Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of beta-Lactoglobulin

Abstract : This study describes the effect of copper on the heat-denaturation/aggregation of beta-Lactoglobulin AB at neutral pH. The kinetics of disappearance of native beta-Lactoglobulin under different ionic strength and Cu(2+)/beta-Lactoglobulin molar ratio conditions were followed and the type of interactions (covalent or non-covalent) shared between non-native structures during the heating process were examined. On heating, the rate of disappearance of native beta-Lactoglobulin was accelerated by increasing the Cu(2+)/beta-Lactoglobulin molar ratio. Copper induces oxidation of the free sulfhydryl group of beta-Lactoglobulin resulting mainly in the formation of covalent dimers, which were further associated into large non-covalent aggregates under high ionic strength conditions. Characterisation of the beta-Lactoglobulin dimers reveals the existence of three different molecular species arising randomly (dimers A-A, A-B and B-B), in which tertiary structure was completely lost. The quantity of added copper constitutes a powerful way to control the heat-denaturation/aggregation process of beta-Lactoglobulin in particular regarding the relative proportion of covalent and non-covalent interactions into formed aggregates.
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Article dans une revue
Food Chemistry, Elsevier, 2009, 116 (4), pp.884-891. 〈10.1016/j.foodchem.2009.03.043〉
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Soumis le : vendredi 7 septembre 2012 - 16:04:09
Dernière modification le : mercredi 21 mars 2018 - 16:08:07

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M. Gulzar, Thomas Croguennec, J. Jardin, M. Piot, S. Bouhallab. Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of beta-Lactoglobulin. Food Chemistry, Elsevier, 2009, 116 (4), pp.884-891. 〈10.1016/j.foodchem.2009.03.043〉. 〈hal-00729989〉

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