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A peptide/maltose-binding protein fusion protein used to replace the traditional antigen for immunological detection of deoxynivalenol in food and feed

Xu, Yang, Yang, Hongwei, Huang, Zhibing, Li, Yanping, He, Qinghua, Tu, Zhui, Ji, Yanwei, Ren, Wenjie
Food chemistry 2018 v.268 pp. 242-248
bacteriophages, corn, deoxynivalenol, detection limit, enzyme-linked immunosorbent assay, epitopes, gold, immunoaffinity chromatography, monoclonal antibodies, nanogold, rapid methods, serum albumin, wheat
A deoxynivalenol (DON) epitope clone (D8) was obtained by phage display technology using anti-DON monoclonal antibodies as a target molecule. Subsequently, a DON antigen mimic (D8-maltose-binding protein [MBP]) was synthesized by fusing the mimic epitope peptide with MBP. An enzyme-linked immunosorbent assay (ELISA) and urchin-like gold nanoparticle immunochromatographic assay was developed based on D8-MBP for detection of DON in maize and wheat. The half-maximal inhibitory concentration, lower detection limit, and linear range of the D8-MBP ELISA were 57.98 ± 0.97, 9.83, and 11.32–286.77 ng/mL, respectively. The sensitivity of the D8-MBP ELISA was nearly 2.5 times higher than that of traditional ELISA using DON-bovine serum albumin (BSA). The detection threshold of the colloidal gold immunochromatographic assay for D8-MBP was 25 ng/mL. Thus, D8-MBP could be used to replace the traditional DON-BSA antigen for the immunological detection of DON, permitting low cost, rapid detection of DON.