Role of egg white protein particles’ structure and interface profiles in tailoring high-internal-phase Pickering emulsions with desired applicability

Tailoring food-grade high-internal-phase Pickering emulsions (HIPPEs) with desired applicability has been extremely hindered due to the limited stabilization mechanism deciphering. This study illustrated the specific role of egg white protein (EWP) particlesꞌ structure and interface distribution to the stabilization of HIPPEs. Herein, gelation induced EWP aggregation into its microgel particles (EWPG) with apparent conformation transition (α-helix to β-sheet) and surface activity improvement (e.g., hydrophobicity, interface tension, and wettability). Besides, larger EWPG tended to sparsely absorb on the HIPPEsꞌ interface and achieve admirable long-term stability (6-month storage and 18-days lipid oxidation), owing to higher particle rigidity and steric repulsion. Comparably, EWP (small, soft, and rough) was superior in ready-to-use HIPPEs with centrifugation, freeze-thawing, and nutraceutical delivery demands, accompanied by a stronger rattan-like interfacial network with higher viscoelasticity. Overall, this research would facilitate the facile design of food matrices (e.g., EWP)-based HIPPEs via the gelation-tailored balance of particle structure and interface distribution. •EWPG with larger protein aggregates tended to form a sparse interfacial film.•EWPG (large, rigid, and smooth) could stabilize HIPPEs with long-storage demands.•Rattan-like EWP network improved viscoelasticity and bioaccessibility of HIPPEs.•EWP (small, soft, and rough) was more suitable in forming ready-to-use HIPPEs.•Complex processing could be a double-edged sword for EWP in forming HIPPEs.