Patulin Detoxification by Recombinant Manganese Peroxidase from Moniliophthora roreri Expressed by Pichia pastoris |
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| Authors: | Shuai Wang Xiaolu Wang Leena Penttinen Huiying Luo Yuhong Zhang Bo Liu Bin Yao Nina Hakulinen Wei Zhang Xiaoyun Su |
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| Affiliation: | 1.Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China; (S.W.); (Y.Z.); (B.L.);2.State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China; (X.W.); (H.L.); (B.Y.);3.Department of Chemistry, Joensuu Campus, University of Eastern Finland, FIN-80101 Joensuu, Finland; (L.P.); (N.H.) |
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| Abstract: | 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 (MrMnP) from Moniliophthora roreri can efficiently degrade patulin. The MrMnP gene was cloned into pPICZα(A) and then the recombinant plasmid was transformed into Pichia pastoris X-33. The recombinant strain produced extracellular manganese peroxidase with an activity of up to 3659.5 U/L. The manganese peroxidase MrMnP 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 Escherichia coli as a model, it was demonstrated that the deconstruction of patulin led to detoxification. Collectively, these traits make MrMnP an intriguing candidate useful in enzymatic detoxification of patulin in foods and beverages. |
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| Keywords: | patulin mycotoxin manganese peroxidase apple juice detoxification |
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