X-ray scattering (SAXS). SAXS data were fitted by a theoretical model that considered a system composed of poly dispersed spheres with repulsive interaction and presence of aggregates. Flocculation behavior was caused by the self-assembly properties of NaCas, but the process was more closely related to interfacial protein content than micelles concentration in the aqueous phase. The results indicated that casein aggregation was strongly affected by disaccharide addition, hydrophobic interaction of the emulsion droplets, and interactions among interfacial protein molecules. The structural changes detected in the protein micelles in different environments allowed understanding the macroscopic physical behavior observed in concentrated NaCas emulsions. (C) 2016 Elsevier Ltd. All rights reserved.
dc.description89
dc.descriptionpart 1
dc.description338
dc.description346
dc.descriptionCONICET [PIP 11220110101025]
dc.descriptionNational Agency for the Promotion of Science and Technology (ANPCyT) [PICT 2013-0897]
dc.descriptionUniversity of Buenos Aires [UBA-20020130100136BA]
dc.descriptionFAPESP [2010/09277-7]
dc.descriptionCNPq
dc.descriptionSynchrotron Light National Laboratory (LNLS, Campinas, Brazil) [D11A-SAXS1-14296]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageEnglish
dc.publisherElsevier Science BV
dc.publisherAmsterdam
dc.relationFood Research International
dc.rightsfechado
dc.sourceWOS
dc.subjectSodium Caseinate
dc.subjectDisaccharides
dc.subjectEmulsions
dc.subjectFlocculation
dc.subjectSaxs
dc.subjectTurbiscan
dc.titleNew Insights About Flocculation Process In Sodium Caseinate-stabilized Emulsions
dc.typeArtículos de revistas


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