Production of hyperthermostable GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants enables complete hydrolysis of methylglucuronoxylan to fermentable sugars for biofuel production.
Identifieur interne : 002D49 ( Main/Exploration ); précédent : 002D48; suivant : 002D50Production of hyperthermostable GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants enables complete hydrolysis of methylglucuronoxylan to fermentable sugars for biofuel production.
Auteurs : Jae Yoon Kim [États-Unis] ; Musa Kavas ; Walid M. Fouad ; Guang Nong ; James F. Preston ; Fredy AltpeterSource :
- Plant molecular biology [ 1573-5028 ] ; 2011.
Descripteurs français
- KwdFr :
- Amorces ADN (MeSH), Biocarburants (MeSH), Fermentation (MeSH), Glucuronates (métabolisme), Hydrolyse (MeSH), Métabolisme glucidique (MeSH), Plantes (enzymologie), Plantes (métabolisme), Réaction de polymérisation en chaîne (MeSH), Stabilité enzymatique (MeSH), Technique de Southern (MeSH), Technique de Western (MeSH), Thermotoga maritima (génétique), Xylanes (métabolisme), Xylosidases (biosynthèse), Xylosidases (génétique), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- biosynthèse : Xylosidases.
- enzymologie : Plantes.
- génétique : Thermotoga maritima, Xylosidases.
- métabolisme : Glucuronates, Plantes, Xylanes.
- Amorces ADN, Biocarburants, Fermentation, Hydrolyse, Métabolisme glucidique, Réaction de polymérisation en chaîne, Stabilité enzymatique, Technique de Southern, Technique de Western, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Biofuels (MeSH), Blotting, Southern (MeSH), Blotting, Western (MeSH), Carbohydrate Metabolism (MeSH), DNA Primers (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Enzyme Stability (MeSH), Fermentation (MeSH), Glucuronates (metabolism), Hydrolysis (MeSH), Plants (enzymology), Plants (metabolism), Polymerase Chain Reaction (MeSH), Thermotoga maritima (genetics), Xylans (metabolism), Xylosidases (biosynthesis), Xylosidases (genetics).
- MESH :
- chemical , biosynthesis : Xylosidases.
- chemical , genetics : Xylosidases.
- chemical , metabolism : Glucuronates, Xylans.
- chemical : Biofuels, DNA Primers.
- enzymology : Plants.
- genetics : Thermotoga maritima.
- metabolism : Plants.
- Blotting, Southern, Blotting, Western, Carbohydrate Metabolism, Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Fermentation, Hydrolysis, Polymerase Chain Reaction.
Abstract
Overcoming the recalcitrance in lignocellulosic biomass for efficient hydrolysis of the polysaccharides cellulose and hemicellulose to fermentable sugars is a research priority for the transition from a fossilfuel-based economy to a renewable carbohydrate economy. Methylglucuronoxylans (MeGXn) are the major components of hemicellulose in woody biofuel crops. Here, we describe efficient production of the GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants and demonstrate exceptional stability and catalytic activities of the in planta produced enzyme. Fully expanded leaves from homotransplastomic plants contained enzymatically active Xyl10B at a level of 11-15% of their total soluble protein. Transplastomic plants and their seed progeny were morphologically indistinguishable from non-transgenic plants. Catalytic activity of in planta produced Xyl10B was detected with poplar, sweetgum and birchwood xylan substrates following incubation between 40 and 90 °C and was also stable in dry and stored leaves. Optimal yields of Xyl10B were obtained from dry leaves if crude protein extraction was performed at 85 °C. The transplastomic plant derived Xyl10B showed exceptional catalytic activity and enabled the complete hydrolysis of MeGXn to fermentable sugars with the help of a single accessory enzyme (α-glucuronidase) as revealed by the sugar release assay. Even without this accessory enzyme, the majority of MeGXn was hydrolyzed by the transplastomic plant-derived Xyl10B to fermentable xylose and xylobiose.
DOI: 10.1007/s11103-010-9712-6
PubMed: 21080212
Affiliations:
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Methylglucuronoxylans (MeGXn) are the major components of hemicellulose in woody biofuel crops. Here, we describe efficient production of the GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants and demonstrate exceptional stability and catalytic activities of the in planta produced enzyme. Fully expanded leaves from homotransplastomic plants contained enzymatically active Xyl10B at a level of 11-15% of their total soluble protein. Transplastomic plants and their seed progeny were morphologically indistinguishable from non-transgenic plants. Catalytic activity of in planta produced Xyl10B was detected with poplar, sweetgum and birchwood xylan substrates following incubation between 40 and 90 °C and was also stable in dry and stored leaves. Optimal yields of Xyl10B were obtained from dry leaves if crude protein extraction was performed at 85 °C. The transplastomic plant derived Xyl10B showed exceptional catalytic activity and enabled the complete hydrolysis of MeGXn to fermentable sugars with the help of a single accessory enzyme (α-glucuronidase) as revealed by the sugar release assay. Even without this accessory enzyme, the majority of MeGXn was hydrolyzed by the transplastomic plant-derived Xyl10B to fermentable xylose and xylobiose.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21080212</PMID><DateCompleted><Year>2011</Year><Month>08</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-5028</ISSN><JournalIssue CitedMedium="Internet"><Volume>76</Volume><Issue>3-5</Issue><PubDate><Year>2011</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Plant molecular biology</Title><ISOAbbreviation>Plant Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Production of hyperthermostable GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants enables complete hydrolysis of methylglucuronoxylan to fermentable sugars for biofuel production.</ArticleTitle><Pagination><MedlinePgn>357-69</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11103-010-9712-6</ELocationID><Abstract><AbstractText>Overcoming the recalcitrance in lignocellulosic biomass for efficient hydrolysis of the polysaccharides cellulose and hemicellulose to fermentable sugars is a research priority for the transition from a fossilfuel-based economy to a renewable carbohydrate economy. Methylglucuronoxylans (MeGXn) are the major components of hemicellulose in woody biofuel crops. Here, we describe efficient production of the GH10 xylanase Xyl10B from Thermotoga maritima in transplastomic plants and demonstrate exceptional stability and catalytic activities of the in planta produced enzyme. Fully expanded leaves from homotransplastomic plants contained enzymatically active Xyl10B at a level of 11-15% of their total soluble protein. Transplastomic plants and their seed progeny were morphologically indistinguishable from non-transgenic plants. Catalytic activity of in planta produced Xyl10B was detected with poplar, sweetgum and birchwood xylan substrates following incubation between 40 and 90 °C and was also stable in dry and stored leaves. Optimal yields of Xyl10B were obtained from dry leaves if crude protein extraction was performed at 85 °C. The transplastomic plant derived Xyl10B showed exceptional catalytic activity and enabled the complete hydrolysis of MeGXn to fermentable sugars with the help of a single accessory enzyme (α-glucuronidase) as revealed by the sugar release assay. Even without this accessory enzyme, the majority of MeGXn was hydrolyzed by the transplastomic plant-derived Xyl10B to fermentable xylose and xylobiose.</AbstractText><CopyrightInformation>© Springer Science+Business Media B.V. 2010</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Jae Yoon</ForeName><Initials>JY</Initials><AffiliationInfo><Affiliation>Agronomy Department, Plant Molecular and Cellular Biology Program, Genetics Institute, University of Florida-IFAS, Gainesville, FL, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kavas</LastName><ForeName>Musa</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Fouad</LastName><ForeName>Walid M</ForeName><Initials>WM</Initials></Author><Author ValidYN="Y"><LastName>Nong</LastName><ForeName>Guang</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Preston</LastName><ForeName>James F</ForeName><Initials>JF</Initials></Author><Author ValidYN="Y"><LastName>Altpeter</LastName><ForeName>Fredy</ForeName><Initials>F</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>11</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Plant Mol Biol</MedlineTA><NlmUniqueID>9106343</NlmUniqueID><ISSNLinking>0167-4412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D056804">Biofuels</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005965">Glucuronates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.-</RegistryNumber><NameOfSubstance UI="D014995">Xylosidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D056804" MajorTopicYN="Y">Biofuels</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015139" MajorTopicYN="N">Blotting, Southern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050260" MajorTopicYN="Y">Carbohydrate Metabolism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005285" MajorTopicYN="N">Fermentation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005965" MajorTopicYN="N">Glucuronates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020124" MajorTopicYN="N">Thermotoga maritima</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014995" MajorTopicYN="N">Xylosidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>07</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2010</Year><Month>10</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>11</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>11</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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Fouad</name><name sortKey="Kavas, Musa" sort="Kavas, Musa" uniqKey="Kavas M" first="Musa" last="Kavas">Musa Kavas</name><name sortKey="Nong, Guang" sort="Nong, Guang" uniqKey="Nong G" first="Guang" last="Nong">Guang Nong</name><name sortKey="Preston, James F" sort="Preston, James F" uniqKey="Preston J" first="James F" last="Preston">James F. Preston</name></noCountry><country name="États-Unis"><region name="Floride"><name sortKey="Kim, Jae Yoon" sort="Kim, Jae Yoon" uniqKey="Kim J" first="Jae Yoon" last="Kim">Jae Yoon Kim</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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