Effect of boiling on the structure and immunoreactivity of recombinant peanut protein Ara h 1
Ara h 1 is a key peanut allergen and its activity is significantly affected by protein intrinsic structure which is found to be regulated by heat treatment, although the molecular basis for this regulation has remained largely unknown. Here, we explored the effect of boiling on the structure and all...
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| Autores principales: | , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Taylor & Francis Group
2018
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/05322740d338467d8a1ad12fc7df0a52 |
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| Sumario: | Ara h 1 is a key peanut allergen and its activity is significantly affected by protein intrinsic structure which is found to be regulated by heat treatment, although the molecular basis for this regulation has remained largely unknown. Here, we explored the effect of boiling on the structure and allergenicity of recombinant peanut protein Ara h 1 (rAra h 1). rAra h 1 was purified from E. Coli BL21(DE3) plysS cells and structurally studied. According to the results, rAra h 1 undergoes degradation during the heating process, and the aggregation of fragments happened after 20 min of heating. An increased surface hydrophobic index and a decreased content of α-helixes were found in rAra h 1, indicating a looser protein structure of rAra h 1 caused by heat treatment. Destroyed epitopes during protein degradation and aggregation could be a mechanism of reducing the allergenic nature of rAra h 1 by heat treatment. |
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