Protein particle-stabilized emulsions often lack thermal stability, impacting their industrial use. This study investigated the effects of genipin (GP)-zein cross-linked particles with varying GP-to-protein weight ratios (0/0.02/0.1:1) on emulsion thermal stability. Enhanced stability was observed at the GP level of 0.1. Heat treatment increased the covalent cross-linking in raw particles and emulsions. Isolated particles from heated emulsions grew in size (micrometer scale) with higher GP levels, unlike heated raw particles (nanoscale). GP-protein cross-linking reduced the droplet-droplet and particle-emulsifier interactions in the heated emulsion. Spectroscopic analysis and electrophoresis revealed that GP-zein cross-linking increased protein structural stability and inhibited nondisulfide and non-GP cross-linking reactions in heated emulsions. The GP-zein bridges between particles at the oil-water interface create strong connections in the particle layer (shell), referred to as "particle-shell locking", enhancing the thermal stability of emulsion significantly. This insight aids the future design of protein-particle-based emulsions, preserving properties like aeratability during thermal processing.
Keywords: aeratable emulsion; genipin; mechanism; thermal stability; zein.