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

Liangtao Lv; Xin Qu; Ni Yang; Ishfaq Ahmed

doi:10.1016/j.fochx.2021.100120

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

Food Chem X. 2021 Apr 20:10:100120. doi: 10.1016/j.fochx.2021.100120. eCollection 2021 Jun 30.

Authors

Liangtao Lv^{1

2}, Xin Qu³, Ni Yang⁴, Ishfaq Ahmed¹

Affiliations

¹ College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China.
² Third Affiliated Hospital of Shenzhen University, Shenzhen 518020, China.
³ Qingdao Municipal Center for Disease Control and Prevention, 175 Shandong Road, Shibei District, Qingdao, Shandong Province 266033, China.
⁴ General Surgery Ward 1, Qingdao Eighth People's Hospital, 84 Fengshan Road, Licang District, Qingdao, Shandong Province 266100, China.

Abstract

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.

Keywords: Acrolein; Allergenicity; Oxidation; β-lactoglobulin.