Interfacial Dynamics of Protein Emulsions

Protein emulsions arise when amphiphilic proteins adsorb at the boundary between oil and water, creating stable dispersions of one liquid phase within another. The interfacial dynamics of these systems encompass the sequence of events by which proteins migrate to, unfold at and reorganise on the oil–water interface, forming viscoelastic films that prevent droplet coalescence. Key determinants include protein structure and flexibility, concentration, solution pH, ionic strength and processing aids such as ultrasound or salts. At the interface, hydrophobic residues anchor into the oil phase while polar regions remain solvated, yielding a mechanically robust network. Time-dependent changes in interfacial tension and film thickness govern droplet size and stability, and rheological properties of the continuous phase further modulate droplet interactions. Advances in spectroscopic and microscopic techniques have provided insight into molecular conformations at the interface, while interfacial rheometry has quantified film viscoelasticity. Applications span food formulations, pharmaceuticals and cosmetics, where tailor-made emulsions deliver bioactive compounds, enhance texture or improve shelf life. Understanding the interfacial dynamics of protein emulsions is thus essential for rational design of functional and sustainable colloidal systems.

Research from Nature Portfolio

No recent Nature Portfolio content available.

Interfacial Dynamics of Protein Emulsions publication trend

The graph below shows the total number of articles in interfacial dynamics of protein emulsions across all publications each year (not limited to Nature Index journals).

Technical terms

Emulsion: A mixture of two immiscible liquids (oil and water) in which one is dispersed as droplets in the other under the action of surface-active agents.

Oil–water interface: The boundary region between oil droplets and the surrounding aqueous phase where amphiphilic molecules adsorb and assemble.

Interfacial tension: The force per unit length resisting deformation of the interface; its reduction by proteins is crucial for droplet formation.

Adsorption kinetics: The rate at which proteins diffuse to and attach on the interface, affecting film build-up and droplet stability.

Interfacial rheology: Study of the viscoelastic properties of the interfacial film, which governs resistance to droplet coalescence under flow.

Surface hydrophobicity: The tendency of protein regions to avoid water and partition into the oil phase, driving anchoring at the interface.

Protein unfolding: Structural rearrangement of globular proteins at the interface, exposing hydrophobic residues to stabilise the emulsion film.

Coalescence: The process by which droplets merge when the interfacial film is insufficiently elastic or continuous to prevent film rupture.

References

1. Role of Medium-Chain Triglycerides on the Emulsifying Properties and Interfacial Adsorption Characteristics of Pork Myofibrillar Protein. Foods (2025).
2. The Improvement of Dispersion Stability and Bioaccessibility of Calcium Carbonate by Solid/Oil/Water (S/O/W) Emulsion. Foods (2022).
3. Role of protein-lipid interactions for food and food-based applications. Food Hydrocolloids (2025).