Effect of heat treatment on structure and immunogenicity of recombinant peanut protein Ara h 2.01

•The immunogenicity and structure of recombinant Ara h 2.01 was investigated.•Ara h 2.01 collapses gradually from room temperature to 100 °C, and the collapse reaches saturation at around 100 °C.•Its secondary structures remain almost the same, while its immunogenicity decreases over the experimental temperature range.•These research results are helpful to the further understanding of the sensitization mechanism of peanut allergen.

Circular dichroism spectra, fluorescence spectra, synchronous fluorescence spectra, resonance light scattering spectra, ELISA experiments, along with bioinformatics method have been used to study the relationship between immunogenicity and structure of recombinant peanut protein Ara h 2.01 with increase in temperature. The experimental results show that the protein collapses gradually within the temperature range from room temperature to 100 °C, and the collapse reaches saturation at around 100 °C, while its secondary structures remain almost the same, and its immunogenicity decreases steadily over the experimental temperature range. These research results can be explained reasonably by its advanced structure and epitopes predicted by bioinformatics, and should be helpful to the further understanding of the sensitization mechanism of food allergen and the guidance of peanut food processing.