Foodborne Bacterial Protein Toxins: Structural Genomics, Stability, and Prospects for Enzymatic Detoxification in Food and Gut Environments

Foodborne bacterial toxins remain a major global health threat, causing millions of diarrheal cases annually by disrupting ion balance, inhibiting protein synthesis, and dysregulating immune responses. Key agents include AB5 enterotoxins such as cholera toxin, heat-labile toxin, and Shiga toxins; heat-stable peptides (STa/STb); staphylococcal superantigens; and pore-forming toxins from Bacillus cereus and Clostridium perfringens . Encoded on mobile genetic elements or chromosomal loci, these structurally robust toxins often resist host proteolysis, limiting natural detoxification. Despite abundant data on individual toxins, an integrated synthesis that links high-resolution structural and genetic features with practical implications for enzymatic neutralization is lacking. This review addresses this gap by compiling the structural genomics of major toxin families and mapping toxin architecture and gene context onto stability profiles and enzymatic vulnerability. We examine their genetic organization, structural stability, and susceptibility to enzymatic neutralization by microbial proteases, probiotic-mediated modulation, and engineered biocatalysts. Enzymatic detoxification of mycotoxins is discussed only as a limited translational analogy: small-molecule conversion by lactonases, oxidoreductases, or hydrolases is biochemically distinct from proteolysis of large, conformationally complex protein toxins. Thus, mycotoxin studies inform enzyme-discovery and engineering workflows but do not constitute direct evidence that these pathways can neutralize AB5 holotoxins, superantigens, or pore-forming toxins.