Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/22663

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Campo DCValorIdioma
dc.contributor.authorMatamá, Maria Teresa-
dc.contributor.authorCasal, Margarida-
dc.contributor.authorPaulo, Artur Cavaco-
dc.date.accessioned2013-01-16T14:58:12Z-
dc.date.available2013-01-16T14:58:12Z-
dc.date.issued2013-
dc.identifier.issn1572-882Xpor
dc.identifier.issn0969-0239por
dc.identifier.urihttps://hdl.handle.net/1822/22663-
dc.description.abstractIn this work, the surface of cellulose, either Avicel or cotton fabric, was modified using cutinases without any previous treatment to swell or to solubilise the polymer. Aiming further improvement of cutinase ester synthase activity on cellulose, an engineered cutinase was investigated. Wild-type cutinase from Fusarium solani and its fusion with the carbohydrate-binding module N1 from Cellulomonas fimi were able to esterify the hydroxyl groups of cellulose with distinct efficiencies depending on the acid substrate/solvent system used, as shown by titration and by ATR-FTIR. The carbonyl stretching peak area increased significantly after enzymatic treatment during 72 h at 30 °C. Cutinase treatment resulted in relative increases of 31 and 9 % when octanoic acid and vegetable oil were used as substrates, respectively. Cutinase-N1 treatment resulted in relative increases of 11 and 29 % in the peak area when octanoic acid and vegetable oil were used as substrates, respectively. The production and application of cutinase fused with the domain N1 as a cellulose ester synthase, here reported for the first time, is therefore an interesting strategy to pursuit.por
dc.description.sponsorshipThis work was co-funded by the European Social Fund through the management authority POPH and FCT, Postdoctoral fellowship reference: SFRH/BPD/47555/2008. The authors also want to thank Doctor Raul Machado for his valuable help on FTIR spectral data treatment.por
dc.language.isoengpor
dc.publisherSpringer por
dc.rightsopenAccesspor
dc.subjectCellulose esterpor
dc.subjectReverse esterasepor
dc.subjectTransesterificationpor
dc.subjectCarbohydrate-binding modulepor
dc.subjectCaprylic acidpor
dc.titleDirect enzymatic esterification of cotton and Avicel with wild-type and engineered cutinasespor
dc.typearticlepor
dc.peerreviewedyespor
dc.relation.publisherversionhttp://dx.doi.org/10.1007/s10570-012-9827-9por
sdum.publicationstatuspublishedpor
oaire.citationStartPage409por
oaire.citationEndPage416por
oaire.citationIssue1por
oaire.citationTitleCellulosepor
oaire.citationVolume20por
dc.identifier.doi10.1007/s10570-012-9827-9por
dc.subject.wosScience & Technologypor
sdum.journalCellulosepor
Aparece nas coleções:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series
DET/2C2T - Artigos em revistas internacionais com arbitragem científica

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