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Effect of Maillard Reaction on IgE Binding Capacity and Conformational Structure of Tropomyosin from Short-Neck Clam (Ruditapes philippinarum)

LIN Haixin1, LIN Hong1, WANG Xiaofei2, LÜ Liangtao1, LI Zhenxing1,*   

  1. 1. Food Safety Laboratory, Ocean University of China, Qingdao 266003, China;
    2. Department of Biological and Chemical Engineering, Weihai Vocational College, Weihai 264200, China
  • Online:2016-02-15 Published:2016-02-26

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Abstract:

The aim of the present study was to assess changes in conformational structures and potential allergenicity of
tropomyosin from short-neck clams after glycation with ribose. Changes in potential allergenicity were characterized by
immunological techniques, while circular dichroism (CD) and available lysine were determined to define conformational
changes. An unfolded structure was found as glycation proceeded. Correspondingly, the amount of available lysine was
reduced by 45.5% and surface hydrophobicity was increased by 192% when the reaction time was 12 h. Indirect enzyme
linked immunosorbent assay (ELISA) and dot-blot results of glycation showed that potential allergenicity correlated well
with structural changes. Allergenicity decreased significantly after unfolding of the protein. These results showed that
conformational changes in tropomyosin induced by glycation significantly influenced the allergenicity of tropomyosin.

Key words: allergen, tropomyosin, Maillard, IgE-binding capacity, short-neck clam

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