ArticleFood chemistry: X2024
Identification of digestion-resistant peptides in various processed peanut reveals their distinct allergenicity.
Article in Food chemistry: X, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper 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
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9 authors.
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Abstract
Peanut protein is a significant food allergen that can trigger severe reactions. The allergenicity of peanut protein may be affected by the thermal processing method and matrices, and its anti-digestibility may also change accordingly. This study investigated how three heat treatment techniques affect the allergenicity and digestibility of peanut proteins and compared the differences in anti-digestive peptide segments by Mass spectrometry. Results showed that boiling and frying reduced sensitization, while roasting potentially increased it. After gastric digestion, allergenicity of Ara h 1 decreases due to breakdown of allergenic peptide segments. Hydrophobic regions of Ara h 1 where monomers interact resist degradation. Compared to boiling and frying, roasting can retain more allergenic peptides containing PGQFEDFF, YLQGFSRN, QEERGQRR, HRIFLAGDKD, and KDLAFPGSGE allergenic epitopes even after prolonged digestion. Meanwhile, digestion-resistant epitopes were affected by matrix and thermal treatments. These findings underscore the potential implications for food processing and allergy management strategies.
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