Abstract
Bovine β-lactoglobulin (β-Lg) is recognized as a significant milk allergen in several countries. In this study, β-Lg was isolated and treated with high hydrostatic pressure (HHP) at 100, 200, 300, 400, and 500MPa. The allergenic properties of the HHP-treated β-Lg were characterized by indirect competitive enzyme-linked immunosorbent assay with anti-β-Lg rabbit antibody and the sera of patients allergic to cows' milk. The conformation of the HHP-treated β-Lg was examined with ultraviolet absorption spectroscopy, endogenous fluorescence spectroscopy, exogenous fluorescence spectroscopy, and circular dichroism spectroscopy analyses. The results indicated that IgG binding increased with treatment pressure, and IgE binding was lowest at 200MPa and highest at 400MPa. The tertiary structure of β-Lg changed significantly after HHP, whereas the primary and secondary structures remained stable. Overall, this study suggests that the conformational changes in HHP-treated β-Lg contribute to its altered allergenicity.
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