ArticleFoods (Basel, Switzerland)2025
Investigation of Co-Assembly of Peanut Protein and Rice Protein: Effects on Protein Conformation and Immunoglobulin E Binding Capacity.
Article in Foods (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Reducing the allergenicity of food components through processing is attracting great attention in the food industry. This study investigated the structure and allergenicity of complexes formed from peanut protein (PP) and rice protein (RP) using the pH-driven method. The properties of the PP-RP complexes were investigated using morphological analysis, multi-spectroscopic characterization, IgE binding capacity analysis, and in vitro digestibility studies. Morphological analysis showed that the complexes lost their particulate structures after pH-driven treatment. Spectroscopic analysis showed that the pH-driven treatment promoted protein structural changes, making them more susceptible to degradation. There were also changes in the tertiary structures of the proteins in the complexes following the pH-driven treatment. The IgE binding capacity and digestibility studies suggested that the pH-driven treatment reduced the potential allergenicity of PP by altering its structure under gastrointestinal conditions. This study provides a promising approach for producing hypoallergenic peanut protein ingredients for use in the food industry.
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