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Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase

Bibliographic Details
Main Author: Gomes, Daniela S.
Publication Date: 2013
Other Authors: Matamá, Maria Teresa, Paulo, Artur Cavaco, Jordão, R. C. C., Takaki, G. M. Campos, Salgueiro, Alexandra A.
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/1822/28718
Summary: 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.
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spelling Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinaseHeterologous cutinaseEnzyme stabilizationCutinases (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.Universidade do MinhoGomes, Daniela S.Matamá, Maria TeresaPaulo, Artur CavacoJordão, R. C. C.Takaki, G. M. CamposSalgueiro, Alexandra A.20132013-01-01T00:00:00Zconference objectinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/1822/28718enginfo:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-11T07:15:49Zoai:repositorium.sdum.uminho.pt:1822/28718Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T16:20:58.617704Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
title Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
spellingShingle Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
Gomes, Daniela S.
Heterologous cutinase
Enzyme stabilization
title_short Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
title_full Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
title_fullStr Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
title_full_unstemmed Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
title_sort Interactions between glycerol, PEG-200 and (NH4)2 SO4 in the stability of heterologous cutinase
author Gomes, Daniela S.
author_facet Gomes, Daniela S.
Matamá, Maria Teresa
Paulo, Artur Cavaco
Jordão, R. C. C.
Takaki, G. M. Campos
Salgueiro, Alexandra A.
author_role author
author2 Matamá, Maria Teresa
Paulo, Artur Cavaco
Jordão, R. C. C.
Takaki, G. M. Campos
Salgueiro, Alexandra A.
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Gomes, Daniela S.
Matamá, Maria Teresa
Paulo, Artur Cavaco
Jordão, R. C. C.
Takaki, G. M. Campos
Salgueiro, Alexandra A.
dc.subject.por.fl_str_mv Heterologous cutinase
Enzyme stabilization
topic Heterologous cutinase
Enzyme stabilization
description 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.
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-01-01T00:00:00Z
dc.type.driver.fl_str_mv conference object
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/28718
url http://hdl.handle.net/1822/28718
dc.language.iso.fl_str_mv eng
language eng
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
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reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
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