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https://hdl.handle.net/1822/28718
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Campo DC | Valor | Idioma |
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dc.contributor.author | Gomes, Daniela S. | - |
dc.contributor.author | Matamá, Maria Teresa | - |
dc.contributor.author | Paulo, Artur Cavaco | - |
dc.contributor.author | Jordão, R. C. C. | - |
dc.contributor.author | Takaki, G. M. Campos | - |
dc.contributor.author | Salgueiro, Alexandra A. | - |
dc.date.accessioned | 2014-04-08T13:25:06Z | - |
dc.date.available | 2014-04-08T13:25:06Z | - |
dc.date.issued | 2013 | - |
dc.identifier.uri | https://hdl.handle.net/1822/28718 | - |
dc.description.abstract | Cutinases (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.iso | eng | por |
dc.rights | openAccess | por |
dc.subject | Heterologous cutinase | por |
dc.subject | Enzyme stabilization | por |
dc.title | Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase | por |
dc.type | conferenceAbstract | por |
dc.peerreviewed | no | por |
sdum.publicationstatus | published | por |
oaire.citationConferenceDate | 02 - 04 Oct. 2013 | por |
sdum.event.type | conference | por |
oaire.citationStartPage | 681 | por |
oaire.citationEndPage | 681 | por |
oaire.citationConferencePlace | Madrid, Espanha | por |
oaire.citationTitle | BioMicroWorld 2013 - V International Conference on Environmental, Industrial and Applied Microbiology | por |
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Ficheiro | Descrição | Tamanho | Formato | |
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Pages from BioMicroWorld2013-Book-of-Abstracts-14.pdf | 101,43 kB | Adobe PDF | Ver/Abrir |