Please use this identifier to cite or link to this item: https://repositorio.uca.edu.ar/handle/123456789/8771
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dc.contributor.authorLópez, Déboraes
dc.contributor.authorBoeris, Valeriaes
dc.contributor.authorSpelzini, Daríoes
dc.contributor.authorBonifacio, Carlaes
dc.contributor.authorPanizzolo, Luis A.es
dc.contributor.authorAbirached, Ceciliaes
dc.date.accessioned2019-09-19T20:26:22Z-
dc.date.available2019-09-19T20:26:22Z-
dc.date.issued2019-
dc.identifier.citationLópez DN, Boeris V, Spelzini D, Bonifacino C, Panizzolo LA, Abirached C. Adsorption of chia proteins at interfaces : kinetics of foam and emulsion formation and destabilization [en línea]. Colloids and Surfaces B: Biointerfaces. 2019;180:503–507. doi:10.1016/j.colsurfb.2019.04.067 Disponible en: https://repositorio.uca.edu.ar/handle/123456789/8771es
dc.identifier.issn0927-7765 (impreso)-
dc.identifier.issn1873-4367 (online)-
dc.identifier.urihttps://repositorio.uca.edu.ar/handle/123456789/8771-
dc.description.abstractAbstract: Chia proteins were extracted by solubilisation at pH 10 or 12 and precipitated at pH 4.5. Isolates were named as CPI10 and CPI12, according to their extraction pH, 10 or 12, respectively. The surface properties of both isolates were studied at neutral conditions. Foams were formed by air bubbling and both the formation and destabilization processes were analysed by conductimetry. The extraction pH significantly affected the interfacial properties of chia proteins. The higher surface hydrophobicity in CPI10 led to more flexible proteins with improved foaming properties. Foams formed by CPI10 were more stable than those by CPI12 due to the formation of a thicker interfacial film, which meant a greater ability to retard liquid drainage. Freshly-made coarse emulsions stabilized with CPI12 showed a lower mean droplet size and a significantly lower degree of overall destabilization than those stabilized with CPI10. None of the two emulsions showed flocculating effect.es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherElsevieres
dc.rightsAcceso abierto. 2 años de embargo*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.sourceColloids and Surfaces B: Biointerfaces. 2019;180:503–507es
dc.subjectCHIAes
dc.subjectPROTEINAS VEGETALESes
dc.subjectCINETICAes
dc.subjectADSORCIONes
dc.subjectPHes
dc.subjectEMULSIONes
dc.subjectESPUMAes
dc.titleAdsorption of chia proteins at interfaces : kinetics of foam and emulsion formation and destabilizationes
dc.typeArtículoes
dc.identifier.doi10.1016/j.colsurfb.2019.04.067-
uca.disciplinaINGENIERIA EN ALIMENTOSes
uca.issnrd1es
uca.affiliationFil: López, Débora N. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Física; Argentinaes
uca.affiliationFil: López, Débora N. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; Argentinaes
uca.affiliationFil: Boeris, Valeria. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química Física; Argentinaes
uca.affiliationFil: Boeris, Valeria. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; Argentinaes
uca.affiliationFil: Spelzini, Darío. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Física Química; Argentinaes
uca.affiliationFil: Spelzini, Darío. Pontificia Universidad Católica Argentina. Facultad de Química e Ingeniería del Rosario; Argentinaes
uca.affiliationFil: Bonifacio, Carla. Universidad de la República. Facultad de Química. Departamento de Ciencia y Tecnología de los Alimentos; Uruguayes
uca.affiliationFIl: Panizzolo, Luis A. Universidad de la República. Facultad de Química. Departamento de Ciencia y Tecnología de los Alimentos; Uruguayes
uca.affiliationFil: Abirached, Cecilia. Universidad de la República. Facultad de Química. Departamento de Ciencia y Tecnología de los Alimentos; Uruguayes
uca.versionacceptedVersiones
item.languageiso639-1en-
item.fulltextWith Fulltext-
item.grantfulltextembargo_20210919-
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