Targeting deoxynivalenol for degradation by a chimeric manganese peroxidase/glutathione system

The manganese peroxidase (MnP) can degrade multiple mycotoxins including deoxynivalenol (DON) efficiently; however, the lignin components abundant in foods and feeds were discovered to interfere with DON catalysis. Herein, using MnP from Ceriporiopsis subvermispora (CsMnP) as a model, it was demonstrated that desired catalysis of DON, but not futile reactions with lignin, in the reaction systems containing feeds could be achieved by engineering MnP and supplementing with a boosting reactant. Specifically, two successive strategies (including the fusion of CsMnP to a DON-recognizing ScFv and identification of glutathione as a specific targeting enhancer) were combined to overcome the lignin competition, which together resulted into elevation of the degradation rate from 2.5% to as high as 82.7% in the feeds. The method to construct a targeting MnP and fortify it with an additional enhancer could be similarly applied to catalyze the many other mycotoxins with yet unknown responsive biocatalysts. [Display omitted] •Targeting with an antibody improved degradation of deoxynivalenol by an MnP in presence of competing lignin.•GSH could further boost deoxynivalenol degradation in a dose-dependent manner.•Oxygen and GSOO· played an important role in GSH-fortified catalysis of deoxynivalenol.