Lignin-modifying enzymes of the white rot basidiomycete Ganoderma lucidum.
Identifieur interne : 004878 ( Main/Exploration ); précédent : 004877; suivant : 004879Lignin-modifying enzymes of the white rot basidiomycete Ganoderma lucidum.
Auteurs : T M D'Souza [États-Unis] ; C S Merritt ; C A ReddySource :
- Applied and environmental microbiology [ 0099-2240 ] ; 1999.
Descripteurs français
- KwdFr :
- Acide gallique (analogues et dérivés), Acide gallique (pharmacologie), Arbres (microbiologie), Basidiomycota (croissance et développement), Basidiomycota (effets des médicaments et des substances chimiques), Basidiomycota (enzymologie), Cinétique (MeSH), Laccase (MeSH), Lignine (métabolisme), Oxidoreductases (biosynthèse), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Peroxidases (biosynthèse), Peroxidases (métabolisme), Spécificité d'espèce (MeSH).
- MESH :
- analogues et dérivés : Acide gallique.
- biosynthèse : Oxidoreductases, Peroxidases.
- croissance et développement : Basidiomycota.
- effets des médicaments et des substances chimiques : Basidiomycota.
- enzymologie : Basidiomycota.
- génétique : Oxidoreductases.
- microbiologie : Arbres.
- métabolisme : Lignine, Oxidoreductases, Peroxidases.
- pharmacologie : Acide gallique.
- Cinétique, Laccase, Spécificité d'espèce.
English descriptors
- KwdEn :
- Basidiomycota (drug effects), Basidiomycota (enzymology), Basidiomycota (growth & development), Gallic Acid (analogs & derivatives), Gallic Acid (pharmacology), Kinetics (MeSH), Laccase (MeSH), Lignin (metabolism), Oxidoreductases (biosynthesis), Oxidoreductases (genetics), Oxidoreductases (metabolism), Peroxidases (biosynthesis), Peroxidases (metabolism), Species Specificity (MeSH), Trees (microbiology).
- MESH :
- chemical , analogs & derivatives : Gallic Acid.
- chemical , biosynthesis : Oxidoreductases, Peroxidases.
- drug effects : Basidiomycota.
- enzymology : Basidiomycota.
- chemical , genetics : Oxidoreductases.
- growth & development : Basidiomycota.
- chemical , metabolism : Lignin, Oxidoreductases, Peroxidases.
- microbiology : Trees.
- chemical , pharmacology : Gallic Acid.
- Kinetics, Laccase, Species Specificity.
Abstract
Ganoderma lucidum, a white rot basidiomycete widely distributed worldwide, was studied for the production of the lignin-modifying enzymes laccase, manganese-dependent peroxidase (MnP), and lignin peroxidase (LiP). Laccase levels observed in high-nitrogen (HN; 24 mM N) shaken cultures were much greater than those seen in low-nitrogen (2.4 mM N), malt extract, or wood-grown cultures and those reported for most other white rot fungi to date. Laccase production was readily seen in cultures grown with pine or poplar (100-mesh-size ground wood) as the sole carbon and energy source. Cultures containing both pine and poplar showed 5- to 10-fold-higher levels of laccase than cultures containing pine or poplar alone. Since syringyl units are structural components important in poplar lignin and other hardwoods but much less so in pine lignin and other softwoods, pine cultures were supplemented with syringic acid, and this resulted in laccase levels comparable to those seen in pine-plus-poplar cultures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of concentrated extracellular culture fluid from HN cultures showed two laccase activity bands (M(r) of 40,000 and 66, 000), whereas isoelectric focusing revealed five major laccase activity bands with estimated pIs of 3.0, 4.25, 4.5, 4.8, and 5.1. Low levels of MnP activity ( approximately 100 U/liter) were detected in poplar-grown cultures but not in cultures grown with pine, with pine plus syringic acid, or in HN medium. No LiP activity was seen in any of the media tested; however, probing the genomic DNA with the LiP cDNA (CLG4) from the white rot fungus Phanerochaete chrysosporium showed distinct hybridization bands suggesting the presence of lip-like sequences in G. lucidum.
DOI: 10.1128/AEM.65.12.5307-5313.1999
PubMed: 10583981
PubMed Central: PMC91721
Affiliations:
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basidiomycete widely distributed worldwide, was studied for the production of the lignin-modifying enzymes laccase, manganese-dependent peroxidase (MnP), and lignin peroxidase (LiP). Laccase levels observed in high-nitrogen (HN; 24 mM N) shaken cultures were much greater than those seen in low-nitrogen (2.4 mM N), malt extract, or wood-grown cultures and those reported for most other white rot fungi to date. Laccase production was readily seen in cultures grown with pine or poplar (100-mesh-size ground wood) as the sole carbon and energy source. Cultures containing both pine and poplar showed 5- to 10-fold-higher levels of laccase than cultures containing pine or poplar alone. Since syringyl units are structural components important in poplar lignin and other hardwoods but much less so in pine lignin and other softwoods, pine cultures were supplemented with syringic acid, and this resulted in laccase levels comparable to those seen in pine-plus-poplar cultures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of concentrated extracellular culture fluid from HN cultures showed two laccase activity bands (M(r) of 40,000 and 66, 000), whereas isoelectric focusing revealed five major laccase activity bands with estimated pIs of 3.0, 4.25, 4.5, 4.8, and 5.1. Low levels of MnP activity ( approximately 100 U/liter) were detected in poplar-grown cultures but not in cultures grown with pine, with pine plus syringic acid, or in HN medium. No LiP activity was seen in any of the media tested; however, probing the genomic DNA with the LiP cDNA (CLG4) from the white rot fungus Phanerochaete chrysosporium showed distinct hybridization bands suggesting the presence of lip-like sequences in G. lucidum.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10583981</PMID><DateCompleted><Year>2000</Year><Month>01</Month><Day>27</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>65</Volume><Issue>12</Issue><PubDate><Year>1999</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Lignin-modifying enzymes of the white rot basidiomycete Ganoderma lucidum.</ArticleTitle><Pagination><MedlinePgn>5307-13</MedlinePgn></Pagination><Abstract><AbstractText>Ganoderma lucidum, a white rot basidiomycete widely distributed worldwide, was studied for the production of the lignin-modifying enzymes laccase, manganese-dependent peroxidase (MnP), and lignin peroxidase (LiP). Laccase levels observed in high-nitrogen (HN; 24 mM N) shaken cultures were much greater than those seen in low-nitrogen (2.4 mM N), malt extract, or wood-grown cultures and those reported for most other white rot fungi to date. Laccase production was readily seen in cultures grown with pine or poplar (100-mesh-size ground wood) as the sole carbon and energy source. Cultures containing both pine and poplar showed 5- to 10-fold-higher levels of laccase than cultures containing pine or poplar alone. Since syringyl units are structural components important in poplar lignin and other hardwoods but much less so in pine lignin and other softwoods, pine cultures were supplemented with syringic acid, and this resulted in laccase levels comparable to those seen in pine-plus-poplar cultures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of concentrated extracellular culture fluid from HN cultures showed two laccase activity bands (M(r) of 40,000 and 66, 000), whereas isoelectric focusing revealed five major laccase activity bands with estimated pIs of 3.0, 4.25, 4.5, 4.8, and 5.1. Low levels of MnP activity ( approximately 100 U/liter) were detected in poplar-grown cultures but not in cultures grown with pine, with pine plus syringic acid, or in HN medium. No LiP activity was seen in any of the media tested; however, probing the genomic DNA with the LiP cDNA (CLG4) from the white rot fungus Phanerochaete chrysosporium showed distinct hybridization bands suggesting the presence of lip-like sequences in G. lucidum.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>D'Souza</LastName><ForeName>T M</ForeName><Initials>TM</Initials><AffiliationInfo><Affiliation>Department of Microbiology and NSF Center for Microbial Ecology, Michigan State University, East Lansing, Michigan 48824-1101, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Merritt</LastName><ForeName>C S</ForeName><Initials>CS</Initials></Author><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>C A</ForeName><Initials>CA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-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>632XD903SP</RegistryNumber><NameOfSubstance UI="D005707">Gallic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>E390O181H5</RegistryNumber><NameOfSubstance UI="C001945">syringic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</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="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005707" MajorTopicYN="N">Gallic Acid</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042845" MajorTopicYN="N">Laccase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" 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IdType="pubmed">8167033</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Merritt, C S" sort="Merritt, C S" uniqKey="Merritt C" first="C S" last="Merritt">C S Merritt</name><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="D Souza, T M" sort="D Souza, T M" uniqKey="D Souza T" first="T M" last="D'Souza">T M D'Souza</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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