Abstract The effect of hydrothermal treatments, high‐pressure homogenization (HPH) and their combined effects on faba bean protein isolate (FBI) and concentrate (FBC) dispersions was investigated. With HPH, a significant reduction in particle size was observed for FBI but not for FBC. For FBI, dispersion stability under accelerated gravitation was significantly improved by both hydrothermal and HPH. For FBC, hydrothermal treatment had a negative effect on dispersion stability unless it was combined with HPH. The protein dispersibility of FBI increased, and FBC decreased with increasing temperature. Upon HPH, the protein dispersibility of FBI dramatically improved, making it almost completely soluble. All FBI dispersions had a higher surface charge compared to FBC. SDS PAGE profile showed strong protein crosslinking in the original FBI, leading to a loss of legumin and vicilin bands, which were visible in a more native state of FBC. Physical modifications did not significantly affect the viscosities except for a significant increase in FBC heated at 75°C due to starch gelatinization. The equilibrium interfacial tension of the modified FBI was significantly lower than the FBC. Analysis of dynamic interfacial adsorption showed that FBI had a much faster initial diffusion (beyond detection limit) towards the interface than FBC. Physical modifications improved the surface hydrophobicity of the proteins, leading to faster interfacial adsorption. Overall, FBI dispersions had improved functional properties compared to FBC, and HPH had a more significant effect than hydrothermal treatments. Physically modified FBI could be a promising emulsifier in various food applications.

The effect of heat treatment and high‐pressure homogenization on the dispersibility and interfacial behavior of faba bean protein isolate and concentrate