Gly m Bd 60 K, which is the α subunit of β-conglycinin, is a major soybean (Glycine max) allergen. We used high hydrostatic pressure (HHP), thermal techniques, and glycation to treat β-conglycinin, which can effectively reduce the antigenicity of β-conglycinin. β-conglycinin was used to immunize New Zealand rabbits, and the antiserum had a titer > 1: 1 × 10⁵ and an IC₅₀ of 2.254 μg/mL. β-conglycinin was subjected to HHP, thermal techniques, and glycation and mixed with rabbit antiserum against β-conglycinin to obtain the site-specific antiserum. The overlapping gene fragments of Gly m Bd 60 K were amplified by polymerase chain reaction (PCR), then cloned into a T7 phage vector and packaged in vitro, the recombinant T7 phages were constructed. Indirect ELISA (iELISA) was used to locate the destroyed antigenic sites and, after three rounds of segment expression and identification, the C2-1 and C2-2 fragments were identified as destroyed antigenic sites of Gly m Bd 60 K. Allergenicity analysis showed that the C2-1 and C2-2 fragments reacted with allergic patients' serum, which indicated that the destroyed sites were allergic sites.

Gly m Bd 60 K是β-伴大豆球蛋白的α亚基，是一种主要的大豆（Glycine max）过敏原。我们使用高静水压（HHP），热技术和糖基化处理β-伴大豆球蛋白，可有效降低β-伴大豆球蛋白的抗原性。β-伴大豆球蛋白用于免疫新西兰兔，抗血清的效价> 1：1×10 ⁵，IC ₅₀为2.254μg/ mL。对β-伴大豆球蛋白进行HHP，热技术和糖基化处理，并与针对β-伴大豆球蛋白的兔抗血清混合以获得位点特异性抗血清。通过聚合酶链反应（PCR）扩增Gly m Bd 60 K的重叠基因片段，然后将其克隆到T7噬菌体载体中并进行体外包装，构建了重组T7噬菌体。使用间接ELISA（iELISA）定位破坏的抗原位点，经过三轮片段表达和鉴定后，C2-1和C2-2片段被鉴定为Gly m Bd 60 K的破坏的抗原位点。 C2-1和C2-2片段与过敏患者的血清反应，表明被破坏的部位是过敏部位。