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Enhancing the Thermal Stability of Zein Particle-Stabilized Aeratable Emulsions Through Genipin-Protein Cross-Linking and Its Possible Mechanism of Action.

Zelong LiuMeiyu XuSumei ZhouJing WangZhaoxian Huang
Published in: Journal of agricultural and food chemistry (2024)
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.
Keyphrases
  • protein protein
  • amino acid
  • binding protein
  • single cell
  • body mass index
  • high throughput
  • molecular docking
  • physical activity
  • heavy metals
  • high resolution
  • molecular dynamics simulations
  • weight gain
  • data analysis