The consumption of agricultural products contaminated with mycotoxins poses a significant threat to the health of both humans and animals. Maize frequently becomes contaminated with toxic fungi while it is still growing in the field. Therefore, more proactive measures should be implemented to reduce mycotoxin levels during the storage and processing of maize after harvest. This article analyzes the prevalent mycotoxins found in maize, specifically aflatoxins, ochratoxins, trichothecenes, fumonisins, and zearalenone. The study provides a comprehensive analysis of the occurrence of mycotoxins in maize during storage, as well as fate analysis of them during processing. It summarizes the impacts of storage time, environmental conditions, storage methods, and agricultural practices on mycotoxin occurrence during storage in the post-harvest period. Furthermore, the different distribution of mycotoxins across various fractions during both dry- and wet-milling processes in the post-harvest processing period is analyzed. Additionally, the strategies to control mycotoxins in maize are also proposed during the post-harvest period. This review offers valuable insights for future research on mycotoxin contamination in maize during the post-harvest period.

Fumonisins (FBs) are mycotoxins that threaten public health and food safety worldwide. Enzymatic degradation of Fumonisin B1 (FB₁) through decarboxylation has attracted much attention, whereas application of FB₁ carboxylesterase in detoxification requires more effective expression of the recombinant carboxylesterase. In this study, the carboxylesterase FumDM from Sphingopyxis sp. ASAG22 was codon-optimized and co-expressed with five different molecular chaperones (PDI, CPR5, ERO1, HAC1, and Bip) in order to improve the expression level of FumDM in Pichia pastoris (also known as Komagataella phaffii) GS115. The co-expression of different chaperones caused varying degrees of improvement in FumDM activity for FB₁. The enzyme activities of recombinant strains over-expressing PDI and CPR5 reached the highest levels of 259.47 U/mL and 161.34 U/mL, 635% and 357% higher than the original enzyme activity, respectively. Transcriptomic analysis of the two recombinant strains in comparison with the control strain showed that the correct folding of proteins assisted by molecular chaperones played a key role in the improvement of FumDM expression and its enzyme activity. This study demonstrated that co-expression of carboxylesterase FumDM and folding chaperones was an efficient strategy and therefore might inspire new perspectives on the improvement of carboxylesterase for detoxification of FB₁.