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Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition

1
Food Quality & Design Group, Wageningen University & Research Centre, 6700 AA Wageningen, The Netherlands
2
Cell Biology & Immunology, Wageningen University & Research Centre, 6700 AA Wageningen, The Netherlands
3
Wageningen Food & Biobased Research, Wageningen University & Research Centre, 6700 AA Wageningen, The Netherlands
4
Laboratory of Food Chemistry, Wageningen University and Research, 6700 AA Wageningen, The Netherlands
5
FrieslandCampina, 3800 BN Amersfoort, The Netherlands
6
Erasmus University medical Centre Rotterdam, Dept. Internal Medicine, 3000 CA Rotterdam, The Netherlands
*
Author to whom correspondence should be addressed.
Nutrients 2019, 11(6), 1432; https://doi.org/10.3390/nu11061432
Received: 17 May 2019 / Revised: 12 June 2019 / Accepted: 17 June 2019 / Published: 25 June 2019
(This article belongs to the Special Issue Cow's Milk and Allergy)
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Abstract

The effect of glycation and aggregation of thermally processed β-lactoglobulin (BLG) on binding to sRAGE and specific immunoglobulin E (sIgE) from cow milk allergic (CMA) patients were investigated. BLG was heated under dry conditions (water activity < 0.7) and wet conditions (in phosphate buffer at pH 7.4) at low temperature (<73 °C) and high temperatures (>90 °C) in the presence or absence of the milk sugar lactose. Nε-(carboxymethyl)-l-lysine (CML) western blot and glycation staining were used to directly identify glycation structures on the protein fractions on SDS-PAGE. Western blot was used to specify sRAGE and sIgE binding fractions. sRAGE binding was highest under wet-heated BLG independent of the presence of the milk sugar lactose. Under wet heating, high-molecular-weight aggregates were most potent and did not require the presence of CML to generate sRAGE binding ligands. In the dry system, sRAGE binding was observed only in the presence of lactose. sIgE binding affinity showed large individual differences and revealed four binding profiles. Dependent on the individual, sIgE binding decreased or increased by wet heating independent of the presence of lactose. Dry heating required the presence of lactose to show increased binding to aggregates in most individuals. This study highlights an important role of heating condition-dependent protein aggregation and glycation in changing the immunogenicity and antigenicity of cow’s milk BLG. View Full-Text
Keywords: aggregation; allergenicity; β-lactoglobulin; CML; glycation; sRAGE; IgE binding aggregation; allergenicity; β-lactoglobulin; CML; glycation; sRAGE; IgE binding
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Zenker, H.E.; Ewaz, A.; Deng, Y.; Savelkoul, H.F.J.; van Neerven, R.J.; De Jong, N.W.; Wichers, H.J.; Hettinga, K.A.; Teodorowicz, M. Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition. Nutrients 2019, 11, 1432.

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