Phase separation dynamics of gluten protein mixtures
2019
Banc, Amélie | Pincemaille, Justine | Costanzo, Salvatore | Chauveau, Edouard | Appavou, Marie-Sousai | Morel, Marie Helene | Menut, Paul | Ramos, Laurence | Laboratoire Charles Coulomb (L2C) ; Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) | Ingénierie des Agro-polymères et Technologies Émergentes (UMR IATE) ; Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Institut National de la Recherche Agronomique (INRA)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro) | Forschungszentrum Jülich = Research Center Juelich (FZ Juelich) | Ingénierie, Procédés, Aliments (GENIAL) ; Institut National de la Recherche Agronomique (INRA)-AgroParisTech | Labex Numev (ANR-10-LAB-20) | ANR-10-LABX-0020,NUMEV,Digital and Hardware Solutions and Modeling for the Environement and Life Sciences(2010)
We investigate by time-resolved synchrotron ultra-small X-ray scattering the dynamics of liquid–liquid phase-separation (LLPS) of gluten protein suspensions following a temperature quench. Samples at a fixed concentration (237 mg ml$^{−1}$) but with different protein compositions are investigated. In our experimental conditions, we show that fluid viscoelastic samples depleted in polymeric glutenin phase-separate following a spinodal decomposition process. We quantitatively probe the late stage coarsening that results from a competition between thermodynamics that speeds up the coarsening rate as the quench depth increases and transport that slows down the rate. For even deeper quenches, the even higher viscoelasticity of the continuous phase leads to a “quasi” arrested phase separation. Anomalous phase-separation dynamics is by contrast measured for a gel sample rich in glutenin, due to elastic constraints. This work illustrates the role of viscoelasticity in the dynamics of LLPS in protein dispersions.
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