Combined multispectral analysis and molecular docking to research the interaction of soybean isolate protein with different kinds of phospholipid liposomes and its effect on liposome properties.

Liposomes were modified due to suboptimal stability. Soybean lecithin liposomes (SLip), hydrogenated soybean lecithin liposomes (HLip), and egg yolk lecithin liposomes (ELip) were modified with different concentrations of soybean isolate protein (SPI) to form SLip-SPI, HLip-SPI, and ELip-SPI. The physical properties, interactions, and stability of liposomes were investigated. The vesicle size of SPI-liposomes was increased, SLip-SPI5.0, HLip-SPI2.5, and ELip-SPI5.0 had the best micromorphology and lowest surface roughness. The binding of both was dominated by hydrogen bonding and hydrophobic interactions, and SLip exhibited the strongest binding affinity. SPI modification enhanced liposome stability, denser liposome membrane structure, and effective retardation of lipid oxidation during storage. Simulation of digestion showed the release rate of proanthocyanidins from SLip-SPI (43.91 %), HLip-SPI (36.96 %), and ELip-SPI (41.44 %) were less than unmodified liposomes, effectively delayed the release of proanthocyanidins. The above findings contributed to design different types of liposome delivery systems while enhancing the application of SPI.