Poly(N-isopropylacrylamide)-based microgels are soft colloids undergoing a Volume Phase Transition (VPT) close to ambient temperature. Although widely employed for fundamental research and application purposes, the modifications of the microgel internal structure occurring at the VPT are not yet completely understood, especially concerning the role of electrostatics. Here we study in detail, both experimentally and numerically, the effect of the addition of acrylic acid (AAc) co-monomer on the microgel deswelling process. By combining viscosimetry, light scattering and electrophoresis, we show that the progressive addition of AAc increases the microgel mass and suppresses

Understanding the origin of the unique rheological properties of wheat gluten, the protein fraction of wheat grain, is crucial in bread-making processes and has raised questions of scientists for decades. Gluten is a complex mixture of two families of proteins, monomeric gliadins and polymeric glutenins. To better understand the respective role of the different classes of proteins in the supramolecular structure of gluten and its link to the material properties, we investigate here concentrated dispersions of gluten proteins in water with a fixed total protein concentration but variable composition in gliadin and glutenin. Linear viscoelasticity measurements show a gradual increase in the viscosity of the samples as the glutenin mass content increases from 7 to 66%. While the gliadin-rich samples are microphase-separated viscous fluids, homogeneous and transparent pre-gel and gels are obtained with the replacement of gliadin by glutenin. To unravel the flow properties of the gluten samples, we perform shear startup experiments at different shear-rates. In accordance with the linear viscoelastic signature, three classes of behavior are evidenced depending on the protein composition. As samples get depleted in gliadin and enriched in glutenin, distinctive features are measured: (i) viscosity undershoot suggesting droplet elongation for microphase-separated dispersions, (ii) stress overshoot and partial structural relaxation for near-critical pre-gels, and (iii) strain hardening and flow instabilities of gels. We discuss the experimental results by analogy with the behavior of model systems, including viscoelastic emulsions, branched polymer melts, and critical gels, and provide a consistent physical picture of the supramolecular features of the three classes of protein dispersions.

The key parameter controlling the glass transition of colloidal suspensions is ϕ, the fraction of the sample volume occupied by the particles. Unfortunately, changing ϕ by varying an external parameter, e.g. temperature T as in molecular glass formers, is not possible, unless one uses thermosensitive colloidal particles, like the popular poly(Nisopropylacrylamide) (PNiPAM) microgels. These however have several drawbacks, including high deformability, osmotic deswelling and interpenetration, which complicate their use as a model system to study the colloidal glass transition. Here, we propose a new system consisting of a colloidal suspension of non-deformable spherical silica nanoparticles, in which PNiPAM hydrogel spheres of ∼ 100 − 200 µm size are suspended. These non-colloidal 'mesogels' allow for controlling the sample volume effectively available to the silica nanoparticles and hence their ϕ, thanks to the T-induced change in mesogels volume. Using optical microscopy, we first show that the mesogels retain their ability to change size with T when suspended in Ludox suspensions, similarly as in water. We then show that their size is independent of the sample thermal history, such that a well-defined, reversible relationship between T and ϕ may be established. Finally, we use space-resolved dynamic light scattering to demonstrate that, upon varying T , our system exhibits a broad range of dynamical behaviors across the glass transition and beyond, comparable with those exhibited by a series of distinct silica nanoparticle suspensions of various ϕ.

Wheat gluten includes two major proteins classes, gliadin (25–60 kg/mol) and glutenin polymers (100 to > 2,000 kg/mol) each comprising several polypeptides routinely identified by size-exclusion chromatography and electrophoresis. Gluten proteins are rich in glutamine (30%) and contain several repeated sequences, linking them to the wide class of intrinsically disordered protein (IDP). Here we showed that an ethanol/water (EtOH/W, 50/50, v/v) extract of an industrial gluten, comprising 1/3 of glutenin polymers and 2/3 of gliadin, underwent liquid-liquid phase separation (LLPS) below 14 °C, leading to two coexisting phases, respectively rich and poor in protein. As the quenching depth increased, proteins of lower and lower molecular weight joined the rich phase, akin to what would have been obtained for a polydisperse polymer sample. Within the rich phase the mass ratio of glutenin over gliadin decreased from 2.5 to 0.5 as the temperature dropped from 14 °C to −0.8 °C. Concomitantly the concentration in glutenin polymers increased up to 143 ± 6 g/L (at 9 °C) and then stopped to evolve, suggesting that the binodal line intersected the gelation line below this temperature. Applying the Flory-Huggins (FH) lattice model for each gluten protein classes, we demonstrated that their partitioning in the coexisting phases followed a same temperature dependency. However, some gliadin species joined the rich phase above their critical temperature. Here, specific interactions with the glutenin polymers through weak forces were exemplified. The study demonstrated the relevance of the Flory-Huggins (FH) lattice model in predicting phase behavior even when applied to complex protein mixtures.