Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: A review.
Identifieur interne : 000186 ( Main/Exploration ); précédent : 000185; suivant : 000187Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: A review.
Auteurs : Tayssir Kadri [Canada] ; Tarek Rouissi [Canada] ; Satinder Kaur Brar [Canada] ; Maximiliano Cledon [Canada] ; Saurabhjyoti Sarma [Canada] ; Mausam Verma [Canada]Source :
- Journal of environmental sciences (China) [ 1001-0742 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Champignons.
- métabolisme : Hydrocarbures aromatiques polycycliques, Laccase, Peroxidases, Polluants du sol.
- Dépollution biologique de l'environnement, Microbiologie du sol, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Laccase, Peroxidases, Polycyclic Aromatic Hydrocarbons, Soil Pollutants.
- enzymology : Fungi.
- Biodegradation, Environmental, Oxidation-Reduction, Soil Microbiology.
Abstract
Polycyclic aromatic hydrocarbons (PAHs) are a large group of chemicals. They represent an important concern due to their widespread distribution in the environment, their resistance to biodegradation, their potential to bioaccumulate and their harmful effects. Several pilot treatments have been implemented to prevent economic consequences and deterioration of soil and water quality. As a promising option, fungal enzymes are regarded as a powerful choice for degradation of PAHs. Phanerochaete chrysosporium, Pleurotus ostreatus and Bjerkandera adusta are most commonly used for the degradation of such compounds due to their production of ligninolytic enzymes such as lignin peroxidase, manganese peroxidase and laccase. The rate of biodegradation depends on many culture conditions, such as temperature, oxygen, accessibility of nutrients and agitated or shallow culture. Moreover, the addition of biosurfactants can strongly modify the enzyme activity. The removal of PAHs is dependent on the ionization potential. The study of the kinetics is not completely comprehended, and it becomes more challenging when fungi are applied for bioremediation. Degradation studies in soil are much more complicated than liquid cultures because of the heterogeneity of soil, thus, many factors should be considered when studying soil bioremediation, such as desorption and bioavailability of PAHs. Different degradation pathways can be suggested. The peroxidases are heme-containing enzymes having common catalytic cycles. One molecule of hydrogen peroxide oxidizes the resting enzyme withdrawing two electrons. Subsequently, the peroxidase is reduced back in two steps of one electron oxidation. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds.
DOI: 10.1016/j.jes.2016.08.023
PubMed: 28115152
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: satinder.brar@ete.inrs.ca.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9</wicri:regionArea><wicri:noRegion>QC G1K 9A9</wicri:noRegion></affiliation></author><author><name sortKey="Cledon, Maximiliano" sort="Cledon, Maximiliano" uniqKey="Cledon M" first="Maximiliano" last="Cledon">Maximiliano Cledon</name><affiliation wicri:level="1"><nlm:affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9</wicri:regionArea><wicri:noRegion>QC G1K 9A9</wicri:noRegion></affiliation></author><author><name sortKey="Sarma, Saurabhjyoti" sort="Sarma, Saurabhjyoti" uniqKey="Sarma S" first="Saurabhjyoti" last="Sarma">Saurabhjyoti Sarma</name><affiliation wicri:level="1"><nlm:affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9</wicri:regionArea><wicri:noRegion>QC G1K 9A9</wicri:noRegion></affiliation></author><author><name sortKey="Verma, Mausam" sort="Verma, Mausam" uniqKey="Verma M" first="Mausam" last="Verma">Mausam Verma</name><affiliation wicri:level="1"><nlm:affiliation>CO(2) Solutions Inc., 2300, rue Jean-Perrin, Québec, QC G2C 1T9, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>CO(2) Solutions Inc., 2300, rue Jean-Perrin, Québec, QC G2C 1T9</wicri:regionArea><wicri:noRegion>QC G2C 1T9</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of environmental sciences (China)</title><idno type="ISSN">1001-0742</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biodegradation, Environmental (MeSH)</term><term>Fungi (enzymology)</term><term>Laccase (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (metabolism)</term><term>Polycyclic Aromatic Hydrocarbons (metabolism)</term><term>Soil Microbiology (MeSH)</term><term>Soil Pollutants (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Champignons (enzymologie)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Hydrocarbures aromatiques polycycliques (métabolisme)</term><term>Laccase (métabolisme)</term><term>Microbiologie du sol (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (métabolisme)</term><term>Polluants du sol (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Laccase</term><term>Peroxidases</term><term>Polycyclic Aromatic Hydrocarbons</term><term>Soil Pollutants</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>Hydrocarbures aromatiques polycycliques</term><term>Laccase</term><term>Peroxidases</term><term>Polluants du sol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Oxidation-Reduction</term><term>Soil Microbiology</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dépollution biologique de l'environnement</term><term>Microbiologie du sol</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Polycyclic aromatic hydrocarbons (PAHs) are a large group of chemicals. They represent an important concern due to their widespread distribution in the environment, their resistance to biodegradation, their potential to bioaccumulate and their harmful effects. Several pilot treatments have been implemented to prevent economic consequences and deterioration of soil and water quality. As a promising option, fungal enzymes are regarded as a powerful choice for degradation of PAHs. Phanerochaete chrysosporium, Pleurotus ostreatus and Bjerkandera adusta are most commonly used for the degradation of such compounds due to their production of ligninolytic enzymes such as lignin peroxidase, manganese peroxidase and laccase. The rate of biodegradation depends on many culture conditions, such as temperature, oxygen, accessibility of nutrients and agitated or shallow culture. Moreover, the addition of biosurfactants can strongly modify the enzyme activity. The removal of PAHs is dependent on the ionization potential. The study of the kinetics is not completely comprehended, and it becomes more challenging when fungi are applied for bioremediation. Degradation studies in soil are much more complicated than liquid cultures because of the heterogeneity of soil, thus, many factors should be considered when studying soil bioremediation, such as desorption and bioavailability of PAHs. Different degradation pathways can be suggested. The peroxidases are heme-containing enzymes having common catalytic cycles. One molecule of hydrogen peroxide oxidizes the resting enzyme withdrawing two electrons. Subsequently, the peroxidase is reduced back in two steps of one electron oxidation. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28115152</PMID><DateCompleted><Year>2017</Year><Month>02</Month><Day>09</Day></DateCompleted><DateRevised><Year>2017</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1001-0742</ISSN><JournalIssue CitedMedium="Internet"><Volume>51</Volume><PubDate><Year>2017</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Journal of environmental sciences (China)</Title><ISOAbbreviation>J Environ Sci (China)</ISOAbbreviation></Journal><ArticleTitle>Biodegradation of polycyclic aromatic hydrocarbons (PAHs) by fungal enzymes: A review.</ArticleTitle><Pagination><MedlinePgn>52-74</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1001-0742(16)30616-7</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jes.2016.08.023</ELocationID><Abstract><AbstractText>Polycyclic aromatic hydrocarbons (PAHs) are a large group of chemicals. They represent an important concern due to their widespread distribution in the environment, their resistance to biodegradation, their potential to bioaccumulate and their harmful effects. Several pilot treatments have been implemented to prevent economic consequences and deterioration of soil and water quality. As a promising option, fungal enzymes are regarded as a powerful choice for degradation of PAHs. Phanerochaete chrysosporium, Pleurotus ostreatus and Bjerkandera adusta are most commonly used for the degradation of such compounds due to their production of ligninolytic enzymes such as lignin peroxidase, manganese peroxidase and laccase. The rate of biodegradation depends on many culture conditions, such as temperature, oxygen, accessibility of nutrients and agitated or shallow culture. Moreover, the addition of biosurfactants can strongly modify the enzyme activity. The removal of PAHs is dependent on the ionization potential. The study of the kinetics is not completely comprehended, and it becomes more challenging when fungi are applied for bioremediation. Degradation studies in soil are much more complicated than liquid cultures because of the heterogeneity of soil, thus, many factors should be considered when studying soil bioremediation, such as desorption and bioavailability of PAHs. Different degradation pathways can be suggested. The peroxidases are heme-containing enzymes having common catalytic cycles. One molecule of hydrogen peroxide oxidizes the resting enzyme withdrawing two electrons. Subsequently, the peroxidase is reduced back in two steps of one electron oxidation. Laccases are copper-containing oxidases. They reduce molecular oxygen to water and oxidize phenolic compounds.</AbstractText><CopyrightInformation>Copyright © 2016. Published by Elsevier B.V.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kadri</LastName><ForeName>Tayssir</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouissi</LastName><ForeName>Tarek</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kaur Brar</LastName><ForeName>Satinder</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada. Electronic address: satinder.brar@ete.inrs.ca.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cledon</LastName><ForeName>Maximiliano</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sarma</LastName><ForeName>Saurabhjyoti</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>INRS-ETE, Université du Québec, 490 Rue de la Couronne, Québec, QC G1K 9A9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Verma</LastName><ForeName>Mausam</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>CO(2) Solutions Inc., 2300, rue Jean-Perrin, Québec, QC G2C 1T9, Canada.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>10</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Environ Sci (China)</MedlineTA><NlmUniqueID>100967627</NlmUniqueID><ISSNLinking>1001-0742</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011084">Polycyclic Aromatic Hydrocarbons</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012989">Soil Pollutants</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.10.3.2</RegistryNumber><NameOfSubstance UI="D042845">Laccase</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="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</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="D011084" MajorTopicYN="N">Polycyclic Aromatic Hydrocarbons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012988" MajorTopicYN="Y">Soil Microbiology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012989" MajorTopicYN="N">Soil Pollutants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Biodegradation</Keyword><Keyword MajorTopicYN="N">Enzymes</Keyword><Keyword MajorTopicYN="N">Fungi</Keyword><Keyword MajorTopicYN="N">Polycyclic aromatic hydrocarbons (PAHs)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>03</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>08</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>08</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>1</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>1</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>2</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28115152</ArticleId><ArticleId IdType="pii">S1001-0742(16)30616-7</ArticleId><ArticleId IdType="doi">10.1016/j.jes.2016.08.023</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="Kadri, Tayssir" sort="Kadri, Tayssir" uniqKey="Kadri T" first="Tayssir" last="Kadri">Tayssir Kadri</name></noRegion><name sortKey="Cledon, Maximiliano" sort="Cledon, Maximiliano" uniqKey="Cledon M" first="Maximiliano" last="Cledon">Maximiliano Cledon</name><name sortKey="Kaur Brar, Satinder" sort="Kaur Brar, Satinder" uniqKey="Kaur Brar S" first="Satinder" last="Kaur Brar">Satinder Kaur Brar</name><name sortKey="Rouissi, Tarek" sort="Rouissi, Tarek" uniqKey="Rouissi T" first="Tarek" last="Rouissi">Tarek Rouissi</name><name sortKey="Sarma, Saurabhjyoti" sort="Sarma, Saurabhjyoti" uniqKey="Sarma S" first="Saurabhjyoti" last="Sarma">Saurabhjyoti Sarma</name><name sortKey="Verma, Mausam" sort="Verma, Mausam" uniqKey="Verma M" first="Mausam" last="Verma">Mausam Verma</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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