Binding of Licochalcone A to Whey Protein Enhancing Its Antioxidant Activity and Maintaining Its Antibacterial Activity.

Incorporating LA into whey protein by forming whey protein isolate-LA (WPI-LA) and polymerized whey protein-LA (PWP-LA) complexes is a good way to maintain its bioactivity and improve its functional performance within food matrices. Herein, we found that WPI and PWP were able to interact with LA as suggested by multi-spectroscopy, molecular docking, and molecular dynamics simulations. The interaction between whey protein and LA was a spontaneous non-covalent binding process, while PWP had a higher affinity for LA than WPI, resulting from its more negatively binding free energy with LA.

Influence of ultrasound and enzymatic cross-linking on freeze-thaw stability and release properties of whey protein isolate hydrogel.

This study investigated the effect of ultrasound and enzymatic cross-linking on the freeze-thaw (FT) stability and release properties of whey protein isolate hydrogels. We evaluated the FT stability by the changes in the microstructure, riboflavin retention, syneresis, water holding capacity (WHC), and texture of gels subjected to 3 FT cycles. High-intensity ultrasound (HUS) and transglutaminase (TGase)-mediated cross-linking improved the FT stability of whey protein isolate hydrogels loaded with riboflavin (WPISAR), as demonstrated by a more uniform and denser porous structure, significantly higher riboflavin retention, WHC, and textural properties, and lower syneresis after 3 FT cycles than those of untreated hydrogels.

Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking.

This study investigated the effects of high-intensity ultrasound (HUS) and transglutaminase pretreatment on the gelation behavior of whey protein soluble aggregate (WPISA) emulsions. HUS pretreatment and TGase-mediated cross-linking delayed the onset of gelation but significantly increased ( < 0.05) the gel firmness (G') both after gel formation at 25 °C and during storage at 4 °C.