An amperometric enzyme biosensor for real-time measurements of cellobiohydrolase activity on insoluble cellulose.
Identifieur interne : 000468 ( Main/Exploration ); précédent : 000467; suivant : 000469An amperometric enzyme biosensor for real-time measurements of cellobiohydrolase activity on insoluble cellulose.
Auteurs : Nicolaj Cruys-Bagger [Danemark] ; Guilin Ren ; Hirosuke Tatsumi ; Martin J. Baumann ; Nikolaj Spodsberg ; Heidi Delcomyn Andersen ; Lo Gorton ; Kim Borch ; Peter WesthSource :
- Biotechnology and bioengineering [ 1097-0290 ] ; 2012.
Descripteurs français
- KwdFr :
- Analyse de régression (MeSH), Carbohydrate dehydrogenases (composition chimique), Carbohydrate dehydrogenases (métabolisme), Cellulose (analyse), Cellulose (métabolisme), Cellulose 1,4-beta-cellobiosidase (métabolisme), Chromatographie en phase liquide à haute performance (MeSH), Cinétique (MeSH), Enzymes immobilisées (composition chimique), Enzymes immobilisées (métabolisme), Hydrolyse (MeSH), Limite de détection (MeSH), Phanerochaete (enzymologie), Protéines fongiques (composition chimique), Protéines fongiques (métabolisme), Reproductibilité des résultats (MeSH), Techniques de biocapteur (MeSH), Trichoderma (enzymologie), Électrodes (MeSH).
- MESH :
- analyse : Cellulose.
- composition chimique : Carbohydrate dehydrogenases, Enzymes immobilisées, Protéines fongiques.
- enzymologie : Phanerochaete, Trichoderma.
- métabolisme : Carbohydrate dehydrogenases, Cellulose, Cellulose 1,4-beta-cellobiosidase, Enzymes immobilisées, Protéines fongiques.
- Analyse de régression, Chromatographie en phase liquide à haute performance, Cinétique, Hydrolyse, Limite de détection, Reproductibilité des résultats, Techniques de biocapteur, Électrodes.
English descriptors
- KwdEn :
- Biosensing Techniques (MeSH), Carbohydrate Dehydrogenases (chemistry), Carbohydrate Dehydrogenases (metabolism), Cellulose (analysis), Cellulose (metabolism), Cellulose 1,4-beta-Cellobiosidase (metabolism), Chromatography, High Pressure Liquid (MeSH), Electrodes (MeSH), Enzymes, Immobilized (chemistry), Enzymes, Immobilized (metabolism), Fungal Proteins (chemistry), Fungal Proteins (metabolism), Hydrolysis (MeSH), Kinetics (MeSH), Limit of Detection (MeSH), Phanerochaete (enzymology), Regression Analysis (MeSH), Reproducibility of Results (MeSH), Trichoderma (enzymology).
- MESH :
- chemical , analysis : Cellulose.
- chemical , chemistry : Carbohydrate Dehydrogenases, Enzymes, Immobilized, Fungal Proteins.
- chemical , metabolism : Carbohydrate Dehydrogenases, Cellulose, Cellulose 1,4-beta-Cellobiosidase, Enzymes, Immobilized, Fungal Proteins.
- enzymology : Phanerochaete, Trichoderma.
- Biosensing Techniques, Chromatography, High Pressure Liquid, Electrodes, Hydrolysis, Kinetics, Limit of Detection, Regression Analysis, Reproducibility of Results.
Abstract
An amperometric enzyme biosensor for continuous detection of cellobiose has been implemented as an enzyme assay for cellulases. We show that the initial kinetics for cellobiohydrolase I, Cel7A from Trichoderma reesei, acting on different types of cellulose substrates, semi-crystalline and amorphous, can be monitored directly and in real-time by an enzyme-modified electrode based on cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium (Pc). PcCDH was cross-linked and immobilized on the surface of a carbon paste electrode which contained a mediator, benzoquinone. An oxidation current of the reduced mediator, hydroquinone, produced by the CDH-catalyzed reaction with cellobiose, was recorded under constant-potential amperometry at +0.5 V (vs. Ag/AgCl). The CDH-biosensors showed high sensitivity (87.7 µA mM(-1) cm(-2)), low detection limit (25 nM), and fast response time (t(95%) ≈ 3 s) and this provided experimental access to the transient kinetics of cellobiohydrolases acting on insoluble cellulose. The response from the CDH-biosensor during enzymatic hydrolysis was corrected for the specificity of PcCDH for the β-anomer of cello-oligosaccharides and the approach were validated against HPLC. It is suggested that quantitative, real-time data on pure insoluble cellulose substrates will be useful in attempts to probe the molecular mechanism underlying enzymatic hydrolysis of cellulose.
DOI: 10.1002/bit.24593
PubMed: 22767376
Affiliations:
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Baumann</name></author><author><name sortKey="Spodsberg, Nikolaj" sort="Spodsberg, Nikolaj" uniqKey="Spodsberg N" first="Nikolaj" last="Spodsberg">Nikolaj Spodsberg</name></author><author><name sortKey="Andersen, Heidi Delcomyn" sort="Andersen, Heidi Delcomyn" uniqKey="Andersen H" first="Heidi Delcomyn" last="Andersen">Heidi Delcomyn Andersen</name></author><author><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></author><author><name sortKey="Borch, Kim" sort="Borch, Kim" uniqKey="Borch K" first="Kim" last="Borch">Kim Borch</name></author><author><name sortKey="Westh, Peter" sort="Westh, Peter" uniqKey="Westh P" first="Peter" last="Westh">Peter Westh</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22767376</idno><idno type="pmid">22767376</idno><idno type="doi">10.1002/bit.24593</idno><idno type="wicri:Area/Main/Corpus">000415</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000415</idno><idno type="wicri:Area/Main/Curation">000415</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000415</idno><idno type="wicri:Area/Main/Exploration">000415</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">An amperometric enzyme biosensor for real-time measurements of cellobiohydrolase activity on insoluble cellulose.</title><author><name sortKey="Cruys Bagger, Nicolaj" sort="Cruys Bagger, Nicolaj" uniqKey="Cruys Bagger N" first="Nicolaj" last="Cruys-Bagger">Nicolaj Cruys-Bagger</name><affiliation wicri:level="1"><nlm:affiliation>Research Unit for Functional Biomaterials, NSM, Roskilde University, Universitetsvej 1, DK-4000 Roskilde, Denmark.</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Research Unit for Functional Biomaterials, NSM, Roskilde University, Universitetsvej 1, DK-4000 Roskilde</wicri:regionArea><wicri:noRegion>DK-4000 Roskilde</wicri:noRegion></affiliation></author><author><name sortKey="Ren, Guilin" sort="Ren, Guilin" uniqKey="Ren G" first="Guilin" last="Ren">Guilin Ren</name></author><author><name sortKey="Tatsumi, Hirosuke" sort="Tatsumi, Hirosuke" uniqKey="Tatsumi H" first="Hirosuke" last="Tatsumi">Hirosuke Tatsumi</name></author><author><name sortKey="Baumann, Martin J" sort="Baumann, Martin J" uniqKey="Baumann M" first="Martin J" last="Baumann">Martin J. Baumann</name></author><author><name sortKey="Spodsberg, Nikolaj" sort="Spodsberg, Nikolaj" uniqKey="Spodsberg N" first="Nikolaj" last="Spodsberg">Nikolaj Spodsberg</name></author><author><name sortKey="Andersen, Heidi Delcomyn" sort="Andersen, Heidi Delcomyn" uniqKey="Andersen H" first="Heidi Delcomyn" last="Andersen">Heidi Delcomyn Andersen</name></author><author><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name></author><author><name sortKey="Borch, Kim" sort="Borch, Kim" uniqKey="Borch K" first="Kim" last="Borch">Kim Borch</name></author><author><name sortKey="Westh, Peter" sort="Westh, Peter" uniqKey="Westh P" first="Peter" last="Westh">Peter Westh</name></author></analytic><series><title level="j">Biotechnology and bioengineering</title><idno type="eISSN">1097-0290</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biosensing Techniques (MeSH)</term><term>Carbohydrate Dehydrogenases (chemistry)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Cellulose (analysis)</term><term>Cellulose (metabolism)</term><term>Cellulose 1,4-beta-Cellobiosidase (metabolism)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Electrodes (MeSH)</term><term>Enzymes, Immobilized (chemistry)</term><term>Enzymes, Immobilized (metabolism)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (metabolism)</term><term>Hydrolysis (MeSH)</term><term>Kinetics (MeSH)</term><term>Limit of Detection (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Regression Analysis (MeSH)</term><term>Reproducibility of Results (MeSH)</term><term>Trichoderma (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de régression (MeSH)</term><term>Carbohydrate dehydrogenases (composition chimique)</term><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Cellulose (analyse)</term><term>Cellulose (métabolisme)</term><term>Cellulose 1,4-beta-cellobiosidase (métabolisme)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Cinétique (MeSH)</term><term>Enzymes immobilisées (composition chimique)</term><term>Enzymes immobilisées (métabolisme)</term><term>Hydrolyse (MeSH)</term><term>Limite de détection (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (métabolisme)</term><term>Reproductibilité des résultats (MeSH)</term><term>Techniques de biocapteur (MeSH)</term><term>Trichoderma (enzymologie)</term><term>Électrodes (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Cellulose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Enzymes, Immobilized</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cellulose</term><term>Cellulose 1,4-beta-Cellobiosidase</term><term>Enzymes, Immobilized</term><term>Fungal Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Cellulose</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Enzymes immobilisées</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term><term>Trichoderma</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Cellulose</term><term>Cellulose 1,4-beta-cellobiosidase</term><term>Enzymes immobilisées</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biosensing Techniques</term><term>Chromatography, High Pressure Liquid</term><term>Electrodes</term><term>Hydrolysis</term><term>Kinetics</term><term>Limit of Detection</term><term>Regression Analysis</term><term>Reproducibility of Results</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de régression</term><term>Chromatographie en phase liquide à haute performance</term><term>Cinétique</term><term>Hydrolyse</term><term>Limite de détection</term><term>Reproductibilité des résultats</term><term>Techniques de biocapteur</term><term>Électrodes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An amperometric enzyme biosensor for continuous detection of cellobiose has been implemented as an enzyme assay for cellulases. We show that the initial kinetics for cellobiohydrolase I, Cel7A from Trichoderma reesei, acting on different types of cellulose substrates, semi-crystalline and amorphous, can be monitored directly and in real-time by an enzyme-modified electrode based on cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium (Pc). PcCDH was cross-linked and immobilized on the surface of a carbon paste electrode which contained a mediator, benzoquinone. An oxidation current of the reduced mediator, hydroquinone, produced by the CDH-catalyzed reaction with cellobiose, was recorded under constant-potential amperometry at +0.5 V (vs. Ag/AgCl). The CDH-biosensors showed high sensitivity (87.7 µA mM(-1) cm(-2)), low detection limit (25 nM), and fast response time (t(95%) ≈ 3 s) and this provided experimental access to the transient kinetics of cellobiohydrolases acting on insoluble cellulose. The response from the CDH-biosensor during enzymatic hydrolysis was corrected for the specificity of PcCDH for the β-anomer of cello-oligosaccharides and the approach were validated against HPLC. It is suggested that quantitative, real-time data on pure insoluble cellulose substrates will be useful in attempts to probe the molecular mechanism underlying enzymatic hydrolysis of cellulose.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22767376</PMID><DateCompleted><Year>2013</Year><Month>03</Month><Day>20</Day></DateCompleted><DateRevised><Year>2012</Year><Month>10</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1097-0290</ISSN><JournalIssue CitedMedium="Internet"><Volume>109</Volume><Issue>12</Issue><PubDate><Year>2012</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Biotechnology and bioengineering</Title><ISOAbbreviation>Biotechnol Bioeng</ISOAbbreviation></Journal><ArticleTitle>An amperometric enzyme biosensor for real-time measurements of cellobiohydrolase activity on insoluble cellulose.</ArticleTitle><Pagination><MedlinePgn>3199-204</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/bit.24593</ELocationID><Abstract><AbstractText>An amperometric enzyme biosensor for continuous detection of cellobiose has been implemented as an enzyme assay for cellulases. We show that the initial kinetics for cellobiohydrolase I, Cel7A from Trichoderma reesei, acting on different types of cellulose substrates, semi-crystalline and amorphous, can be monitored directly and in real-time by an enzyme-modified electrode based on cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium (Pc). PcCDH was cross-linked and immobilized on the surface of a carbon paste electrode which contained a mediator, benzoquinone. An oxidation current of the reduced mediator, hydroquinone, produced by the CDH-catalyzed reaction with cellobiose, was recorded under constant-potential amperometry at +0.5 V (vs. Ag/AgCl). The CDH-biosensors showed high sensitivity (87.7 µA mM(-1) cm(-2)), low detection limit (25 nM), and fast response time (t(95%) ≈ 3 s) and this provided experimental access to the transient kinetics of cellobiohydrolases acting on insoluble cellulose. The response from the CDH-biosensor during enzymatic hydrolysis was corrected for the specificity of PcCDH for the β-anomer of cello-oligosaccharides and the approach were validated against HPLC. It is suggested that quantitative, real-time data on pure insoluble cellulose substrates will be useful in attempts to probe the molecular mechanism underlying enzymatic hydrolysis of cellulose.</AbstractText><CopyrightInformation>Copyright © 2012 Wiley Periodicals, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cruys-Bagger</LastName><ForeName>Nicolaj</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Research Unit for Functional Biomaterials, NSM, Roskilde University, Universitetsvej 1, DK-4000 Roskilde, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ren</LastName><ForeName>Guilin</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Tatsumi</LastName><ForeName>Hirosuke</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Baumann</LastName><ForeName>Martin J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Spodsberg</LastName><ForeName>Nikolaj</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Andersen</LastName><ForeName>Heidi Delcomyn</ForeName><Initials>HD</Initials></Author><Author ValidYN="Y"><LastName>Gorton</LastName><ForeName>Lo</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Borch</LastName><ForeName>Kim</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Westh</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>07</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biotechnol Bioeng</MedlineTA><NlmUniqueID>7502021</NlmUniqueID><ISSNLinking>0006-3592</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004800">Enzymes, Immobilized</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D002237">Carbohydrate Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.99.18</RegistryNumber><NameOfSubstance UI="C019859">cellobiose-quinone oxidoreductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.91</RegistryNumber><NameOfSubstance UI="D043366">Cellulose 1,4-beta-Cellobiosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015374" MajorTopicYN="Y">Biosensing Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002237" MajorTopicYN="N">Carbohydrate Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="N">Cellulose</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D043366" MajorTopicYN="N">Cellulose 1,4-beta-Cellobiosidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004566" MajorTopicYN="N">Electrodes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004800" MajorTopicYN="N">Enzymes, Immobilized</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057230" MajorTopicYN="N">Limit of Detection</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012044" MajorTopicYN="N">Regression Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015203" MajorTopicYN="N">Reproducibility of Results</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014242" MajorTopicYN="N">Trichoderma</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>04</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>06</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>06</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>7</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>7</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>3</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22767376</ArticleId><ArticleId IdType="doi">10.1002/bit.24593</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Danemark</li></country></list><tree><noCountry><name sortKey="Andersen, Heidi Delcomyn" sort="Andersen, Heidi Delcomyn" uniqKey="Andersen H" first="Heidi Delcomyn" last="Andersen">Heidi Delcomyn Andersen</name><name sortKey="Baumann, Martin J" sort="Baumann, Martin J" uniqKey="Baumann M" first="Martin J" last="Baumann">Martin J. Baumann</name><name sortKey="Borch, Kim" sort="Borch, Kim" uniqKey="Borch K" first="Kim" last="Borch">Kim Borch</name><name sortKey="Gorton, Lo" sort="Gorton, Lo" uniqKey="Gorton L" first="Lo" last="Gorton">Lo Gorton</name><name sortKey="Ren, Guilin" sort="Ren, Guilin" uniqKey="Ren G" first="Guilin" last="Ren">Guilin Ren</name><name sortKey="Spodsberg, Nikolaj" sort="Spodsberg, Nikolaj" uniqKey="Spodsberg N" first="Nikolaj" last="Spodsberg">Nikolaj Spodsberg</name><name sortKey="Tatsumi, Hirosuke" sort="Tatsumi, Hirosuke" uniqKey="Tatsumi H" first="Hirosuke" last="Tatsumi">Hirosuke Tatsumi</name><name sortKey="Westh, Peter" sort="Westh, Peter" uniqKey="Westh P" first="Peter" last="Westh">Peter Westh</name></noCountry><country name="Danemark"><noRegion><name sortKey="Cruys Bagger, Nicolaj" sort="Cruys Bagger, Nicolaj" uniqKey="Cruys Bagger N" first="Nicolaj" last="Cruys-Bagger">Nicolaj Cruys-Bagger</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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