ArticleFoods (Basel, Switzerland)2024
Heat Treatment of Hazelnut Allergens Monitored by Polyclonal Sera and Epitope Fingerprinting.
Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Multiscale Structural Remodeling of Oleosins by Thermal Processing: Mechanisms and Implications for Allergenicity Modulation in Oilseed Crops.Comprehensive reviews in food science and food safety · 2026Review
- [Vegan beware! Allergenic potential of legumes].Dermatologie (Heidelberg, Germany) · 2025Review
- Ultrasound and Heat Treatment and Its Potential to Reduce Fennel Allergenicity.Foods (Basel, Switzerland) · 2025Article
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Authors and funding
9 authors.
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Abstract
Hazelnuts are frequently involved in IgE-mediated reactions and are the main cause of nut allergies in Europe. Most food products are processed before human consumption. Food processing can modify the structure, properties, and function of proteins, and as a result, the IgE-binding capacity of allergens can be affected. In this study, we aimed to investigate epitope changes caused by the roasting of hazelnuts using epitope fingerprinting. Rabbit sera were raised against hazelnut proteins, and their epitopes were characterized. Immunoassays using specific polyclonal antibodies from rabbits targeting the main allergens in hazelnuts revealed marked reductions in the levels of Cor a 1 (PR-10), Cor a 11 (7S globulin), and Cor a 14 (2S albumin). However, rabbit antibodies can recognize different epitopes. Using antibodies that are different and characterized could help establish reliable methods for estimating the effects of treatments on the allergenicity of foods. In this work, we provide the first practical application that could lead to sets of peptide epitopes to compare and standardize immune diagnostics, even for complex protein preparations.
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