Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions.
Identifieur interne : 000D08 ( Main/Exploration ); précédent : 000D07; suivant : 000D09Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions.
Auteurs : S B Dass [États-Unis] ; C G Dosoretz ; C A Reddy ; H E GrethleinSource :
- Archives of microbiology [ 0302-8933 ] ; 1995.
Descripteurs français
- KwdFr :
- Azote (pharmacologie), Basidiomycota (effets des médicaments et des substances chimiques), Basidiomycota (enzymologie), Concentration en ions d'hydrogène (MeSH), Dépollution biologique de l'environnement (MeSH), Endopeptidases (composition chimique), Endopeptidases (effets des médicaments et des substances chimiques), Endopeptidases (isolement et purification), Endopeptidases (métabolisme), Inhibiteurs de protéases (pharmacologie), Lignine (métabolisme), Peroxidases (métabolisme), Température (MeSH).
- MESH :
- composition chimique : Endopeptidases.
- effets des médicaments et des substances chimiques : Basidiomycota, Endopeptidases.
- enzymologie : Basidiomycota.
- isolement et purification : Endopeptidases.
- métabolisme : Endopeptidases, Lignine, Peroxidases.
- pharmacologie : Azote, Inhibiteurs de protéases.
- Concentration en ions d'hydrogène, Dépollution biologique de l'environnement, Température.
English descriptors
- KwdEn :
- Basidiomycota (drug effects), Basidiomycota (enzymology), Biodegradation, Environmental (MeSH), Endopeptidases (chemistry), Endopeptidases (drug effects), Endopeptidases (isolation & purification), Endopeptidases (metabolism), Hydrogen-Ion Concentration (MeSH), Lignin (metabolism), Nitrogen (pharmacology), Peroxidases (metabolism), Protease Inhibitors (pharmacology), Temperature (MeSH).
- MESH :
- chemical , chemistry : Endopeptidases.
- drug effects : Basidiomycota, Endopeptidases.
- enzymology : Basidiomycota.
- chemical , isolation & purification : Endopeptidases.
- chemical , metabolism : Endopeptidases, Lignin, Peroxidases.
- chemical , pharmacology : Nitrogen, Protease Inhibitors.
- Biodegradation, Environmental, Hydrogen-Ion Concentration, Temperature.
Abstract
When subjected to nitrogen limitation, the wood-degrading fungus Phanerochaete chrysosporium produces two groups of secondary metabolic, extracellular isoenzymes that depolymerize lignin in wood: lignin peroxidases and manganese peroxidases. We have shown earlier the turnover in activity of the lignin peroxidases to be due in part to extracellular proteolytic activity. This paper reports the electrophoretic characterization of two sets of acidic extracellular proteases produced by submerged cultures of P. chrysosporium. The protease activity seen on day 2 of incubation, during primary growth when nitrogen levels are not known to be limiting, consisted of at least six proteolytic bands ranging in size from 82 to 22 kDa. The activity of this primary protease was strongly reduced in the presence of SDS. Following the day 2, when nitrogen levels are known to become limiting and cultures become ligninolytic, the main protease activity (secondary protease) consisted of a major proteolytic band of 76 kDa and a minor band of 25 kDa. The major and minor secondary protease activities were inhibited by phenylmethyl-sulfonyl fluoride and pepstatin A, respectively. When cultures were grown in the presence of excess nitrogen (non-ligninolytic condition), the primary protease remained the principal protease throughout the culture period. These results identify and characterize a specific proteolytic activity associated with conditions that promote lignin degradation.
DOI: 10.1007/BF00393377
PubMed: 7763133
Affiliations:
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Le document en format XML
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Dosoretz</name></author><author><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name></author><author><name sortKey="Grethlein, H E" sort="Grethlein, H E" uniqKey="Grethlein H" first="H E" last="Grethlein">H E Grethlein</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:7763133</idno><idno type="pmid">7763133</idno><idno type="doi">10.1007/BF00393377</idno><idno type="wicri:Area/Main/Corpus">000D10</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D10</idno><idno type="wicri:Area/Main/Curation">000D10</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D10</idno><idno type="wicri:Area/Main/Exploration">000D10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions.</title><author><name sortKey="Dass, S B" sort="Dass, S B" uniqKey="Dass S" first="S B" last="Dass">S B Dass</name><affiliation wicri:level="4"><nlm:affiliation>Department of Microbiology and Public Health, Michigan State University, East Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Public Health, Michigan State University, East Lansing 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Dosoretz, C G" sort="Dosoretz, C G" uniqKey="Dosoretz C" first="C G" last="Dosoretz">C G Dosoretz</name></author><author><name sortKey="Reddy, C A" sort="Reddy, C A" uniqKey="Reddy C" first="C A" last="Reddy">C A Reddy</name></author><author><name sortKey="Grethlein, H E" sort="Grethlein, H E" uniqKey="Grethlein H" first="H E" last="Grethlein">H E Grethlein</name></author></analytic><series><title level="j">Archives of microbiology</title><idno type="ISSN">0302-8933</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (drug effects)</term><term>Basidiomycota (enzymology)</term><term>Biodegradation, Environmental (MeSH)</term><term>Endopeptidases (chemistry)</term><term>Endopeptidases (drug effects)</term><term>Endopeptidases (isolation & purification)</term><term>Endopeptidases (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Lignin (metabolism)</term><term>Nitrogen (pharmacology)</term><term>Peroxidases (metabolism)</term><term>Protease Inhibitors (pharmacology)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Azote (pharmacologie)</term><term>Basidiomycota (effets des médicaments et des substances chimiques)</term><term>Basidiomycota (enzymologie)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Endopeptidases (composition chimique)</term><term>Endopeptidases (effets des médicaments et des substances chimiques)</term><term>Endopeptidases (isolement et purification)</term><term>Endopeptidases (métabolisme)</term><term>Inhibiteurs de protéases (pharmacologie)</term><term>Lignine (métabolisme)</term><term>Peroxidases (métabolisme)</term><term>Température (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Basidiomycota</term><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Basidiomycota</term><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endopeptidases</term><term>Lignin</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endopeptidases</term><term>Lignine</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Azote</term><term>Inhibiteurs de protéases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Nitrogen</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Hydrogen-Ion Concentration</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Dépollution biologique de l'environnement</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">When subjected to nitrogen limitation, the wood-degrading fungus Phanerochaete chrysosporium produces two groups of secondary metabolic, extracellular isoenzymes that depolymerize lignin in wood: lignin peroxidases and manganese peroxidases. We have shown earlier the turnover in activity of the lignin peroxidases to be due in part to extracellular proteolytic activity. This paper reports the electrophoretic characterization of two sets of acidic extracellular proteases produced by submerged cultures of P. chrysosporium. The protease activity seen on day 2 of incubation, during primary growth when nitrogen levels are not known to be limiting, consisted of at least six proteolytic bands ranging in size from 82 to 22 kDa. The activity of this primary protease was strongly reduced in the presence of SDS. Following the day 2, when nitrogen levels are known to become limiting and cultures become ligninolytic, the main protease activity (secondary protease) consisted of a major proteolytic band of 76 kDa and a minor band of 25 kDa. The major and minor secondary protease activities were inhibited by phenylmethyl-sulfonyl fluoride and pepstatin A, respectively. When cultures were grown in the presence of excess nitrogen (non-ligninolytic condition), the primary protease remained the principal protease throughout the culture period. These results identify and characterize a specific proteolytic activity associated with conditions that promote lignin degradation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7763133</PMID><DateCompleted><Year>1995</Year><Month>06</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0302-8933</ISSN><JournalIssue CitedMedium="Print"><Volume>163</Volume><Issue>4</Issue><PubDate><Year>1995</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Archives of microbiology</Title><ISOAbbreviation>Arch Microbiol</ISOAbbreviation></Journal><ArticleTitle>Extracellular proteases produced by the wood-degrading fungus Phanerochaete chrysosporium under ligninolytic and non-ligninolytic conditions.</ArticleTitle><Pagination><MedlinePgn>254-8</MedlinePgn></Pagination><Abstract><AbstractText>When subjected to nitrogen limitation, the wood-degrading fungus Phanerochaete chrysosporium produces two groups of secondary metabolic, extracellular isoenzymes that depolymerize lignin in wood: lignin peroxidases and manganese peroxidases. We have shown earlier the turnover in activity of the lignin peroxidases to be due in part to extracellular proteolytic activity. This paper reports the electrophoretic characterization of two sets of acidic extracellular proteases produced by submerged cultures of P. chrysosporium. The protease activity seen on day 2 of incubation, during primary growth when nitrogen levels are not known to be limiting, consisted of at least six proteolytic bands ranging in size from 82 to 22 kDa. The activity of this primary protease was strongly reduced in the presence of SDS. Following the day 2, when nitrogen levels are known to become limiting and cultures become ligninolytic, the main protease activity (secondary protease) consisted of a major proteolytic band of 76 kDa and a minor band of 25 kDa. The major and minor secondary protease activities were inhibited by phenylmethyl-sulfonyl fluoride and pepstatin A, respectively. When cultures were grown in the presence of excess nitrogen (non-ligninolytic condition), the primary protease remained the principal protease throughout the culture period. These results identify and characterize a specific proteolytic activity associated with conditions that promote lignin degradation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dass</LastName><ForeName>S B</ForeName><Initials>SB</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Public Health, Michigan State University, East Lansing 48824, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dosoretz</LastName><ForeName>C G</ForeName><Initials>CG</Initials></Author><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>C A</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Grethlein</LastName><ForeName>H E</ForeName><Initials>HE</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>IR01 GM39032-01</GrantID><Acronym>GM</Acronym><Agency>NIGMS 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>Germany</Country><MedlineTA>Arch Microbiol</MedlineTA><NlmUniqueID>0410427</NlmUniqueID><ISSNLinking>0302-8933</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</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 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>N762921K75</RegistryNumber><NameOfSubstance UI="D009584">Nitrogen</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></MeshHeading><MeshHeading><DescriptorName UI="D001673" MajorTopicYN="N">Biodegradation, Environmental</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>4</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7763133</ArticleId><ArticleId IdType="doi">10.1007/BF00393377</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Eur J Biochem. 1982 Jun;124(3):635-42</Citation><ArticleIdList><ArticleId IdType="pubmed">7049699</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Environ Microbiol. 1990 Apr;56(4):837-43</Citation><ArticleIdList><ArticleId 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last="Grethlein">H E Grethlein</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="Dass, S B" sort="Dass, S B" uniqKey="Dass S" first="S B" last="Dass">S B Dass</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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