| Summary: | The fungal secondary metabolite patulin is a mycotoxin widespread in foods and beverages which poses a serious threat to human health. However, no enzyme was known to be able to degrade this mycotoxin. For the first time, we discovered that a manganese peroxidase (<i>Mr</i>MnP) from <i>Moniliophthora roreri</i> can efficiently degrade patulin. The <i>Mr</i>MnP gene was cloned into pPICZα(A) and then the recombinant plasmid was transformed into <i>Pichia pastoris</i> X-33. The recombinant strain produced extracellular manganese peroxidase with an activity of up to 3659.5 U/L. The manganese peroxidase <i>Mr</i>MnP was able to rapidly degrade patulin, with hydroascladiol appearing as a main degradation product. Five mg/L of pure patulin were completely degraded within 5 h. Moreover, up to 95% of the toxin was eliminated in a simulated patulin-contaminated apple juice after 24 h. Using <i>Escherichia coli</i> as a model, it was demonstrated that the deconstruction of patulin led to detoxification. Collectively, these traits make <i>Mr</i>MnP an intriguing candidate useful in enzymatic detoxification of patulin in foods and beverages.
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