[Studies on thermal denaturation of peanut allergen Ara h1 and its interaction with reducing sugars]

Guang Pu Xue Yu Guang Pu Fen Xi. 2013 Aug;33(8):2128-31.
[Article in Chinese]

Abstract

The thermal denaturation of peanut allergen Ara h1, its interaction with reducing sugars and the corresponding changes in allergenicity were investigated by circular dichroism (CD), fluorescence and ELISA method comprehensively. The experimental results indicate that the secondary structure of Ara h1 changes significantly along with decreasing alpha-helical structure and its allergenicity with the temperature higher than 85 degrees C, and that both xylose and fructose can stabilize Ara h1 protein structure through interacting with Ara h1 protein and decrease its allergenicity obviously. This study should be helpful to the further understanding of sensitization mechanism of food allergy and be useful for the guidance on reasonable manufacturing of peanut foods.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Plant / chemistry*
  • Arachis / chemistry*
  • Carbohydrates / chemistry*
  • Circular Dichroism
  • Glycoproteins / chemistry*
  • Hot Temperature
  • Membrane Proteins
  • Plant Proteins / chemistry*
  • Protein Denaturation*
  • Spectrometry, Fluorescence*

Substances

  • Antigens, Plant
  • Ara h 1 protein, Arachis hypogaea
  • Carbohydrates
  • Glycoproteins
  • Membrane Proteins
  • Plant Proteins