Influence of pH and lipid membrane on the liquid-liquid phase separation of wheat γ-gliadin in aqueous conditions.

Protein body (PB) formation in wheat seeds is a critical process influencing seed content and nutritional quality. In this study, we investigate the potential mechanisms governing PB formation through an in vitro approach, focusing on γ-gliadin, a key wheat storage protein. We used a microfluidic technique to encapsulate γ-gliadin within giant unilamellar vesicles (GUVs) and tune the physicochemical conditions in a controlled and rapid way. We examined the influence of pH and protein concentration on LLPS and protein-membrane interactions using various microscopy and spectroscopy techniques. We showed that γ-gliadin encapsulated in GUVs can undergo a pH-triggered liquid-liquid phase separation (LLPS) by two distinct mechanisms depending on the γ-gliadin concentration. At low protein concentrations, γ-gliadins phase separate by a nucleation and growth-like process, while, at higher protein concentration and pH above 6.0, γ-gliadin formed a bi-continuous phase suggesting a spinodal decomposition-like mechanism. Fluorescence and microscopy data suggested that γ-gliadin dense phase exhibited affinity for the GUV membrane, forming a layer at the interface and affecting the reversibility of the phase separation.

Oil core microcapsules by inverse gelation technique.

A promising technique for oil encapsulation in Ca-alginate capsules by inverse gelation was proposed by Abang et al. This method consists of emulsifying calcium chloride solution in oil and then adding it dropwise in an alginate solution to produce Ca-alginate capsules. Spherical capsules with diameters around 3 mm were produced by this technique, however the production of smaller capsules was not demonstrated. The objective of this study is to propose a new method of oil encapsulation in a Ca-alginate membrane by inverse gelation. The optimisation of the method leads to microcapsules with diameters around 500 µm. In a search of microcapsules with improved diffusion characteristics, the size reduction is an essential factor to broaden the applications in food, cosmetics and pharmaceuticals areas. This work contributes to a better understanding of the inverse gelation technique and allows the production of microcapsules with a well-defined shell-core structure.

Microfluidics-assisted diffusion self-assembly: toward the control of the shape and size of pectin hydrogel microparticles.

We demonstrated the generation of pectin hydrogel microparticles having complex shapes either by combining the phenomenon of gelation and water diffusion-induced self-assembly in microfluidic channels (on-chip) or by the deformation of the pregelled droplets outside the channels (off-chip) at a fluid-fluid interface. We proved that by tuning the mode of pectin cross-linking (CaCl2 vs CaCO3) and the degree of shrinking (water content in the dimethyl carbonate (DMC) organic continuous phase) we can control the shape of the final particle. Sphere, doughnut, oblate ellipsoid, or mushroom-type morphologies were thus produced, demonstrating the ability to control the formation of anisotropic biopolymer-based hydrogel microparticles using microfluidics. Shape changes were explained by the redistribution of calcium ions in combination with the local Peclet number experienced by the microdroplets during the on-chip process. Moreover, during the off-chip process, the interplay between elastic and viscous forces for microdroplets entering the CaCl2-DMC interface caused deformation of the pregelled droplets to occur and therefore resulted in the formation of microparticles with a mushroom-like morphology.

Tuning silica particle shape at fluid interfaces.

By exploring the phenomenon of water diffusion induced self-assembly of silica particle in microfluidic channels, we show that both the geometric confinement experienced by the droplet and the local Peclet number are responsible for the final particle shape. This study will facilitate the understanding and ultimately control of self assembly at fluid interfaces.