大豆所含的致敏原蛋白是引起食物过敏的首因。不同加工方法可降低大豆主要致敏原蛋白β-伴大豆球蛋白致敏性。然而，这些致敏性变化的结构生物学实质尚未得到充分揭示。本项目首先用过敏原口服、抗体吸收等方法获得加工破坏的过敏原表位特异性抗体，然后通过生物信息学方法对β-伴大豆球蛋白进行结构分析，并在T7噬菌体表面展示交错的β-伴大豆球蛋白片段，筛选与加工破坏的过敏原表位特异性抗体结合的阳性克隆，接着用同样方法精确定位其亚分子结构，最后通过氨基酸置换技术确定关键氨基酸残基。该研究不仅能为食品工业提供加工方法筛选的理论依据，也可以进一步发展出快速检测加工食品脱敏效果的应用产品。

The key reason of food allergy is the allergen protein contained in the soybean. The different processing methods could reduce the allergenicity of β-conglycinins, which are the major soybean allergen protein. However, the essence of structural biology of allergenicity changes has not been fully revealed. The present study is to investigate the localization of the sub-molecular structures caused by the decrease of allergenicity to β-conglycinins. Firstly, the epitopes specific antibodies to the destruction of the process will be obtained by allergy oral and antibody absorption methods. Then, the structure of β-conglycinins will be analyzed by bioinformatics method, and T7 phages will display the overlapping β-conglycinin fractions. The positive T7 phage clones will be screened and the sub molecular structures will be positioned with the epitopes specific antibodies. Finally, the key amino acid residues will be determined by amino acid replacement technology. The research can not only provide the theoretical basis for the selection of processing methods for the food industry, but also can be applied in the development of the products which can detect the desensitization effect of processed foods rapidly.