Please use this identifier to cite or link to this item: https://repositorio.uca.edu.ar/handle/123456789/8771
Título : Adsorption of chia proteins at interfaces : kinetics of foam and emulsion formation and destabilization
Autor : López, Débora 
Boeris, Valeria 
Spelzini, Darío 
Bonifacio, Carla 
Panizzolo, Luis A. 
Abirached, Cecilia 
Palabras clave : CHIAPROTEINAS VEGETALESCINETICAADSORCIONPHEMULSIONESPUMA
Fecha de publicación : 2019
Editorial : Elsevier
Cita : López 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/123456789/8771
Resumen : Abstract: 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.
URI : https://repositorio.uca.edu.ar/handle/123456789/8771
ISSN : 0927-7765 (impreso)
1873-4367 (online)
Disciplina: INGENIERIA EN ALIMENTOS
DOI: 10.1016/j.colsurfb.2019.04.067
Derechos: Acceso abierto. 2 años de embargo
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