Ultrasound Facilitate Temperature-Dependence Adsorption of Β-Lactoglobulin on Starch Nanoparticles Used for Enhancing Protein Desensitization and Modifying the Physicochemical Properties

This study aimed to probe an effective approach to reduce the allergy of ll-lactoglobulin (llLg) by formation of protein corona on starch nanoparticles (SNPs) and unveil the role of ultrasound in temperature-dependence SNPs-llLg coronas systematically through the llLg adsorption mechanism, changes in secondary structure and physicochemical properties. The adsorption was found to be a spontaneous process that negatively correlate with temperature, while, sonication increased the theoretical maximum binding number of llLg from 4600 to 7800, accompanied with higher binding affinity (Ka) of 58 x 106 M-1 and greater change in secondary structure of llLg with 22 +/- 3.1% of ll-sheet. Functionally, ultrasound facilitated the functional properties changes to llLg induced by adsorption to SNPs that inhibited llLg's immunoglobulin E (IgE) combining capacity for 87 +/- 5%, decreased surface hydrophobicity and digestibility due to the more decrease of ll-sheet, whereas, increased thermal stability and emulsifying ability. These findings promoted the application potential of llLg and SNPs in food.