Enhanced cellulose degradation by nano-complexed enzymes: Synergism between a scaffold-linked exoglucanase and a free endoglucanase.
Identifieur interne : 003276 ( Main/Exploration ); précédent : 003275; suivant : 003277Enhanced cellulose degradation by nano-complexed enzymes: Synergism between a scaffold-linked exoglucanase and a free endoglucanase.
Auteurs : Sarah Moraïs [Israël] ; Arnon Heyman ; Yoav Barak ; Jonathan Caspi ; David B. Wilson ; Raphael Lamed ; Oded Shoseyov ; Edward A. BayerSource :
- Journal of biotechnology [ 1873-4863 ] ; 2010.
Descripteurs français
- KwdFr :
- Biotechnologie (méthodes), Cellulase (métabolisme), Cellulose (métabolisme), Chromatographie sur gel (MeSH), Clostridium (métabolisme), Nanostructures (composition chimique), Nanostructures (ultrastructure), Populus (métabolisme), Protéines chromosomiques nonhistones (métabolisme), Protéines du cycle cellulaire (métabolisme), Protéines recombinantes (métabolisme), Protéines végétales (ultrastructure).
- MESH :
- composition chimique : Nanostructures.
- métabolisme : Cellulase, Cellulose, Clostridium, Populus, Protéines chromosomiques nonhistones, Protéines du cycle cellulaire, Protéines recombinantes.
- méthodes : Biotechnologie.
- ultrastructure : Chromatographie sur gel, Nanostructures, Protéines végétales.
English descriptors
- KwdEn :
- Biotechnology (methods), Cell Cycle Proteins (metabolism), Cellulase (metabolism), Cellulose (metabolism), Chromatography, Gel (MeSH), Chromosomal Proteins, Non-Histone (metabolism), Clostridium (metabolism), Nanostructures (chemistry), Nanostructures (ultrastructure), Plant Proteins (ultrastructure), Populus (metabolism), Recombinant Proteins (metabolism).
- MESH :
- chemical , metabolism : Cell Cycle Proteins, Cellulase, Cellulose, Chromosomal Proteins, Non-Histone, Recombinant Proteins.
- chemistry : Nanostructures.
- metabolism : Clostridium, Populus.
- methods : Biotechnology.
- ultrastructure : Nanostructures, Plant Proteins.
- Chromatography, Gel.
Abstract
Protein molecular scaffolds are attracting interest as natural candidates for the presentation of enzymes and acceleration of catalytic reactions. We have previously reported evidence that the stable protein 1 (SP1) from Populustremula can be employed as a molecular scaffold for the presentation of either catalytic or structural binding (cellulosomal cohesin) modules. In the present work, we have displayed a potent exoglucanase (Cel6B) from the aerobic cellulolytic bacterium, Thermobifida fusca, on a cohesin-bearing SP1 scaffold. For this purpose, a chimaeric form of the enzyme, fused to a cellulosomal dockerin module, was prepared. Full incorporation of 12 dockerin-bearing exoglucanase molecules onto the cohesin-bearing scaffold was achieved. Cellulase activity was tested on two cellulosic substrates with different levels of crystallinity, and the activity of the scaffold-linked exoglucanase was significantly reduced, compared to the free dockerin-containing enzyme. However, addition of relatively low concentrations of a free wild-type endoglucanase (T. fusca Cel5A) that bears a cellulose-binding module, in combination with the complexed exoglucanase resulted in a marked rise in activity on both cellulosic substrates. The endoglucanase cleaves internal sites of the cellulose chains, and the new chain ends of the substrate were now readily accessible to the scaffold-borne exoglucanase, thereby resulting in highly effective, synergistic degradation of cellulosic substrates.
DOI: 10.1016/j.jbiotec.2010.04.012
PubMed: 20438772
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Wilson</name></author><author><name sortKey="Lamed, Raphael" sort="Lamed, Raphael" uniqKey="Lamed R" first="Raphael" last="Lamed">Raphael Lamed</name></author><author><name sortKey="Shoseyov, Oded" sort="Shoseyov, Oded" uniqKey="Shoseyov O" first="Oded" last="Shoseyov">Oded Shoseyov</name></author><author><name sortKey="Bayer, Edward A" sort="Bayer, Edward A" uniqKey="Bayer E" first="Edward A" last="Bayer">Edward A. Bayer</name></author></analytic><series><title level="j">Journal of biotechnology</title><idno type="eISSN">1873-4863</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biotechnology (methods)</term><term>Cell Cycle Proteins (metabolism)</term><term>Cellulase (metabolism)</term><term>Cellulose (metabolism)</term><term>Chromatography, Gel (MeSH)</term><term>Chromosomal Proteins, Non-Histone (metabolism)</term><term>Clostridium (metabolism)</term><term>Nanostructures (chemistry)</term><term>Nanostructures (ultrastructure)</term><term>Plant Proteins (ultrastructure)</term><term>Populus (metabolism)</term><term>Recombinant Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biotechnologie (méthodes)</term><term>Cellulase (métabolisme)</term><term>Cellulose (métabolisme)</term><term>Chromatographie sur gel (MeSH)</term><term>Clostridium (métabolisme)</term><term>Nanostructures (composition chimique)</term><term>Nanostructures (ultrastructure)</term><term>Populus (métabolisme)</term><term>Protéines chromosomiques nonhistones (métabolisme)</term><term>Protéines du cycle cellulaire (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (ultrastructure)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cell Cycle Proteins</term><term>Cellulase</term><term>Cellulose</term><term>Chromosomal Proteins, Non-Histone</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Clostridium</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Biotechnology</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulase</term><term>Cellulose</term><term>Clostridium</term><term>Populus</term><term>Protéines chromosomiques nonhistones</term><term>Protéines du cycle cellulaire</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Biotechnologie</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Nanostructures</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Chromatographie sur gel</term><term>Nanostructures</term><term>Protéines végétales</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein molecular scaffolds are attracting interest as natural candidates for the presentation of enzymes and acceleration of catalytic reactions. We have previously reported evidence that the stable protein 1 (SP1) from Populustremula can be employed as a molecular scaffold for the presentation of either catalytic or structural binding (cellulosomal cohesin) modules. In the present work, we have displayed a potent exoglucanase (Cel6B) from the aerobic cellulolytic bacterium, Thermobifida fusca, on a cohesin-bearing SP1 scaffold. For this purpose, a chimaeric form of the enzyme, fused to a cellulosomal dockerin module, was prepared. Full incorporation of 12 dockerin-bearing exoglucanase molecules onto the cohesin-bearing scaffold was achieved. Cellulase activity was tested on two cellulosic substrates with different levels of crystallinity, and the activity of the scaffold-linked exoglucanase was significantly reduced, compared to the free dockerin-containing enzyme. However, addition of relatively low concentrations of a free wild-type endoglucanase (T. fusca Cel5A) that bears a cellulose-binding module, in combination with the complexed exoglucanase resulted in a marked rise in activity on both cellulosic substrates. The endoglucanase cleaves internal sites of the cellulose chains, and the new chain ends of the substrate were now readily accessible to the scaffold-borne exoglucanase, thereby resulting in highly effective, synergistic degradation of cellulosic substrates.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20438772</PMID><DateCompleted><Year>2010</Year><Month>11</Month><Day>16</Day></DateCompleted><DateRevised><Year>2010</Year><Month>08</Month><Day>05</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4863</ISSN><JournalIssue CitedMedium="Internet"><Volume>147</Volume><Issue>3-4</Issue><PubDate><Year>2010</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Journal of biotechnology</Title><ISOAbbreviation>J Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Enhanced cellulose degradation by nano-complexed enzymes: Synergism between a scaffold-linked exoglucanase and a free endoglucanase.</ArticleTitle><Pagination><MedlinePgn>205-11</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jbiotec.2010.04.012</ELocationID><Abstract><AbstractText>Protein molecular scaffolds are attracting interest as natural candidates for the presentation of enzymes and acceleration of catalytic reactions. We have previously reported evidence that the stable protein 1 (SP1) from Populustremula can be employed as a molecular scaffold for the presentation of either catalytic or structural binding (cellulosomal cohesin) modules. In the present work, we have displayed a potent exoglucanase (Cel6B) from the aerobic cellulolytic bacterium, Thermobifida fusca, on a cohesin-bearing SP1 scaffold. For this purpose, a chimaeric form of the enzyme, fused to a cellulosomal dockerin module, was prepared. Full incorporation of 12 dockerin-bearing exoglucanase molecules onto the cohesin-bearing scaffold was achieved. Cellulase activity was tested on two cellulosic substrates with different levels of crystallinity, and the activity of the scaffold-linked exoglucanase was significantly reduced, compared to the free dockerin-containing enzyme. However, addition of relatively low concentrations of a free wild-type endoglucanase (T. fusca Cel5A) that bears a cellulose-binding module, in combination with the complexed exoglucanase resulted in a marked rise in activity on both cellulosic substrates. The endoglucanase cleaves internal sites of the cellulose chains, and the new chain ends of the substrate were now readily accessible to the scaffold-borne exoglucanase, thereby resulting in highly effective, synergistic degradation of cellulosic substrates.</AbstractText><CopyrightInformation>2010 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moraïs</LastName><ForeName>Sarah</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Heyman</LastName><ForeName>Arnon</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Barak</LastName><ForeName>Yoav</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Caspi</LastName><ForeName>Jonathan</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>David B</ForeName><Initials>DB</Initials></Author><Author ValidYN="Y"><LastName>Lamed</LastName><ForeName>Raphael</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Shoseyov</LastName><ForeName>Oded</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Bayer</LastName><ForeName>Edward A</ForeName><Initials>EA</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>2010</Year><Month>05</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>J Biotechnol</MedlineTA><NlmUniqueID>8411927</NlmUniqueID><ISSNLinking>0168-1656</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002868">Chromosomal Proteins, Non-Histone</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C118077">cohesins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.4</RegistryNumber><NameOfSubstance UI="D002480">Cellulase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001709" MajorTopicYN="N">Biotechnology</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002480" MajorTopicYN="N">Cellulase</DescriptorName><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="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002868" MajorTopicYN="N">Chromosomal Proteins, Non-Histone</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003013" MajorTopicYN="N">Clostridium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D049329" MajorTopicYN="N">Nanostructures</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>01</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2010</Year><Month>04</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2010</Year><Month>04</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>5</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>5</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>11</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20438772</ArticleId><ArticleId IdType="pii">S0168-1656(10)00197-5</ArticleId><ArticleId IdType="doi">10.1016/j.jbiotec.2010.04.012</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Israël</li></country></list><tree><noCountry><name sortKey="Barak, Yoav" sort="Barak, Yoav" uniqKey="Barak Y" first="Yoav" last="Barak">Yoav Barak</name><name sortKey="Bayer, Edward A" sort="Bayer, Edward A" uniqKey="Bayer E" first="Edward A" last="Bayer">Edward A. Bayer</name><name sortKey="Caspi, Jonathan" sort="Caspi, Jonathan" uniqKey="Caspi J" first="Jonathan" last="Caspi">Jonathan Caspi</name><name sortKey="Heyman, Arnon" sort="Heyman, Arnon" uniqKey="Heyman A" first="Arnon" last="Heyman">Arnon Heyman</name><name sortKey="Lamed, Raphael" sort="Lamed, Raphael" uniqKey="Lamed R" first="Raphael" last="Lamed">Raphael Lamed</name><name sortKey="Shoseyov, Oded" sort="Shoseyov, Oded" uniqKey="Shoseyov O" first="Oded" last="Shoseyov">Oded Shoseyov</name><name sortKey="Wilson, David B" sort="Wilson, David B" uniqKey="Wilson D" first="David B" last="Wilson">David B. Wilson</name></noCountry><country name="Israël"><noRegion><name sortKey="Morais, Sarah" sort="Morais, Sarah" uniqKey="Morais S" first="Sarah" last="Moraïs">Sarah Moraïs</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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