Degradation of Four Major Mycotoxins by Eight Manganese Peroxidases in Presence of a Dicarboxylic Acid.
Identifieur interne : 000080 ( Main/Exploration ); précédent : 000079; suivant : 000081Degradation of Four Major Mycotoxins by Eight Manganese Peroxidases in Presence of a Dicarboxylic Acid.
Auteurs : Xiaolu Wang [République populaire de Chine] ; Xing Qin [République populaire de Chine] ; Zhenzhen Hao [République populaire de Chine] ; Huiying Luo [République populaire de Chine] ; Bin Yao [République populaire de Chine] ; Xiaoyun Su [République populaire de Chine]Source :
- Toxins [ 2072-6651 ] ; 2019.
Descripteurs français
- KwdFr :
- Aflatoxine B1 (métabolisme), Champignons (enzymologie), Contamination des aliments (MeSH), Détoxication de phase I (MeSH), Fumonisines (métabolisme), Malonates (pharmacologie), Mycotoxines (métabolisme), Naphtalènesulfonates (MeSH), Peroxidases (métabolisme), Trichothécènes (métabolisme), Zéaralénone (métabolisme).
- MESH :
- enzymologie : Champignons.
- métabolisme : Aflatoxine B1, Fumonisines, Mycotoxines, Peroxidases, Trichothécènes, Zéaralénone.
- pharmacologie : Malonates.
- Contamination des aliments, Détoxication de phase I, Naphtalènesulfonates.
English descriptors
- KwdEn :
- Aflatoxin B1 (metabolism), Food Contamination (MeSH), Fumonisins (metabolism), Fungi (enzymology), Malonates (pharmacology), Metabolic Detoxication, Phase I (MeSH), Mycotoxins (metabolism), Naphthalenesulfonates (MeSH), Peroxidases (metabolism), Trichothecenes (metabolism), Zearalenone (metabolism).
- MESH :
- chemical , metabolism : Aflatoxin B1, Fumonisins, Mycotoxins, Peroxidases, Trichothecenes, Zearalenone.
- enzymology : Fungi.
- chemical , pharmacology : Malonates.
- Food Contamination, Metabolic Detoxication, Phase I, Naphthalenesulfonates.
Abstract
Enzymatic treatment is an attractive method for mycotoxin detoxification, which ideally prefers the use of one or a few enzymes. However, this is challenged by the diverse structures and co-contamination of multiple mycotoxins in food and feed. Lignin-degrading fungi have been discovered to detoxify organics including mycotoxins. Manganese peroxidase (MnP) is a major enzyme responsible for lignin oxidative depolymerization in such fungi. Here, we demonstrate that eight MnPs from different lignocellulose-degrading fungi (five from Irpex lacteus, one from Phanerochaete chrysosporium, one from Ceriporiopsis subvermispora, and another from Nematoloma frowardii) could all degrade four major mycotoxins (aflatoxin B1, AFB1; zearalenone, ZEN; deoxynivalenol, DON; fumonisin B1, FB1) only in the presence of a dicarboxylic acid malonate, in which free radicals play an important role. The I. lacteus and C. subvermispora MnPs behaved similarly in mycotoxins transformation, outperforming the P. chrysosporium and N. frowardii MnPs. The large evolutionary diversity of these MnPs suggests that mycotoxin degradation tends to be a common feature shared by MnPs. MnP can, therefore, serve as a candidate enzyme for the degradation of multiple mycotoxins in food and feed if careful surveillance of the residual toxicity of degradation products is properly carried out.
DOI: 10.3390/toxins11100566
PubMed: 31569657
PubMed Central: PMC6833064
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xiaolu4444@126.com.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Qin, Xing" sort="Qin, Xing" uniqKey="Qin X" first="Xing" last="Qin">Xing Qin</name><affiliation wicri:level="1"><nlm:affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. xingqin@hust.edu.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081</wicri:regionArea><placeName><settlement 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Chine</country><wicri:regionArea>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Luo, Huiying" sort="Luo, Huiying" uniqKey="Luo H" first="Huiying" last="Luo">Huiying Luo</name><affiliation wicri:level="1"><nlm:affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. luohuiying@caas.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Yao, Bin" sort="Yao, Bin" uniqKey="Yao B" first="Bin" last="Yao">Bin Yao</name><affiliation wicri:level="1"><nlm:affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. binyao@caas.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Su, Xiaoyun" sort="Su, Xiaoyun" uniqKey="Su X" first="Xiaoyun" last="Su">Xiaoyun Su</name><affiliation wicri:level="1"><nlm:affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. suxiaoyun@caas.cn.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author></analytic><series><title level="j">Toxins</title><idno type="eISSN">2072-6651</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aflatoxin B1 (metabolism)</term><term>Food Contamination (MeSH)</term><term>Fumonisins (metabolism)</term><term>Fungi (enzymology)</term><term>Malonates (pharmacology)</term><term>Metabolic Detoxication, Phase I (MeSH)</term><term>Mycotoxins (metabolism)</term><term>Naphthalenesulfonates (MeSH)</term><term>Peroxidases (metabolism)</term><term>Trichothecenes (metabolism)</term><term>Zearalenone (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aflatoxine B1 (métabolisme)</term><term>Champignons (enzymologie)</term><term>Contamination des aliments (MeSH)</term><term>Détoxication de phase I (MeSH)</term><term>Fumonisines (métabolisme)</term><term>Malonates (pharmacologie)</term><term>Mycotoxines (métabolisme)</term><term>Naphtalènesulfonates (MeSH)</term><term>Peroxidases (métabolisme)</term><term>Trichothécènes (métabolisme)</term><term>Zéaralénone (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aflatoxin B1</term><term>Fumonisins</term><term>Mycotoxins</term><term>Peroxidases</term><term>Trichothecenes</term><term>Zearalenone</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aflatoxine B1</term><term>Fumonisines</term><term>Mycotoxines</term><term>Peroxidases</term><term>Trichothécènes</term><term>Zéaralénone</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Malonates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Malonates</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Food Contamination</term><term>Metabolic Detoxication, Phase I</term><term>Naphthalenesulfonates</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Contamination des aliments</term><term>Détoxication de phase I</term><term>Naphtalènesulfonates</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Enzymatic treatment is an attractive method for mycotoxin detoxification, which ideally prefers the use of one or a few enzymes. However, this is challenged by the diverse structures and co-contamination of multiple mycotoxins in food and feed. Lignin-degrading fungi have been discovered to detoxify organics including mycotoxins. Manganese peroxidase (MnP) is a major enzyme responsible for lignin oxidative depolymerization in such fungi. Here, we demonstrate that eight MnPs from different lignocellulose-degrading fungi (five from <i>Irpex lacteus</i>, one from <i>Phanerochaete chrysosporium</i>, one from <i>Ceriporiopsis subvermispora</i>, and another from <i>Nematoloma frowardii</i>) could all degrade four major mycotoxins (aflatoxin B<sub>1</sub>, AFB<sub>1</sub>; zearalenone, ZEN; deoxynivalenol, DON; fumonisin B<sub>1</sub>, FB<sub>1</sub>) only in the presence of a dicarboxylic acid malonate, in which free radicals play an important role. The <i>I. lacteus</i> and <i>C. subvermispora</i> MnPs behaved similarly in mycotoxins transformation, outperforming the <i>P. chrysosporium</i> and <i>N. frowardii</i> MnPs. The large evolutionary diversity of these MnPs suggests that mycotoxin degradation tends to be a common feature shared by MnPs. MnP can, therefore, serve as a candidate enzyme for the degradation of multiple mycotoxins in food and feed if careful surveillance of the residual toxicity of degradation products is properly carried out.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31569657</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>19</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2072-6651</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>10</Issue><PubDate><Year>2019</Year><Month>09</Month><Day>27</Day></PubDate></JournalIssue><Title>Toxins</Title><ISOAbbreviation>Toxins (Basel)</ISOAbbreviation></Journal><ArticleTitle>Degradation of Four Major Mycotoxins by Eight Manganese Peroxidases in Presence of a Dicarboxylic Acid.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E566</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/toxins11100566</ELocationID><Abstract><AbstractText>Enzymatic treatment is an attractive method for mycotoxin detoxification, which ideally prefers the use of one or a few enzymes. However, this is challenged by the diverse structures and co-contamination of multiple mycotoxins in food and feed. Lignin-degrading fungi have been discovered to detoxify organics including mycotoxins. Manganese peroxidase (MnP) is a major enzyme responsible for lignin oxidative depolymerization in such fungi. Here, we demonstrate that eight MnPs from different lignocellulose-degrading fungi (five from <i>Irpex lacteus</i>, one from <i>Phanerochaete chrysosporium</i>, one from <i>Ceriporiopsis subvermispora</i>, and another from <i>Nematoloma frowardii</i>) could all degrade four major mycotoxins (aflatoxin B<sub>1</sub>, AFB<sub>1</sub>; zearalenone, ZEN; deoxynivalenol, DON; fumonisin B<sub>1</sub>, FB<sub>1</sub>) only in the presence of a dicarboxylic acid malonate, in which free radicals play an important role. The <i>I. lacteus</i> and <i>C. subvermispora</i> MnPs behaved similarly in mycotoxins transformation, outperforming the <i>P. chrysosporium</i> and <i>N. frowardii</i> MnPs. The large evolutionary diversity of these MnPs suggests that mycotoxin degradation tends to be a common feature shared by MnPs. MnP can, therefore, serve as a candidate enzyme for the degradation of multiple mycotoxins in food and feed if careful surveillance of the residual toxicity of degradation products is properly carried out.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Xiaolu</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. xiaolu4444@126.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qin</LastName><ForeName>Xing</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. xingqin@hust.edu.cn.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China. xingqin@hust.edu.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hao</LastName><ForeName>Zhenzhen</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. zhenzhenhao2012@163.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Huiying</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. luohuiying@caas.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yao</LastName><ForeName>Bin</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. binyao@caas.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Su</LastName><ForeName>Xiaoyun</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China. suxiaoyun@caas.cn.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>09</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Toxins (Basel)</MedlineTA><NlmUniqueID>101530765</NlmUniqueID><ISSNLinking>2072-6651</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037341">Fumonisins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008314">Malonates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009183">Mycotoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009282">Naphthalenesulfonates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014255">Trichothecenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>3ZZM97XZ32</RegistryNumber><NameOfSubstance UI="C056933">fumonisin B1</NameOfSubstance></Chemical><Chemical><RegistryNumber>5W827M159J</RegistryNumber><NameOfSubstance UI="D015025">Zearalenone</NameOfSubstance></Chemical><Chemical><RegistryNumber>9KX7ZMG0MK</RegistryNumber><NameOfSubstance UI="C030290">malonic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>9N2N2Y55MH</RegistryNumber><NameOfSubstance UI="D016604">Aflatoxin B1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>JT37HYP23V</RegistryNumber><NameOfSubstance UI="C007262">deoxynivalenol</NameOfSubstance></Chemical><Chemical><RegistryNumber>O0HDY58362</RegistryNumber><NameOfSubstance UI="C063421">Remazol black B</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016604" MajorTopicYN="N">Aflatoxin B1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005506" MajorTopicYN="N">Food Contamination</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037341" MajorTopicYN="N">Fumonisins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008314" MajorTopicYN="N">Malonates</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050216" MajorTopicYN="N">Metabolic Detoxication, Phase I</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009183" MajorTopicYN="N">Mycotoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009282" MajorTopicYN="N">Naphthalenesulfonates</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014255" MajorTopicYN="N">Trichothecenes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015025" MajorTopicYN="N">Zearalenone</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">aflatoxin</Keyword><Keyword MajorTopicYN="Y">deoxynivalenol</Keyword><Keyword MajorTopicYN="Y">detoxification</Keyword><Keyword MajorTopicYN="Y">fumonisin</Keyword><Keyword MajorTopicYN="Y">manganese peroxidase</Keyword><Keyword MajorTopicYN="Y">mycotoxin</Keyword><Keyword 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Qin</name><name sortKey="Qin, Xing" sort="Qin, Xing" uniqKey="Qin X" first="Xing" last="Qin">Xing Qin</name><name sortKey="Su, Xiaoyun" sort="Su, Xiaoyun" uniqKey="Su X" first="Xiaoyun" last="Su">Xiaoyun Su</name><name sortKey="Yao, Bin" sort="Yao, Bin" uniqKey="Yao B" first="Bin" last="Yao">Bin Yao</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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