Autor: |
Fengwen Huang, Zhigang Liu, Xuli Wu, Ming Ying, Hua-feng Xiao, Zhangli Hu, Gang Liu, Liangliang Shen, Shen-Li Tian, Qian-Qian Zhu, Hong Xu, Kai Zhou |
Rok vydání: |
2015 |
Předmět: |
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Zdroj: |
LWT - Food Science and Technology. 60:964-969 |
ISSN: |
0023-6438 |
DOI: |
10.1016/j.lwt.2014.10.044 |
Popis: |
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. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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