Characterization of the covalent binding of allyl isothiocyanate to beta-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry

Keppler, Julia Katharina, Koudelka, Tomas, Palani, Kalpana, Stuhldreier, Mayra Christina, Temps, Friedrich, Tholey, Andreas and Schwarz, Karin (2014) Characterization of the covalent binding of allyl isothiocyanate to beta-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry Journal of Biomolecular Structure & Dynamics, 32 (7). pp. 1103-1117.

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Abstract

Reversible binding of small compounds through hydrophobic interactions or hydrogen bonding to food proteins (e.g. milk proteins) is a thoroughly researched topic. In contrast, covalent interactions are not well characterized. Here, we report a rare form of positive-cooperativity-linear binding of allyl isothiocyanate with beta-lactoglobulin, resulting in the cleavage of a disulfide bond of the protein. We compared three methods (i.e. fluorescence quenching, equilibrium dialysis, and headspace-water equilibrium) to characterize the binding kinetics and investigated the molecular binding by mass spectrometry. The methodologies used were found to be comparable and reproducible in the presence of high and low ligand concentrations for fluorescence quenching and equilibrium-based methods respectively.

Document Type: Article
Additional Information: Times Cited: 2 Tholey, Andreas /B-3407-2010 0 2
Research affiliation: Kiel University
Kiel University > Kiel Marine Science
OceanRep > The Future Ocean - Cluster of Excellence
Refereed: Yes
ISSN: 0739-1102
Projects: Future Ocean
Date Deposited: 30 Mar 2015 12:27
Last Modified: 02 Feb 2018 09:32
URI: http://eprints.uni-kiel.de/id/eprint/27742

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