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Article Dans Une Revue Food Research International Année : 2013

Structural consequences of dry heating on alpha-lactalbumin and beta-lactoglobulin at pH 6.5

Résumé

In the present work, we investigated the structural modifications occurring during the dry heating of model whey proteins, β-lactoglobulin and α-lactalbumin. Samples were adjusted to pH 6.5, water activity aw=0.23 and dry heated at 100 °C for up to 24 h, and the structural modifications followed by gel permeation chromatography, reverse phase-HPLC, SDS PAGE and mass spectrometry (LC–MS/MS). The dry heating treatment traps a fraction of the proteins into covalently linked soluble aggregates. Moreover, a high proportion of non-aggregated α-lactalbumin (about 73%) was converted into non-native forms. The characteristic of those non-native species was the loss of one or two water molecules per α-lactalbumin molecules. Using tandem mass spectrometric peptide mapping, these chemical modifications were found to be attributed to (i) the formation of a pyroglutamic acid from the N-terminal glutamic acid and (ii) the formation of an internal cyclic imide at position Asp64. The non-native species were not favored in the case of β-lactoglobulin as they represented less than 18% of non-aggregated proteins.
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Dates et versions

hal-01209406 , version 1 (29-05-2020)

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Muhammad Gulzar, Said Bouhallab, Julien Jardin, Valérie Briard-Bion, Thomas Croguennec. Structural consequences of dry heating on alpha-lactalbumin and beta-lactoglobulin at pH 6.5. Food Research International, 2013, 51, pp.899-906. ⟨10.1016/j.foodres.2013.02.025⟩. ⟨hal-01209406⟩
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