Degradation of diuron by Phanerochaete chrysosporium: role of ligninolytic enzymes and cytochrome P450.
Identifieur interne : 000333 ( Main/Corpus ); précédent : 000332; suivant : 000334Degradation of diuron by Phanerochaete chrysosporium: role of ligninolytic enzymes and cytochrome P450.
Auteurs : Jaqueline Da Silva Coelho-Moreira ; Adelar Bracht ; Aline Cristine Da Silva De Souza ; Roselene Ferreira Oliveira ; Anacharis Babeto De Sá-Nakanishi ; Cristina Giatti Marques De Souza ; Rosane Marina PeraltaSource :
- BioMed research international [ 2314-6141 ] ; 2013.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cytochrome P-450 Enzyme System, Diuron, Lignin, Peroxidases.
- enzymology : Phanerochaete.
- metabolism : Phanerochaete.
- Biodegradation, Environmental, Humans, Oxidation-Reduction.
Abstract
The white-rot fungus Phanerochaete chrysosporium was investigated for its capacity to degrade the herbicide diuron in liquid stationary cultures. The presence of diuron increased the production of lignin peroxidase in relation to control cultures but only barely affected the production of manganese peroxidase. The herbicide at the concentration of 7 μ g/mL did not cause any reduction in the biomass production and it was almost completely removed after 10 days. Concomitantly with the removal of diuron, two metabolites, DCPMU [1-(3,4-dichlorophenyl)-3-methylurea] and DCPU [(3,4-dichlorophenyl)urea], were detected in the culture medium at the concentrations of 0.74 μ g/mL and 0.06 μ g/mL, respectively. Crude extracellular ligninolytic enzymes were not efficient in the in vitro degradation of diuron. In addition, 1-aminobenzotriazole (ABT), a cytochrome P450 inhibitor, significantly inhibited both diuron degradation and metabolites production. Significant reduction in the toxicity evaluated by the Lactuca sativa L. bioassay was observed in the cultures after 10 days of cultivation. In conclusion, P. chrysosporium can efficiently metabolize diuron without the accumulation of toxic products.
DOI: 10.1155/2013/251354
PubMed: 24490150
PubMed Central: PMC3892757
Links to Exploration step
pubmed:24490150Le document en format XML
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Souza">Aline Cristine Da Silva De Souza</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Oliveira, Roselene Ferreira" sort="Oliveira, Roselene Ferreira" uniqKey="Oliveira R" first="Roselene Ferreira" last="Oliveira">Roselene Ferreira Oliveira</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Sa Nakanishi, Anacharis Babeto" sort="De Sa Nakanishi, Anacharis Babeto" uniqKey="De Sa Nakanishi A" first="Anacharis Babeto" last="De Sá-Nakanishi">Anacharis Babeto De Sá-Nakanishi</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Souza, Cristina Giatti Marques" sort="De Souza, Cristina 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wicri:corpus="PubMed">000333</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Degradation of diuron by Phanerochaete chrysosporium: role of ligninolytic enzymes and cytochrome P450.</title><author><name sortKey="Coelho Moreira, Jaqueline Da Silva" sort="Coelho Moreira, Jaqueline Da Silva" uniqKey="Coelho Moreira J" first="Jaqueline Da Silva" last="Coelho-Moreira">Jaqueline Da Silva Coelho-Moreira</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Bracht, Adelar" sort="Bracht, Adelar" uniqKey="Bracht A" first="Adelar" last="Bracht">Adelar Bracht</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Souza, Aline Cristine Da Silva" sort="De Souza, Aline Cristine Da Silva" uniqKey="De Souza A" first="Aline Cristine Da Silva" last="De Souza">Aline Cristine Da Silva De Souza</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Oliveira, Roselene Ferreira" sort="Oliveira, Roselene Ferreira" uniqKey="Oliveira R" first="Roselene Ferreira" last="Oliveira">Roselene Ferreira Oliveira</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Sa Nakanishi, Anacharis Babeto" sort="De Sa Nakanishi, Anacharis Babeto" uniqKey="De Sa Nakanishi A" first="Anacharis Babeto" last="De Sá-Nakanishi">Anacharis Babeto De Sá-Nakanishi</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="De Souza, Cristina Giatti Marques" sort="De Souza, Cristina Giatti Marques" uniqKey="De Souza C" first="Cristina Giatti Marques" last="De Souza">Cristina Giatti Marques De Souza</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author><author><name sortKey="Peralta, Rosane Marina" sort="Peralta, Rosane Marina" uniqKey="Peralta R" first="Rosane Marina" last="Peralta">Rosane Marina Peralta</name><affiliation><nlm:affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</nlm:affiliation></affiliation></author></analytic><series><title level="j">BioMed research international</title><idno type="eISSN">2314-6141</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biodegradation, Environmental (MeSH)</term><term>Cytochrome P-450 Enzyme System (metabolism)</term><term>Diuron (metabolism)</term><term>Humans (MeSH)</term><term>Lignin (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term><term>Diuron</term><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Humans</term><term>Oxidation-Reduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The white-rot fungus Phanerochaete chrysosporium was investigated for its capacity to degrade the herbicide diuron in liquid stationary cultures. The presence of diuron increased the production of lignin peroxidase in relation to control cultures but only barely affected the production of manganese peroxidase. The herbicide at the concentration of 7 μ g/mL did not cause any reduction in the biomass production and it was almost completely removed after 10 days. Concomitantly with the removal of diuron, two metabolites, DCPMU [1-(3,4-dichlorophenyl)-3-methylurea] and DCPU [(3,4-dichlorophenyl)urea], were detected in the culture medium at the concentrations of 0.74 μ g/mL and 0.06 μ g/mL, respectively. Crude extracellular ligninolytic enzymes were not efficient in the in vitro degradation of diuron. In addition, 1-aminobenzotriazole (ABT), a cytochrome P450 inhibitor, significantly inhibited both diuron degradation and metabolites production. Significant reduction in the toxicity evaluated by the Lactuca sativa L. bioassay was observed in the cultures after 10 days of cultivation. In conclusion, P. chrysosporium can efficiently metabolize diuron without the accumulation of toxic products.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24490150</PMID><DateCompleted><Year>2014</Year><Month>08</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2314-6141</ISSN><JournalIssue CitedMedium="Internet"><Volume>2013</Volume><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>BioMed research international</Title><ISOAbbreviation>Biomed Res Int</ISOAbbreviation></Journal><ArticleTitle>Degradation of diuron by Phanerochaete chrysosporium: role of ligninolytic enzymes and cytochrome P450.</ArticleTitle><Pagination><MedlinePgn>251354</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1155/2013/251354</ELocationID><Abstract><AbstractText>The white-rot fungus Phanerochaete chrysosporium was investigated for its capacity to degrade the herbicide diuron in liquid stationary cultures. The presence of diuron increased the production of lignin peroxidase in relation to control cultures but only barely affected the production of manganese peroxidase. The herbicide at the concentration of 7 μ g/mL did not cause any reduction in the biomass production and it was almost completely removed after 10 days. Concomitantly with the removal of diuron, two metabolites, DCPMU [1-(3,4-dichlorophenyl)-3-methylurea] and DCPU [(3,4-dichlorophenyl)urea], were detected in the culture medium at the concentrations of 0.74 μ g/mL and 0.06 μ g/mL, respectively. Crude extracellular ligninolytic enzymes were not efficient in the in vitro degradation of diuron. In addition, 1-aminobenzotriazole (ABT), a cytochrome P450 inhibitor, significantly inhibited both diuron degradation and metabolites production. Significant reduction in the toxicity evaluated by the Lactuca sativa L. bioassay was observed in the cultures after 10 days of cultivation. In conclusion, P. chrysosporium can efficiently metabolize diuron without the accumulation of toxic products.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Coelho-Moreira</LastName><ForeName>Jaqueline da Silva</ForeName><Initials>Jda S</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bracht</LastName><ForeName>Adelar</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Souza</LastName><ForeName>Aline Cristine da Silva</ForeName><Initials>AC</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oliveira</LastName><ForeName>Roselene Ferreira</ForeName><Initials>RF</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Sá-Nakanishi</LastName><ForeName>Anacharis Babeto</ForeName><Initials>AB</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Souza</LastName><ForeName>Cristina Giatti Marques</ForeName><Initials>CG</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peralta</LastName><ForeName>Rosane Marina</ForeName><Initials>RM</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, State University of Maringa, 87020-900 Maringá, PR, Brazil.</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>2013</Year><Month>12</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biomed Res Int</MedlineTA><NlmUniqueID>101600173</NlmUniqueID></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-51-2</RegistryNumber><NameOfSubstance UI="D003577">Cytochrome P-450 Enzyme System</NameOfSubstance></Chemical><Chemical><RegistryNumber>9I3SDS92WY</RegistryNumber><NameOfSubstance UI="D004237">Diuron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="Y">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003577" MajorTopicYN="N">Cytochrome P-450 Enzyme System</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004237" MajorTopicYN="N">Diuron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>10</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>11</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>11</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>2</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>2</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>8</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24490150</ArticleId><ArticleId IdType="doi">10.1155/2013/251354</ArticleId><ArticleId IdType="pmc">PMC3892757</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Chemosphere. 2009 Oct;77(5):687-92</Citation><ArticleIdList><ArticleId IdType="pubmed">19695672</ArticleId></ArticleIdList></Reference><Reference><Citation>Environ 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