Abstract
Egg yolks (EY) are widely used in food emulsions due to their high contents of amphiphilic proteins. This study investigated the different characterization and interactions among low-density lipoproteins (LDL), high-density lipoproteins (HDL) and phosvitins (Pv) using fourier transform infrared spectroscopy (FTIR), transmission electron microscopy (TEM), scanning electron microscopy (SEM). The high internal-phase Pickering emulsions (HIPPEs) prepared by those protein complexes were analyzed on the basis of droplet size, optical microstructure, confocal microscopy images, interfacial protein compositions and rheological behavior. Results showed that LDL had a smaller particle size (56.44 ± 1.27 nm) and a greater ability to reduce interfacial tension, resulting in smaller droplet sizes (7.09 ± 0.25 μm) in LDL-stabilized HIPPEs. In contrast, HDL possessed higher hydrophobicity and a greater number of free sulfhydryl groups. The droplets in HDL-stabilized HIPPEs were larger, more compact, and exhibited lower solid lipid balance values in rheological tests. The competing adsorption of HDL and LDL at the interface influenced the properties of HDL-LDL prepared emulsions. However, an appropriate amount of Pv promoted the formation of an electrical double layer between LDL and HDL, further reducing interfacial tension. LDL-HDL-Pv complex stabilized HIPPEs displayed more gel-like rheological properties and the highest stability during the storage. This study provides insights for the development of EY protein-based emulsification systems in food industry.
Published Version
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