Abstract
The gene(s) encoding enzyme(s) involved in the initial reaction during degradation of zearalenone (ZEA) was characterized from the zearalenone utilizer Pseudomonas putida strain ZEA-1, where ZEA was transformed into product with less or no toxicity. A 5.5 kilobase-pair (kbp) Pst1-Kpn1 fragment containing gene(s) encoding for zearalenone degradation was cloned. The cloned gene(s) was actively expressed in Escherichia coli. ZEA degradation by recombinant E. coli was relatively rapid and effective, leaving no detectable ZEA after 24h. In further experiments, cell-free extract of E. coli has been used in the same way, both to confirm these observations and the enzymatic nature of the degradation activity.