食品科学

• 基础研究 • 上一篇    下一篇

美拉德反应对菲律宾蛤仔原肌球蛋白结构及免疫活性的影响

蔺海鑫1,林 洪1,王晓斐2,吕良涛1,李振兴1,*   

  1. 1.中国海洋大学食品安全实验室,山东 青岛 266003;2.威海职业学院生物与化学工程系,山东 威海 264200
  • 出版日期:2016-02-15 发布日期:2016-02-26

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

摘要:

以菲律宾蛤仔原肌球蛋白为研究对象,探讨美拉德反应导致核糖糖化后对其结构及免疫原性的影响。利用酶联免疫及点印记技术分析核糖对原肌球蛋白IgE/IgG结合能力的影响。通过圆二色谱(circular dichroism,CD)、有效赖氨酸含量测定等分析蛋白二级结构及相关基团的变化。结果表明,以美拉德反应为基础的与核糖的糖化反应时间达到12 h后,产物的IgE结合能力下降76.2%,IgG结合能力下降了86.8%,α-螺旋含量下降了71.7%,蛋白表面疏水性增加了192%,有效赖氨酸含量降低了45.5%。实验表明,与核糖的糖基化反应时间达到4 h后能够有效地改变菲律宾蛤仔原肌球蛋白的结构,从而降低其免疫活性。

关键词: 过敏原, 原肌球蛋白, 美拉德, IgE结合活性, 菲律宾蛤仔

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

中图分类号: