Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi.
Identifieur interne : 000D76 ( Main/Exploration ); précédent : 000D75; suivant : 000D77Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi.
Auteurs : A B Orth [États-Unis] ; D J Royse ; M. TienSource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1993.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Champignons.
- métabolisme : Alcohol oxidoreductases, Lignine, Oxidoreductases, Peroxidases.
- Laccase, Spécificité d'espèce.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Alcohol Oxidoreductases, Lignin, Oxidoreductases, Peroxidases.
- enzymology : Fungi.
- chemical : Laccase, Species Specificity.
Abstract
Phanerochaete chrysosporium is rapidly becoming a model system for the study of lignin biodegradation. Numerous studies on the physiology, biochemistry, chemistry, and genetics of this system have been performed. However, P. chrysosporium is not the only fungus to have a lignin-degrading enzyme system. Many other ligninolytic species of fungi, as well as other distantly related organisms which are known to produce lignin peroxidases, are described in this paper. In this study, we demonstrated the presence of the peroxidative enzymes in nine species not previously investigated. The fungi studied produced significant manganese peroxidase activity when they were grown on an oak sawdust substrate supplemented with wheat bran, millet, and sucrose. Many of the fungi also exhibited laccase and/or glyoxal oxidase activity. Inhibitors present in the medium prevented measurement of lignin peroxidase activity. However, Western blots (immunoblots) revealed that several of the fungi produced lignin peroxidase proteins. We concluded from this work that lignin-degrading peroxidases are present in nearly all ligninolytic fungi, but may be expressed differentially in different species. Substantial variability exists in the levels and types of ligninolytic enzymes produced by different white not fungi.
DOI: 10.1128/AEM.59.12.4017-4023.1993
PubMed: 8285705
PubMed Central: PMC195861
Affiliations:
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Tien</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="ISSN">0099-2240</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (metabolism)</term><term>Fungi (enzymology)</term><term>Laccase (MeSH)</term><term>Lignin (metabolism)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidases (metabolism)</term><term>Species Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (métabolisme)</term><term>Champignons (enzymologie)</term><term>Laccase (MeSH)</term><term>Lignine (métabolisme)</term><term>Oxidoreductases (métabolisme)</term><term>Peroxidases (métabolisme)</term><term>Spécificité d'espèce (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Lignin</term><term>Oxidoreductases</term><term>Peroxidases</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>Alcohol oxidoreductases</term><term>Lignine</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Laccase</term><term>Species Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Laccase</term><term>Spécificité d'espèce</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phanerochaete chrysosporium is rapidly becoming a model system for the study of lignin biodegradation. Numerous studies on the physiology, biochemistry, chemistry, and genetics of this system have been performed. However, P. chrysosporium is not the only fungus to have a lignin-degrading enzyme system. Many other ligninolytic species of fungi, as well as other distantly related organisms which are known to produce lignin peroxidases, are described in this paper. In this study, we demonstrated the presence of the peroxidative enzymes in nine species not previously investigated. The fungi studied produced significant manganese peroxidase activity when they were grown on an oak sawdust substrate supplemented with wheat bran, millet, and sucrose. Many of the fungi also exhibited laccase and/or glyoxal oxidase activity. Inhibitors present in the medium prevented measurement of lignin peroxidase activity. However, Western blots (immunoblots) revealed that several of the fungi produced lignin peroxidase proteins. We concluded from this work that lignin-degrading peroxidases are present in nearly all ligninolytic fungi, but may be expressed differentially in different species. Substantial variability exists in the levels and types of ligninolytic enzymes produced by different white not fungi.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8285705</PMID><DateCompleted><Year>1994</Year><Month>02</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>07</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0099-2240</ISSN><JournalIssue CitedMedium="Print"><Volume>59</Volume><Issue>12</Issue><PubDate><Year>1993</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi.</ArticleTitle><Pagination><MedlinePgn>4017-23</MedlinePgn></Pagination><Abstract><AbstractText>Phanerochaete chrysosporium is rapidly becoming a model system for the study of lignin biodegradation. Numerous studies on the physiology, biochemistry, chemistry, and genetics of this system have been performed. However, P. chrysosporium is not the only fungus to have a lignin-degrading enzyme system. Many other ligninolytic species of fungi, as well as other distantly related organisms which are known to produce lignin peroxidases, are described in this paper. In this study, we demonstrated the presence of the peroxidative enzymes in nine species not previously investigated. The fungi studied produced significant manganese peroxidase activity when they were grown on an oak sawdust substrate supplemented with wheat bran, millet, and sucrose. Many of the fungi also exhibited laccase and/or glyoxal oxidase activity. Inhibitors present in the medium prevented measurement of lignin peroxidase activity. However, Western blots (immunoblots) revealed that several of the fungi produced lignin peroxidase proteins. We concluded from this work that lignin-degrading peroxidases are present in nearly all ligninolytic fungi, but may be expressed differentially in different species. Substantial variability exists in the levels and types of ligninolytic enzymes produced by different white not fungi.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Orth</LastName><ForeName>A B</ForeName><Initials>AB</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Royse</LastName><ForeName>D J</ForeName><Initials>DJ</Initials></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1-F32-ES05503</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>1-P42ES04922-01</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Environ Microbiol</MedlineTA><NlmUniqueID>7605801</NlmUniqueID><ISSNLinking>0099-2240</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C052371">glyoxal 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IdType="pubmed">16348221</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region><settlement><li>University Park (Pennsylvanie)</li></settlement><orgName><li>Université d'État de Pennsylvanie</li></orgName></list><tree><noCountry><name sortKey="Royse, D J" sort="Royse, D J" uniqKey="Royse D" first="D J" last="Royse">D J Royse</name><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Orth, A B" sort="Orth, A B" uniqKey="Orth A" first="A B" last="Orth">A B Orth</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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