Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i>
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 <...
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2022-06-01
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author | Shuai Wang Xiaolu Wang Leena Penttinen Huiying Luo Yuhong Zhang Bo Liu Bin Yao Nina Hakulinen Wei Zhang Xiaoyun Su |
author_facet | Shuai Wang Xiaolu Wang Leena Penttinen Huiying Luo Yuhong Zhang Bo Liu Bin Yao Nina Hakulinen Wei Zhang Xiaoyun Su |
author_sort | Shuai Wang |
collection | DOAJ |
description | 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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spelling | doaj.art-215318fd34744813b0fa573e0d77d6e72023-12-03T12:20:57ZengMDPI AGToxins2072-66512022-06-0114744010.3390/toxins14070440Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i>Shuai Wang0Xiaolu Wang1Leena Penttinen2Huiying Luo3Yuhong Zhang4Bo Liu5Bin Yao6Nina Hakulinen7Wei Zhang8Xiaoyun Su9Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaDepartment of Chemistry, Joensuu Campus, University of Eastern Finland, FIN-80101 Joensuu, FinlandState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, ChinaBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaDepartment of Chemistry, Joensuu Campus, University of Eastern Finland, FIN-80101 Joensuu, FinlandBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, ChinaState Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, ChinaThe 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.https://www.mdpi.com/2072-6651/14/7/440patulinmycotoxinmanganese peroxidaseapple juicedetoxification |
spellingShingle | Shuai Wang Xiaolu Wang Leena Penttinen Huiying Luo Yuhong Zhang Bo Liu Bin Yao Nina Hakulinen Wei Zhang Xiaoyun Su Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i> Toxins patulin mycotoxin manganese peroxidase apple juice detoxification |
title | Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i> |
title_full | Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i> |
title_fullStr | Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i> |
title_full_unstemmed | Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i> |
title_short | Patulin Detoxification by Recombinant Manganese Peroxidase from <i>Moniliophthora roreri</i> Expressed by <i>Pichia pastoris</i> |
title_sort | patulin detoxification by recombinant manganese peroxidase from i moniliophthora roreri i expressed by i pichia pastoris i |
topic | patulin mycotoxin manganese peroxidase apple juice detoxification |
url | https://www.mdpi.com/2072-6651/14/7/440 |
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