LAUSR

There is an increasing interest in the development of high internal phase emulsions (HIPE) stabilized by food-grade nanoparticles due to their potential applications in the food industry. In this study, cross-linked egg white protein isolates (cEPIs) are prepared by adding 10 u/g, 20 u/g, and 40 u/g of transglutaminase (TG), and the impacts of interface properties of cEPIs and emulsifying of HIPEs are investigated. Relative to the native EPI, the cEPIs have more irregular and agglomerated morphology, and the turbidity and hydrophobicity are significantly increased. The particle size and zeta potential of cEPIs considerably varied with the addition of TG. In HIPE, the formation, physical properties, and microstructure are characterized by visual observations, the Turbiscan stability index, and CLSM. The results indicated that stable and gel-like HIPEs are formed by cEPIs at oil internal phase (φ) values of 0.75–0.90. Especially for the enzyme additions of 20 u/g, the cEPIs had the best storage stability and the lowest TSI value (2.50) and formed a gel network structure at φ values of 0.9 microscopically. Overall, this study can enrich the theoretical frame of interface properties by enzyme treatment. Besides, it would be of great importance for the research of HIPE stabilized by cEPIs appropriate to be applied in food formulations.