The conformational structural change of β-lactoglobulin via acrolein treatment reduced the allergenicity

β-lactoglobulin (BLG) is a major allergen of milk. Since lipid peroxidation such as acrolein commonly exists during milk processing, it is necessary to evaluate its influence on BLG structure and potential allergenicity. The structure of acrolein-treated BLG was detected using SDS-PAGE, fluorescence, ultraviolet spectrum (UV), circular dichroism (CD) and LC-MS-MS, and the potential allergenicity was assessed by in vitro and in vivo assays. Results showed that acrolein could cause structural changes by BLG aggregation, which decreased the IgE binding capacity. Further, the release of mediators and cytokines decreased with acrolein treatment in RBL-2H3 cells. Mice showed lower allergenicity by the levels of BLG-specific antibody and the release of histamine and mMCP-1. These results explained that acrolein-induced BLG aggregation could damage the allergic epitopes and decrease the allergenicity of BLG in milk. The study will provide a new aspect to explore the natural phenomenon of allergen changes during food processing.