Synergistic effect of microfluidization and transglutaminase cross-linking on the structural and oil–water interface functional properties of whey protein concentrate for improving the thermal stability of nanoemulsions

Generally, whey protein concentrate (WPC) undergoes high-temperature denaturation and aggregation, which reduces its emulsifying properties and is not conducive to as an emulsifier to maintain the thermal stability of emulsions. In this study, dynamic high-pressure microfluidization technology (DHPM) combined with TGase (TG) cross-linking was applied to prepare DHPM-TG-WPC, and the thermal stabilization mechanism of nanoemulsions prepared with DHPM-TG-WPC was explored. Results showed DHPM treatment could promote the formation of TG-crosslinked WPC polymers. Compared to WPC, the free sulfhydryl and free amino group content of DHPM-TG-WPC was significantly decreased (P < 0.05), the surface hydrophobicity and interfacial tension of DHPM-TG-WPC were increased by 45.23 % and 62.34 %, respectively. And its emulsifying stability index and interface protein adsorption was significantly enhanced (P < 0.05). Furthermore, compared to WPC, DHPM-WPC and TG-WPC, DHPM-TG-WPC-stabilized nanoemulsions showed the best 15 days of storage stability after thermal sterilization. This study provides a theoretical basis for the application of modified-WPC emulsion.