Abstract:To analyze the effects of reactive oxygen species oxidation on the structure，functional properties，and sensitization of bovine milk β-lactoglobulin（β-LG）during bovine milk processing，β-LG was studied，and the changes in the structure of β-LG before and after reactive oxygen species oxidation were analyzed using circular dichroism，surface hydrophobicity，and endogenous fluorescence spectroscopy.In addition，the changes in functional properties were determined，while the changes in sensitization were evaluated by enzyme linked immunosorbent assay（ELISA）and rat basophilic leukemia cells（RBL-2H3）.The resultsshowed that after reactive oxygen speciesoxidation，the α-helix content of β-LG was reduced；the secondary structure was more disordered；the surface hydrophobicity was elevated；the intensity of endogenous fluorescence was reduced；the foaming ability and stability were increased；the emulsion activity was reduced，but the emulsion stability was elevated.β-LG's immunoglobulin E-binding ability and the content of β-hexosidase and histamine in RBL-2H3 were reduced.It was shown that proper oxidation during processing could alter the conformational structure of bovine milk β -LG，resulting in a significant improvement of functional properties with a reduction of potential sensitization.This study provided a reference for exploring the changing patterns of functional properties and sensitization of bovine milk proteins during food processing.