ArticleNutrients2019
Differential Effects of Dry vs. Wet Heating of β-Lactoglobulin on Formation of sRAGE Binding Ligands and sIgE Epitope Recognition.
Article in Nutrients, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Bibliometric Analysis of Cow's Milk Protein Allergy Research in the Past Two Decades.Journal of inflammation research · 2026Article
- Sex-specific differences of advanced glycation end products in diabetes.Nutrition & diabetes · 2025Review
- Functional Characterization of Glycated Peptide Aggregates in Whey Protein Hydrolysates.Food science & nutrition · 2025Article
- Home-made vs industry-made: Nutrient composition and content of potentially harmful compounds of different food products.Current research in food science · 2025Article
- Diabetic Glycation of Human Serum Albumin Affects Its Immunogenicity.Biomolecules · 2024Article
- Maillard Reaction Induced Changes in Allergenicity of Food.Foods (Basel, Switzerland) · 2022Review
- Receptor Mediated Effects of Advanced Glycation End Products (AGEs) on Innate and Adaptative Immunity: Relevance for Food Allergy.Nutrients · 2022Review
- No Glycation Required: Interference of Casein in AGE Receptor Binding Tests.Foods (Basel, Switzerland) · 2021Article
- Enhanced Uptake of Processed Bovine β-Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity.Molecular nutrition & food research · 2021Article
- Cow's Milk Processing-Friend or Foe in Food Allergy?Foods (Basel, Switzerland) · 2021Review
- Article
- Binding of CML-Modified as Well as Heat-Glycated β-lactoglobulin to Receptors for AGEs Is Determined by Charge and Hydrophobicity.International journal of molecular sciences · 2020Article
- A THP-1 Cell Line-Based Exploration of Immune Responses Toward Heat-Treated BLG.Frontiers in nutrition · 2020Article
- The Two Faces of Cow's Milk and Allergy: Induction of Cow's Milk Allergy vs. Prevention of Asthma.Nutrients · 2019Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
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.
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