A novel method using immuno-affinity chromatography for isolating β-conglycinin from soybean proteins

Abstract A monoclonal antibody (Mab) 6G 4 against soybean β-conglycinin has been prepared using a conjugate of chicken ovalbumin and a synthetic peptide that corresponded to one of the epitope sequences of β-conglycinin as the immunogen. An ELISA method for the quantification of β-conglycinin has also been developed. In the present study, we report a novel method for the purification of β-conglycinin by Mab 6G 4 -based immuno-affinity chromatography. β-Conglycinin with a purity of 92.9% was successfully isolated from soybean proteins. Western blot assay was used to further identify its characteristics and the results demonstrated that the purified β-conglycinin maintains its biological activities. Therefore, the Mab-based immuno-affinity chromatography is an available method for purification of β-conglycinin. It also provides a new opportunity for future study on the mechanism of food allergy responses using high purity β-conglycinin as the experimental material.