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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.