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dc.rights.licenseopenen_US
dc.relation.isnodoubleb2960623-6b1a-40bd-a597-453d693380f7*
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorDRIDI, Wafa
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHARSCOAT SCHIAVO, Christelle
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorMONTEIL, Julien
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorFAURE, Chrystel
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLEAL-CALDERON, Fernando
dc.date.accessioned2020-04-10T08:58:46Z
dc.date.available2020-04-10T08:58:46Z
dc.date.issued2018
dc.identifier.issn0743-7463en_US
dc.identifier.other10.1021/acs.langmuir.8b02029en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4211
dc.description.abstractEnHexadecane-in-water emulsions were fabricated by means of a microfluidizer using two types of protein stabilizers, sodium caseinate (NaCAS) and beta-lactoglobulin (BLG). A study of the dependence of the mean droplet diameter and protein coverage on protein concentration was performed. At low protein concentrations, the emulsions were monodisperse and their mean droplet size was governed by the so-called limited-coalescence process. In this regime, the interfacial coverage was constant and was deduced from the linear evolution of the total interfacial area as a function of the amount of adsorbed proteins. In emulsions based on NaCAS, almost all the initial protein content was adsorbed at the interfaces. Emulsions formulated at very low protein content underwent unlimited coalescence after prolonged storage or when submitted to centrifugation. Additional NaCAS was incorporated in the continuous phase, right after the emulsification process, as a means of ensuring kinetic stability. The interfacial coverage increased after protein addition. Other strategies including acidification and salt addition were also probed to gain stability. Instead, in emulsions based on BLG, only partial adsorption of the initial protein content was observed. The corresponding emulsions remained kinetically stable against coalescence and no further addition of protein was required after emulsification. Our approach allows to obtain monodisperse, kinetically stable emulsions, and to master their average droplet size, while minimizing the amount of proteins.
dc.language.isoENen_US
dc.subject.enEmulsions
dc.subject.enInterfaces
dc.subject.enLiquids
dc.subject.enEmulsification
dc.subject.enStability
dc.title.enMonodisperse O/W emulsions stabilized by proteins: how to master the average droplet size and stability, while minimizing the amount of proteins
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.langmuir.8b02029
dc.subject.halChimie/Matériauxen_US
bordeaux.journalLangmuiren_US
bordeaux.page9228-9237en_US
bordeaux.volume34en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue31en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03184349
hal.version1
hal.date.transferred2021-03-29T11:53:12Z
hal.exporttrue
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