In order to explore the interaction between nano-liposome (N-lip) and food protein， N-lip was prepared by the thin film dispersion method. Lactoferrin (Lf) was used as the model protein to evaluate the effects of the nanoliposome/lactoferrin (N-lip/Lf) complex formation under different protein concentrations and dripping methods on the particle size， Zeta-potential and polydispersity coefficient， and the stealth rate (Fs) was used to estimate the degree of binding of N-lip and Lf. The transmission electron microscope was used to compare the morphological changes before and after the action of lactoferrin， and the interaction between Lf and N-lip was analyzed by spectroscopy and X-ray diffraction. The results showed that: when the phospholipid mass concentration was 10.0 mg/mL， the mass ratio of phospholipid to cholesterol was 10∶1， the mass ratio of phospholipid to Tween-80 was 4∶1， and the protein mass concentration was 0.1 mg/mL， the average particle size and the zeta potential of the N-lip/Lf complex formed were (100.80±0.141) nm and (-54.9±2.276) mV， respectivlely， with favourable dispersion. Transmission electron microscope observation showed that Lf formed a light-colored wrapper around the edge of N-lip. The interaction between Lf and N-lip promoted the hydrophobicity of the environment where tryptophan and tyrosine residues in Lf were located， and the content of the alpha-helical structure of Lf increased； Lf could interact with the N-lip phospholipid bilayer membrane through hydrogen bonding， van der Waals force and hydrophobic interaction， adsorb to the surface of the phospholipid membrane and change the polar environment of the N-lip membrane. The research results can provide a theoretical basis for the interaction between liposomes and food proteins and the potential application of the former in the food industry.