Ochratoxin A degrading enzymes of Stenotrophomonas sp. 043-1a

Ochratoxin A is a secondary metabolite that acts as a mycotoxin and is produced by Aspergillus, Penicillium, and other fungal species. It is a threat to animal and human health due to nephrotoxic, carcinogenic, and genotoxic properties and its widespread incidence in agricultural products. To reduce this threat, biological remediation processes are of growing interest. The aerobic gram-negative bacterium Stenotrophomonassp. 043-1a, isolated from soil, was previously shown to degrade ochratoxin A into the non-toxic ochratoxin a and l-phenylalanine (Schatzmayr et al. ). However, the enzyme or enzymes catalyzing this reaction in this strain remained elusive. Here, we report the targeted purification of Stenotrophomonassp. 043-1a lysate via ammonium sulfate precipitation, size-exclusion chromatography, and hydrophobic interaction chromatography to identify the ochratoxin A degrading enzymes by subsequent peptide fragment fingerprinting. The metallo-dependent hydrolase Chr1_3858681_3267 and a member of the peptidase S9 family, Chr1_3858681_771, were shown to degrade ochratoxin A. This was, to our knowledge, the first report of an ochratoxin A degrading enzyme from the peptidase S9 family.

Automated summary

Ochratoxin A, a mycotoxin produced by certain fungi, poses a threat to animal and human health due to its nephrotoxic, carcinogenic, and genotoxic properties. Stenotrophomonas sp. 043-1a, a bacterium isolated from soil, has been previously shown to degrade ochratoxin A into non-toxic compounds. In this study, the enzymes responsible for this degradation were identified as the metallo-dependent hydrolase Chr1_3858681_3267 and a member of the peptidase S9 family, Chr1_3858681_771. This is the first report of an ochratoxin A degrading enzyme from the peptidase S9 family.