Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose.
Identifieur interne : 000546 ( Main/Exploration ); précédent : 000545; suivant : 000547Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose.
Auteurs : Sonam Mahajan [Canada] ; Emma R. MasterSource :
- Applied microbiology and biotechnology [ 1432-0614 ] ; 2010.
Descripteurs français
- KwdFr :
- Cellulase (composition chimique), Cellulase (génétique), Cellulase (métabolisme), Cellulases (composition chimique), Cellulases (génétique), Cellulases (métabolisme), Cellulose (métabolisme), Glycosidases (composition chimique), Glycosidases (génétique), Glycosidases (métabolisme), Lignine (métabolisme), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Peptide hydrolases (composition chimique), Peptide hydrolases (métabolisme), Phanerochaete (croissance et développement), Phanerochaete (enzymologie), Phanerochaete (génétique), Phanerochaete (métabolisme), Picea (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéomique (MeSH), Spectrométrie de masse en tandem (MeSH), beta-Mannosidase (composition chimique), beta-Mannosidase (génétique), beta-Mannosidase (métabolisme).
- MESH :
- composition chimique : Cellulase, Cellulases, Glycosidases, Oxidoreductases, Peptide hydrolases, Protéines fongiques, beta-Mannosidase.
- croissance et développement : Phanerochaete.
- enzymologie : Phanerochaete.
- génétique : Cellulase, Cellulases, Glycosidases, Phanerochaete, Protéines fongiques, beta-Mannosidase.
- métabolisme : Cellulase, Cellulases, Cellulose, Glycosidases, Lignine, Oxidoreductases, Peptide hydrolases, Phanerochaete, Picea, Protéines fongiques, beta-Mannosidase.
- Protéomique, Spectrométrie de masse en tandem.
English descriptors
- KwdEn :
- Cellulase (chemistry), Cellulase (genetics), Cellulase (metabolism), Cellulases (chemistry), Cellulases (genetics), Cellulases (metabolism), Cellulose (metabolism), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Glycoside Hydrolases (chemistry), Glycoside Hydrolases (genetics), Glycoside Hydrolases (metabolism), Lignin (metabolism), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Peptide Hydrolases (chemistry), Peptide Hydrolases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Phanerochaete (growth & development), Phanerochaete (metabolism), Picea (metabolism), Proteomics (MeSH), Tandem Mass Spectrometry (MeSH), beta-Mannosidase (chemistry), beta-Mannosidase (genetics), beta-Mannosidase (metabolism).
- MESH :
- chemical , chemistry : Cellulase, Cellulases, Fungal Proteins, Glycoside Hydrolases, Oxidoreductases, Peptide Hydrolases, beta-Mannosidase.
- chemical , genetics : Cellulase, Cellulases, Fungal Proteins, Glycoside Hydrolases, beta-Mannosidase.
- chemical , metabolism : Cellulase, Cellulases, Cellulose, Fungal Proteins, Glycoside Hydrolases, Lignin, Oxidoreductases, Peptide Hydrolases, beta-Mannosidase.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- growth & development : Phanerochaete.
- metabolism : Phanerochaete, Picea.
- Proteomics, Tandem Mass Spectrometry.
Abstract
Proteins secreted by the white-rot, softwood-degrading fungus Phanerochaete carnosa during growth on cellulose and spruce were analyzed using tandem mass spectrometry and de novo sequencing. Homology-driven proteomics was applied to compare P. carnosa peptide sequences to proteins in Phanerochaete chrysosporium using MS BLAST and non-gapped alignment. In this way, 665 and 365 peptides from cellulose and spruce cultivations, respectively, were annotated. Predicted activities included endoglucanases from glycoside hydrolase (GH) families 5, 16, and 61, cellobiohydrolases from GH6 and GH7, GH3 beta-glucosidases, xylanases from GH10 and GH11, GH2 beta-mannosidases, and debranching hemicellulases from GH43 and CE15. Peptides corresponding to glyoxal oxidases, peroxidases, and glycopeptides that could participate in lignin degradation were also detected. Overall, predicted activities detected in extracellular filtrates of cellulose and spruce cultures were similar, suggesting that the adaptation of P. carnosa to growth on lignocellulose might result from fine tuning the expression of similar enzyme families.
DOI: 10.1007/s00253-010-2516-4
PubMed: 20306191
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose.</title><author><name sortKey="Mahajan, Sonam" sort="Mahajan, Sonam" uniqKey="Mahajan S" first="Sonam" last="Mahajan">Sonam Mahajan</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Master, Emma R" sort="Master, Emma R" uniqKey="Master E" first="Emma R" last="Master">Emma R. Master</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20306191</idno><idno type="pmid">20306191</idno><idno type="doi">10.1007/s00253-010-2516-4</idno><idno type="wicri:Area/Main/Corpus">000562</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000562</idno><idno type="wicri:Area/Main/Curation">000562</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000562</idno><idno type="wicri:Area/Main/Exploration">000562</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose.</title><author><name sortKey="Mahajan, Sonam" sort="Mahajan, Sonam" uniqKey="Mahajan S" first="Sonam" last="Mahajan">Sonam Mahajan</name><affiliation wicri:level="4"><nlm:affiliation>Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5</wicri:regionArea><orgName type="university">Université de Toronto</orgName><placeName><settlement type="city">Toronto</settlement><region type="state">Ontario</region></placeName></affiliation></author><author><name sortKey="Master, Emma R" sort="Master, Emma R" uniqKey="Master E" first="Emma R" last="Master">Emma R. Master</name></author></analytic><series><title level="j">Applied microbiology and biotechnology</title><idno type="eISSN">1432-0614</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cellulase (chemistry)</term><term>Cellulase (genetics)</term><term>Cellulase (metabolism)</term><term>Cellulases (chemistry)</term><term>Cellulases (genetics)</term><term>Cellulases (metabolism)</term><term>Cellulose (metabolism)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Glycoside Hydrolases (chemistry)</term><term>Glycoside Hydrolases (genetics)</term><term>Glycoside Hydrolases (metabolism)</term><term>Lignin (metabolism)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (metabolism)</term><term>Peptide Hydrolases (chemistry)</term><term>Peptide Hydrolases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Phanerochaete (growth & development)</term><term>Phanerochaete (metabolism)</term><term>Picea (metabolism)</term><term>Proteomics (MeSH)</term><term>Tandem Mass Spectrometry (MeSH)</term><term>beta-Mannosidase (chemistry)</term><term>beta-Mannosidase (genetics)</term><term>beta-Mannosidase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellulase (composition chimique)</term><term>Cellulase (génétique)</term><term>Cellulase (métabolisme)</term><term>Cellulases (composition chimique)</term><term>Cellulases (génétique)</term><term>Cellulases (métabolisme)</term><term>Cellulose (métabolisme)</term><term>Glycosidases (composition chimique)</term><term>Glycosidases (génétique)</term><term>Glycosidases (métabolisme)</term><term>Lignine (métabolisme)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (métabolisme)</term><term>Peptide hydrolases (composition chimique)</term><term>Peptide hydrolases (métabolisme)</term><term>Phanerochaete (croissance et développement)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Phanerochaete (métabolisme)</term><term>Picea (métabolisme)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Protéomique (MeSH)</term><term>Spectrométrie de masse en tandem (MeSH)</term><term>beta-Mannosidase (composition chimique)</term><term>beta-Mannosidase (génétique)</term><term>beta-Mannosidase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulase</term><term>Cellulases</term><term>Fungal Proteins</term><term>Glycoside Hydrolases</term><term>Oxidoreductases</term><term>Peptide Hydrolases</term><term>beta-Mannosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cellulase</term><term>Cellulases</term><term>Fungal Proteins</term><term>Glycoside Hydrolases</term><term>beta-Mannosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulase</term><term>Cellulases</term><term>Cellulose</term><term>Fungal Proteins</term><term>Glycoside Hydrolases</term><term>Lignin</term><term>Oxidoreductases</term><term>Peptide Hydrolases</term><term>beta-Mannosidase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulase</term><term>Cellulases</term><term>Glycosidases</term><term>Oxidoreductases</term><term>Peptide hydrolases</term><term>Protéines fongiques</term><term>beta-Mannosidase</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cellulase</term><term>Cellulases</term><term>Glycosidases</term><term>Phanerochaete</term><term>Protéines fongiques</term><term>beta-Mannosidase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term><term>Picea</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulase</term><term>Cellulases</term><term>Cellulose</term><term>Glycosidases</term><term>Lignine</term><term>Oxidoreductases</term><term>Peptide hydrolases</term><term>Phanerochaete</term><term>Picea</term><term>Protéines fongiques</term><term>beta-Mannosidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Proteomics</term><term>Tandem Mass Spectrometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Protéomique</term><term>Spectrométrie de masse en tandem</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Proteins secreted by the white-rot, softwood-degrading fungus Phanerochaete carnosa during growth on cellulose and spruce were analyzed using tandem mass spectrometry and de novo sequencing. Homology-driven proteomics was applied to compare P. carnosa peptide sequences to proteins in Phanerochaete chrysosporium using MS BLAST and non-gapped alignment. In this way, 665 and 365 peptides from cellulose and spruce cultivations, respectively, were annotated. Predicted activities included endoglucanases from glycoside hydrolase (GH) families 5, 16, and 61, cellobiohydrolases from GH6 and GH7, GH3 beta-glucosidases, xylanases from GH10 and GH11, GH2 beta-mannosidases, and debranching hemicellulases from GH43 and CE15. Peptides corresponding to glyoxal oxidases, peroxidases, and glycopeptides that could participate in lignin degradation were also detected. Overall, predicted activities detected in extracellular filtrates of cellulose and spruce cultures were similar, suggesting that the adaptation of P. carnosa to growth on lignocellulose might result from fine tuning the expression of similar enzyme families.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20306191</PMID><DateCompleted><Year>2010</Year><Month>08</Month><Day>10</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-0614</ISSN><JournalIssue CitedMedium="Internet"><Volume>86</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>May</Month></PubDate></JournalIssue><Title>Applied microbiology and biotechnology</Title><ISOAbbreviation>Appl Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose.</ArticleTitle><Pagination><MedlinePgn>1903-14</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00253-010-2516-4</ELocationID><Abstract><AbstractText>Proteins secreted by the white-rot, softwood-degrading fungus Phanerochaete carnosa during growth on cellulose and spruce were analyzed using tandem mass spectrometry and de novo sequencing. Homology-driven proteomics was applied to compare P. carnosa peptide sequences to proteins in Phanerochaete chrysosporium using MS BLAST and non-gapped alignment. In this way, 665 and 365 peptides from cellulose and spruce cultivations, respectively, were annotated. Predicted activities included endoglucanases from glycoside hydrolase (GH) families 5, 16, and 61, cellobiohydrolases from GH6 and GH7, GH3 beta-glucosidases, xylanases from GH10 and GH11, GH2 beta-mannosidases, and debranching hemicellulases from GH43 and CE15. Peptides corresponding to glyoxal oxidases, peroxidases, and glycopeptides that could participate in lignin degradation were also detected. Overall, predicted activities detected in extracellular filtrates of cellulose and spruce cultures were similar, suggesting that the adaptation of P. carnosa to growth on lignocellulose might result from fine tuning the expression of similar enzyme families.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mahajan</LastName><ForeName>Sonam</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering and Applied Chemistry, University of Toronto, 200 College Street, Toronto, ON, M5S 3E5, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Master</LastName><ForeName>Emma R</ForeName><Initials>ER</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>03</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Appl Microbiol Biotechnol</MedlineTA><NlmUniqueID>8406612</NlmUniqueID><ISSNLinking>0175-7598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>11132-73-3</RegistryNumber><NameOfSubstance UI="C036909">lignocellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><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 3.2.1.-</RegistryNumber><NameOfSubstance UI="D044602">Cellulases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D006026">Glycoside Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="C023305">hemicellulase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.25</RegistryNumber><NameOfSubstance UI="D044902">beta-Mannosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>OP1R32D61U</RegistryNumber><NameOfSubstance UI="C109691">microcrystalline cellulose</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044602" MajorTopicYN="N">Cellulases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006026" MajorTopicYN="N">Glycoside Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><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="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D028222" MajorTopicYN="N">Picea</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="Y">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053719" MajorTopicYN="N">Tandem Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044902" MajorTopicYN="N">beta-Mannosidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2009</Year><Month>12</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2010</Year><Month>02</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2010</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>3</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>3</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>8</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20306191</ArticleId><ArticleId IdType="doi">10.1007/s00253-010-2516-4</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Ontario</li></region><settlement><li>Toronto</li></settlement><orgName><li>Université de Toronto</li></orgName></list><tree><noCountry><name sortKey="Master, Emma R" sort="Master, Emma R" uniqKey="Master E" first="Emma R" last="Master">Emma R. Master</name></noCountry><country name="Canada"><region name="Ontario"><name sortKey="Mahajan, Sonam" sort="Mahajan, Sonam" uniqKey="Mahajan S" first="Sonam" last="Mahajan">Sonam Mahajan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/PhanerochaeteV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000546 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000546 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= PhanerochaeteV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:20306191
|texte= Proteomic characterization of lignocellulose-degrading enzymes secreted by Phanerochaete carnosa grown on spruce and microcrystalline cellulose.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:20306191" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |