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. Hydrogen bonds, van der Waals forces, and electrostatic interactions were responsible for WPI-LA interactions. Hydrophobic forces, van der Waals, and hydrogen bonds positively accounted for PWP-LA interactions. The antioxidant activity of LA was improved by complexation with whey proteins as identified by DPPH and ABTS. The antimicrobial efficiency of LA was partially screened by complexation with whey protein with MIC values increased by seven-fold compared to free LA but successfully recovered to its original efficiency upon isolating it from the complex. This work demonstrates the promising antioxidant and antibacterial activities of the whey protein-LA complex and provides a good candidate for developing a new class of natural functional ingredients for food systems.