Regioselective analysis of heat-induced conformational changes of β-lactoglobulin by quantitative liquid chromatography-mass spectrometry analysis of chemical labeling kinetics.

Autor: Liu J; Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Straße 10, 91058 Erlangen, Germany. Electronic address: jiajia.liu@fau.de., Gensberger-Reigl S; Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Straße 10, 91058 Erlangen, Germany. Electronic address: sabrina.gensberger@fau.de., Zenker H; Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Straße 10, 91058 Erlangen, Germany. Electronic address: hannah.zenker@fau.de., Schichtl TM; Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Straße 10, 91058 Erlangen, Germany. Electronic address: theresa.maria.schichtl@fau.de., Utz W; Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Straße 10, 91058 Erlangen, Germany. Electronic address: wolfgang.utz@fau.de., Pischetsrieder M; Food Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Straße 10, 91058 Erlangen, Germany; FAU NeW - Research Center New Bioactive Compounds, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), Nikolaus-Fiebiger-Str. 10, 91058 Erlangen, Germany. Electronic address: monika.pischetsrieder@fau.de.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2024 Dec 01; Vol. 460 (Pt 3), pp. 140716. Date of Electronic Publication: 2024 Aug 02.
DOI: 10.1016/j.foodchem.2024.140716
Abstrakt: 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 8 (both N-terminal chain), K 60 (β-sheet C), K 75 (β-sheet D), K 77 (DE loop), K 83 (β-sheet E), K 100 and K 101 (FG loop). The residues K 14 (β-sheet A1), K 47 (β-sheet B), K 69 , K 70 (both β-sheet D), and K 91 (β-sheet F) were not involved in conformational changes.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.)
Databáze: MEDLINE
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