A model study on the site-specificity of (−)-epicatechin-induced reactions in β-lactoglobulin by high-resolution mass spectrometry in combination with bioinformatics
Börsig A, Konar N, Dalabasmaz S (2023)
Publication Type: Journal article
Publication year: 2023
Journal
Book Volume: 408
Article Number: 135242
DOI: 10.1016/j.foodchem.2022.135242
Abstract
Polyphenol–protein reactions in model solutions of β-lactoglobulin (β-LG) incubated with (−)-epicatechin at 37 °C and 60 °C were monitored by microLC–timsTOF Pro-MS/MS combined with bioinformatics strategies. The addition of (−)-epicatechin to the model solutions resulted in changes in tryptic peptide profiles. Covalent bond formation between (−)-epicatechin o-quinones and β-LG was identified for the residues S27, S30, K60, C66, K69, and C160, with C160 being the predominant binding site. Furthermore, the incubation of β-LG with (−)-epicatechin significantly promoted oxidation, especially for the residues M7 and M24. The reaction of monomeric (−)-epicatechin o-quinone at C160 was also identified in the milk chocolate sample. The adaptation of this study by extending the scope of the reaction products offers significant potential for comprehensive food profiling strategies.
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APA:
Börsig, A., Konar, N., & Dalabasmaz, S. (2023). A model study on the site-specificity of (−)-epicatechin-induced reactions in β-lactoglobulin by high-resolution mass spectrometry in combination with bioinformatics. Food Chemistry, 408. https://doi.org/10.1016/j.foodchem.2022.135242
MLA:
Börsig, Amelie, Nevzat Konar, and Sevim Dalabasmaz. "A model study on the site-specificity of (−)-epicatechin-induced reactions in β-lactoglobulin by high-resolution mass spectrometry in combination with bioinformatics." Food Chemistry 408 (2023).
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