Modification of cellulose fiber surfaces by use of a lipase and a xyloglucan endotransglycosylase.
Identifieur interne : 003F01 ( Main/Exploration ); précédent : 003F00; suivant : 003F02Modification of cellulose fiber surfaces by use of a lipase and a xyloglucan endotransglycosylase.
Auteurs : Malin T. Gustavsson [Suède] ; Per V. Persson ; Tommy Iversen ; Mats Martinelle ; Karl Hult ; Tuula T. Teeri ; Harry BrumerSource :
- Biomacromolecules [ 1525-7797 ]
Descripteurs français
- KwdFr :
- Acylation (MeSH), Arbres (enzymologie), Candida (enzymologie), Cellulose (composition chimique), Cellulose (synthèse chimique), Conformation des glucides (MeSH), Données de séquences moléculaires (MeSH), Glucanes (composition chimique), Glycosyltransferase (composition chimique), Oligosaccharides (composition chimique), Propriétés de surface (MeSH), Protéines fongiques (MeSH), Séquence glucidique (MeSH), Triacylglycerol lipase (biosynthèse), Triacylglycerol lipase (composition chimique), Xylanes (composition chimique).
- MESH :
- biosynthèse : Triacylglycerol lipase.
- composition chimique : Cellulose, Glucanes, Glycosyltransferase, Oligosaccharides, Triacylglycerol lipase, Xylanes.
- enzymologie : Arbres, Candida.
- synthèse chimique : Cellulose.
- Acylation, Conformation des glucides, Données de séquences moléculaires, Propriétés de surface, Protéines fongiques, Séquence glucidique.
English descriptors
- KwdEn :
- Acylation (MeSH), Candida (enzymology), Carbohydrate Conformation (MeSH), Carbohydrate Sequence (MeSH), Cellulose (chemical synthesis), Cellulose (chemistry), Fungal Proteins (MeSH), Glucans (chemistry), Glycosyltransferases (chemistry), Lipase (biosynthesis), Lipase (chemistry), Molecular Sequence Data (MeSH), Oligosaccharides (chemistry), Surface Properties (MeSH), Trees (enzymology), Xylans (chemistry).
- MESH :
- chemical , biosynthesis : Lipase.
- chemical , chemical synthesis : Cellulose.
- chemical , chemistry : Cellulose, Glucans, Glycosyltransferases, Lipase, Oligosaccharides, Xylans.
- enzymology : Candida, Trees.
- Acylation, Carbohydrate Conformation, Carbohydrate Sequence, Fungal Proteins, Molecular Sequence Data, Surface Properties.
Abstract
A strategy for the modification of cellulose fiber surfaces was developed that used the ability of Candida antarctica lipase B (CALB) to acylate carbohydrates with high regioselectivity, combined with the transglycosylating activity of the Populus tremula x P. tremuloides xyloglucan endotransglycosylase 16A (PttXET16A). Xyloglucan oligosaccharides (XGOs) prepared from tamarind xyloglucan were acylated with CALB as a catalyst and vinyl stearate or gamma-thiobutyrolactone as acyl donors to produce carbohydrate molecules with hydrophobic alkyl chains or reactive sulfhydryl groups, respectively. The modified XGOs were shown to act as glycosyl acceptors in the transglycosylation reaction catalyzed by PttXET16A and could therefore be incorporated into high M(r) xyloglucan chains. The resulting xyloglucan molecules exhibited a high affinity for cellulose surfaces, which enabled the essentially irreversible introduction of fatty acid esters or thiol groups to cellulose fibers.
DOI: 10.1021/bm049588i
PubMed: 15638521
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Persson</name></author><author><name sortKey="Iversen, Tommy" sort="Iversen, Tommy" uniqKey="Iversen T" first="Tommy" last="Iversen">Tommy Iversen</name></author><author><name sortKey="Martinelle, Mats" sort="Martinelle, Mats" uniqKey="Martinelle M" first="Mats" last="Martinelle">Mats Martinelle</name></author><author><name sortKey="Hult, Karl" sort="Hult, Karl" uniqKey="Hult K" first="Karl" last="Hult">Karl Hult</name></author><author><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. 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Gustavsson</name><affiliation wicri:level="1"><nlm:affiliation>Royal Institute of Technology, Department of Biotechnology, AlbaNova University Centre, SE-106 91 Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Royal Institute of Technology, Department of Biotechnology, AlbaNova University Centre, SE-106 91 Stockholm</wicri:regionArea><wicri:noRegion>SE-106 91 Stockholm</wicri:noRegion></affiliation></author><author><name sortKey="Persson, Per V" sort="Persson, Per V" uniqKey="Persson P" first="Per V" last="Persson">Per V. Persson</name></author><author><name sortKey="Iversen, Tommy" sort="Iversen, Tommy" uniqKey="Iversen T" first="Tommy" last="Iversen">Tommy Iversen</name></author><author><name sortKey="Martinelle, Mats" sort="Martinelle, Mats" uniqKey="Martinelle M" first="Mats" last="Martinelle">Mats Martinelle</name></author><author><name sortKey="Hult, Karl" sort="Hult, Karl" uniqKey="Hult K" first="Karl" last="Hult">Karl Hult</name></author><author><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></author><author><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name></author></analytic><series><title level="j">Biomacromolecules</title><idno type="ISSN">1525-7797</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acylation (MeSH)</term><term>Candida (enzymology)</term><term>Carbohydrate Conformation (MeSH)</term><term>Carbohydrate Sequence (MeSH)</term><term>Cellulose (chemical synthesis)</term><term>Cellulose (chemistry)</term><term>Fungal Proteins (MeSH)</term><term>Glucans (chemistry)</term><term>Glycosyltransferases (chemistry)</term><term>Lipase (biosynthesis)</term><term>Lipase (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Oligosaccharides (chemistry)</term><term>Surface Properties (MeSH)</term><term>Trees (enzymology)</term><term>Xylans (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acylation (MeSH)</term><term>Arbres (enzymologie)</term><term>Candida (enzymologie)</term><term>Cellulose (composition chimique)</term><term>Cellulose (synthèse chimique)</term><term>Conformation des glucides (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glucanes (composition chimique)</term><term>Glycosyltransferase (composition chimique)</term><term>Oligosaccharides (composition chimique)</term><term>Propriétés de surface (MeSH)</term><term>Protéines fongiques (MeSH)</term><term>Séquence glucidique (MeSH)</term><term>Triacylglycerol lipase (biosynthèse)</term><term>Triacylglycerol lipase (composition chimique)</term><term>Xylanes (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Lipase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Cellulose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cellulose</term><term>Glucans</term><term>Glycosyltransferases</term><term>Lipase</term><term>Oligosaccharides</term><term>Xylans</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Triacylglycerol lipase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulose</term><term>Glucanes</term><term>Glycosyltransferase</term><term>Oligosaccharides</term><term>Triacylglycerol lipase</term><term>Xylanes</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arbres</term><term>Candida</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Candida</term><term>Trees</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Cellulose</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Acylation</term><term>Carbohydrate Conformation</term><term>Carbohydrate Sequence</term><term>Fungal Proteins</term><term>Molecular Sequence Data</term><term>Surface Properties</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acylation</term><term>Conformation des glucides</term><term>Données de séquences moléculaires</term><term>Propriétés de surface</term><term>Protéines fongiques</term><term>Séquence glucidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A strategy for the modification of cellulose fiber surfaces was developed that used the ability of Candida antarctica lipase B (CALB) to acylate carbohydrates with high regioselectivity, combined with the transglycosylating activity of the Populus tremula x P. tremuloides xyloglucan endotransglycosylase 16A (PttXET16A). Xyloglucan oligosaccharides (XGOs) prepared from tamarind xyloglucan were acylated with CALB as a catalyst and vinyl stearate or gamma-thiobutyrolactone as acyl donors to produce carbohydrate molecules with hydrophobic alkyl chains or reactive sulfhydryl groups, respectively. The modified XGOs were shown to act as glycosyl acceptors in the transglycosylation reaction catalyzed by PttXET16A and could therefore be incorporated into high M(r) xyloglucan chains. The resulting xyloglucan molecules exhibited a high affinity for cellulose surfaces, which enabled the essentially irreversible introduction of fatty acid esters or thiol groups to cellulose fibers.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15638521</PMID><DateCompleted><Year>2005</Year><Month>06</Month><Day>02</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1525-7797</ISSN><JournalIssue CitedMedium="Print"><Volume>6</Volume><Issue>1</Issue><PubDate><MedlineDate>2005 Jan-Feb</MedlineDate></PubDate></JournalIssue><Title>Biomacromolecules</Title><ISOAbbreviation>Biomacromolecules</ISOAbbreviation></Journal><ArticleTitle>Modification of cellulose fiber surfaces by use of a lipase and a xyloglucan endotransglycosylase.</ArticleTitle><Pagination><MedlinePgn>196-203</MedlinePgn></Pagination><Abstract><AbstractText>A strategy for the modification of cellulose fiber surfaces was developed that used the ability of Candida antarctica lipase B (CALB) to acylate carbohydrates with high regioselectivity, combined with the transglycosylating activity of the Populus tremula x P. tremuloides xyloglucan endotransglycosylase 16A (PttXET16A). Xyloglucan oligosaccharides (XGOs) prepared from tamarind xyloglucan were acylated with CALB as a catalyst and vinyl stearate or gamma-thiobutyrolactone as acyl donors to produce carbohydrate molecules with hydrophobic alkyl chains or reactive sulfhydryl groups, respectively. The modified XGOs were shown to act as glycosyl acceptors in the transglycosylation reaction catalyzed by PttXET16A and could therefore be incorporated into high M(r) xyloglucan chains. The resulting xyloglucan molecules exhibited a high affinity for cellulose surfaces, which enabled the essentially irreversible introduction of fatty acid esters or thiol groups to cellulose fibers.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gustavsson</LastName><ForeName>Malin T</ForeName><Initials>MT</Initials><AffiliationInfo><Affiliation>Royal Institute of Technology, Department of Biotechnology, AlbaNova University Centre, SE-106 91 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Persson</LastName><ForeName>Per V</ForeName><Initials>PV</Initials></Author><Author ValidYN="Y"><LastName>Iversen</LastName><ForeName>Tommy</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Martinelle</LastName><ForeName>Mats</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Hult</LastName><ForeName>Karl</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Teeri</LastName><ForeName>Tuula T</ForeName><Initials>TT</Initials></Author><Author ValidYN="Y"><LastName>Brumer</LastName><ForeName>Harry</ForeName><Initials>H</Initials><Suffix>3rd</Suffix></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biomacromolecules</MedlineTA><NlmUniqueID>100892849</NlmUniqueID><ISSNLinking>1525-7797</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005936">Glucans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014990">Xylans</NameOfSubstance></Chemical><Chemical><RegistryNumber>37294-28-3</RegistryNumber><NameOfSubstance UI="C029353">xyloglucan</NameOfSubstance></Chemical><Chemical><RegistryNumber>9004-34-6</RegistryNumber><NameOfSubstance UI="D002482">Cellulose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.-</RegistryNumber><NameOfSubstance UI="D016695">Glycosyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.4.1.-</RegistryNumber><NameOfSubstance UI="C073693">xyloglucan endotransglycosylase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.3</RegistryNumber><NameOfSubstance UI="D008049">Lipase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.3</RegistryNumber><NameOfSubstance UI="C431349">lipase B, Candida antarctica</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000215" MajorTopicYN="N">Acylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002175" MajorTopicYN="N">Candida</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002236" MajorTopicYN="N">Carbohydrate Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002240" MajorTopicYN="N">Carbohydrate Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002482" MajorTopicYN="Y">Cellulose</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005936" MajorTopicYN="N">Glucans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016695" MajorTopicYN="N">Glycosyltransferases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008049" MajorTopicYN="N">Lipase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009844" MajorTopicYN="N">Oligosaccharides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014197" MajorTopicYN="N">Trees</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014990" MajorTopicYN="N">Xylans</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>1</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>6</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>1</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15638521</ArticleId><ArticleId IdType="doi">10.1021/bm049588i</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Brumer, Harry" sort="Brumer, Harry" uniqKey="Brumer H" first="Harry" last="Brumer">Harry Brumer</name><name sortKey="Hult, Karl" sort="Hult, Karl" uniqKey="Hult K" first="Karl" last="Hult">Karl Hult</name><name sortKey="Iversen, Tommy" sort="Iversen, Tommy" uniqKey="Iversen T" first="Tommy" last="Iversen">Tommy Iversen</name><name sortKey="Martinelle, Mats" sort="Martinelle, Mats" uniqKey="Martinelle M" first="Mats" last="Martinelle">Mats Martinelle</name><name sortKey="Persson, Per V" sort="Persson, Per V" uniqKey="Persson P" first="Per V" last="Persson">Per V. Persson</name><name sortKey="Teeri, Tuula T" sort="Teeri, Tuula T" uniqKey="Teeri T" first="Tuula T" last="Teeri">Tuula T. Teeri</name></noCountry><country name="Suède"><noRegion><name sortKey="Gustavsson, Malin T" sort="Gustavsson, Malin T" uniqKey="Gustavsson M" first="Malin T" last="Gustavsson">Malin T. Gustavsson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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