Droplet microfluidics revolutionizes the way experiments and analyses are conducted in many fields of science, based on decades of basic research. Applied sciences are also impacted, opening new perspectives on how we look at complex matter. In particular, food and nutritional sciences still have many research questions unsolved, and conventional laboratory methods are not always suitable to answer them. In this review, we present how microfluidics have been used in these fields to produce and investigate various droplet-based systems, namely simple and double emulsions, microgels, microparticles, and microcapsules with food-grade compositions. We show that droplet microfluidic devices enable unprecedented control over their production and properties, and can be integrated in lab-on-chip platforms for in situ and time-resolved analyses. This approach is illustrated for on-chip measurements of droplet interfacial properties, droplet–droplet coalescence, phase behavior of biopolymer mixtures, and reaction kinetics related to food digestion and nutrient absorption. As a perspective, we present promising developments in the adjacent fields of biochemistry and microbiology, as well as advanced microfluidics–analytical instrument coupling, all of which could be applied to solve research questions at the interface of food and nutritional sciences.

Proteins are widely used to stabilize emulsions, and plant proteins have raised increasing interest for this purpose. The interfacial and emulsifying properties of proteins depend largely on their molecular properties. We used fluorescence spectroscopy to characterize the conformation of food proteins from different biological origins (dairy or pea) and transformation processes (commercial or lab-made isolates) in solution and at the oil–water interface. The fourth derivative of fluorescence spectra provided insights in the local environment of tryptophan (Trp) residues and thus in the protein structure. In emulsions, whey proteins adsorbed with their Trp-rich region at the oil–water interface. Proteins in the commercial pea isolate were present as soluble aggregates, and no changes in the local environment of the Trp residues were detected upon emulsification, suggesting that these structures adsorb without conformational changes. The lab-purified pea proteins were less aggregated and a Trp-free region of the vicilin adsorbed at the oil–water interface.

Animal- and plant-based proteins are present in a wide variety of raw and processed foods. They play an important role in determining the final structure of food matrices. Food proteins are diverse in terms of their biological origin, molecular structure, and supramolecular assembly. This diversity has led to segmented experimental studies that typically focus on one or two proteins but hinder a more general understanding of food protein structuring as a whole. In this review, we propose a unified view of how soft-matter physics can be used to control food protein assembly. We discuss physical models from polymer and colloidal science that best describe and predict the phase behavior of proteins. We explore the occurrence of phase transitions along two axes: increasing protein concentration and increasing molecular attraction. This review provides new perspectives on the link between the interactions, phase transitions, and assembly of proteins that can help in designing new food products and innovative food processing operations.

We investigated the liquid–liquid phase separation of wheat storage proteins with molecular weight (MW) ranging from 25 kg mol⁻¹ to 300 kg mol⁻¹. We characterized the onset of the phase separation upon a temperature decrease by turbidity. The protein compositions at equilibrium after temperature quenches were additionally determined by size-exclusion-high performance liquid chromatography. We found that wheat proteins can be classified into two classes according to their phase behaviour. The partition of the proteins between the two phases depends on their MW above a critical size of 45 kg mol⁻¹. For those high MW proteins, we observed that the behaviour is similar to the one of neutral, linear polymers. Their partition and critical parameters are well described by Flory–Huggins theory. Proteins below 45 kg mol⁻¹, namely α-, β-and γ-gliadins, have similar interaction potentials under the physico-chemical conditions tested. Their phase diagrams, characterized by a low value of critical volume fraction, are characteristic of long-range interactions. Wheat protein behaviour can resultantly be rationalized in a much simpler way than expected from their complex composition.