Ultrasound facilitate temperature-dependence adsorption of β-lactoglobulin on starch nanoparticles used for enhancing protein desensitization and modifying the physicochemical properties

Abstract

This study aimed to probe an effective approach to reduce the allergy of β-lactoglobulin (βLg) by formation of protein corona on starch nanoparticles (SNPs) and unveil the role of ultrasound in temperature-dependence SNPs-βLg coronas systematically through the βLg 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 βLg from 4600 to 7800, accompanied with higher binding affinity (Ka) of 58 × 106 M−1 and greater change in secondary structure of βLg with 22 ± 3.1% of β-sheet. Functionally, ultrasound facilitated the functional properties changes to βLg induced by adsorption to SNPs that inhibited βLg's immunoglobulin E (IgE) combining capacity for 87 ± 5%, decreased surface hydrophobicity and digestibility due to the more decrease of β-sheet, whereas, increased thermal stability and emulsifying ability. These findings promoted the application potential of βLg and SNPs in food.