High-Pressure Homogenization Effects on Protein Emulsions

High-pressure homogenization (HPH) is a robust mechanical process that forces protein–oil mixtures through narrow gaps at pressures up to several hundred megapascals, generating intense shear, turbulence and cavitation. These forces reduce droplet size, unfold protein structures and promote adsorption at oil–water interfaces, thereby enhancing emulsion stability, surface activity and functional performance. Structural alterations include disruption of non-covalent bonds, exposure of hydrophobic patches and changes in secondary conformation, which collectively improve solubility, interfacial tension reduction and resistance to coalescence. Rheological behaviour is often modified, yielding emulsions with tailored viscosity or gel-like characteristics. Applications span food formulation—where improved mouthfeel, shelf-life and nutrient delivery are sought—to pharmaceuticals and cosmetics, where controlled release and nanoscale delivery systems are critical. HPH thus represents a versatile tool for designing protein-stabilised emulsions with precisely tuned techno-functional properties and broad commercial relevance.

Research from Nature Portfolio

No recent Nature Portfolio content available.

High-Pressure Homogenization Effects on Protein Emulsions publication trend

The graph below shows the total number of articles in high-pressure homogenization effects on protein emulsions across all publications each year (not limited to Nature Index journals).

Technical terms

High-pressure homogenization: A mechanical process that applies very high pressure to force mixtures through narrow channels, generating shear and cavitation to reduce particle size and alter molecular structures.

Emulsion: A dispersion of one liquid into another immiscible liquid, typically oil droplets within water, stabilised by surface-active agents such as proteins.

Zeta potential: The electrical potential at the slipping plane of a particle in suspension, reflecting surface charge and predicting colloidal stability against aggregation.

Surface hydrophobicity: A measure of the degree to which hydrophobic regions of a protein are exposed at an interface, influencing adsorption strength and emulsion formation.

References

1. The Effect of High Pressure Homogenization on the Structure of Dual-Protein and Its Emulsion Functional Properties. Foods (2023).
2. Physicochemical, conformational and functional changes of quinoa protein affected by high-pressure homogenization. LWT (2023).
3. Effects of high-pressure homogenization on physicochemical and functional properties of enzymatic hydrolyzed soybean protein concentrate. Frontiers in Nutrition (2022).