The interaction mechanism between liposome and whey protein: Effect of liposomal vesicles concentration

Abstract The interaction mechanism between liposomes (Lips) and whey protein isolates (WPI) with different mass ratios was explored in this paper. After binding with different concentration of Lips, the changes in hydrophilic and hydrophobic regions of WPI were investigated with fluorescein isothiocyanate (FITC) and pyrene fluorescence probes. The spatial structure changes of WPI were further characterized by differential scanning calorimetry, Fourier transform infrared spectroscopy, and circular dichroism. The results indicated that the structure of WPI was changed due to binding with Lips in hydrophilic and hydrophobic groups. The binding process might result in the migration, recombination, and alignment of WPI and Lip groups. Moreover, the oil‐water interfacial tension with WPI decreased from 9.20 mN/m to 3.29 mN/m upon increasing the Lip‐to‐WPI ratio. This work suggests that the physiochemical properties of Lip–WPI complexes could be manipulated by adjusting the Lip‐to‐WPI ratio. This study shed some light on the mechanism explanation of the WPI structural changes due to the interaction with Lips during food processing.