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Article Abstract
β-Lactoglobulin is a main allergen in cow's milk; its allergenicity is strongly impacted by processing. To understand heat-induced epitope-specific effects, the present study analyzed regiospecific conformational changes of heated native β-lactoglobulin variant A (BLG-A). Complementary fluorescence spectroscopy methods indicated two denaturation phases comprising minor sequential conformational changes (25-75 °C) and complete transitions (80-90 °C). Regioselective conformational changes of BLG-A in the native state (25 °C), sequential (70 °C) and complete transition (90 °C) were determined by quantitative liquid chromatography-mass spectrometry analysis of chemical labeling kinetics covering 14 lysine residues and the N-terminus. Conformational changes in two phases were observed for N-terminus, K (both N-terminal chain), K (β-sheet C), K (β-sheet D), K (DE loop), K (β-sheet E), K and K (FG loop). The residues K (β-sheet A1), K (β-sheet B), K, K (both β-sheet D), and K (β-sheet F) were not involved in conformational changes.
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| http://dx.doi.org/10.1016/j.foodchem.2024.140716 | DOI Listing |
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