Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/28718

Registo completo
Campo DCValorIdioma
dc.contributor.authorGomes, Daniela S.-
dc.contributor.authorMatamá, Maria Teresa-
dc.contributor.authorPaulo, Artur Cavaco-
dc.contributor.authorJordão, R. C. C.-
dc.contributor.authorTakaki, G. M. Campos-
dc.contributor.authorSalgueiro, Alexandra A.-
dc.date.accessioned2014-04-08T13:25:06Z-
dc.date.available2014-04-08T13:25:06Z-
dc.date.issued2013-
dc.identifier.urihttps://hdl.handle.net/1822/28718-
dc.description.abstractCutinases (EC 3.1.1.74)are versatile enzymes that have hydrolytic activity on various esters [1]. The spacial structure and the catalytic site of the enzymes can be protected by chemical additives to promove the stability of the activity [2, 3]. The goal of this work was to improve the stability of a recombinant cutinase produced by Escherichia coli.por
dc.language.isoengpor
dc.rightsopenAccesspor
dc.subjectHeterologous cutinasepor
dc.subjectEnzyme stabilizationpor
dc.titleInteractions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinasepor
dc.typeconferenceAbstractpor
dc.peerreviewednopor
sdum.publicationstatuspublishedpor
oaire.citationConferenceDate02 - 04 Oct. 2013por
sdum.event.typeconferencepor
oaire.citationStartPage681por
oaire.citationEndPage681por
oaire.citationConferencePlaceMadrid, Espanhapor
oaire.citationTitleBioMicroWorld 2013 - V International Conference on Environmental, Industrial and Applied Microbiologypor
Aparece nas coleções:CEB - Resumos em Livros de Atas / Abstracts in Proceedings

Ficheiros deste registo:
Ficheiro Descrição TamanhoFormato 
Pages from BioMicroWorld2013-Book-of-Abstracts-14.pdf101,43 kBAdobe PDFVer/Abrir

Partilhe no FacebookPartilhe no TwitterPartilhe no DeliciousPartilhe no LinkedInPartilhe no DiggAdicionar ao Google BookmarksPartilhe no MySpacePartilhe no Orkut
Exporte no formato BibTex mendeley Exporte no formato Endnote Adicione ao seu ORCID