Enzimas termoestáveis: fontes, produção e aplicação industrial
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1590/S0100-40422007000100025 http://hdl.handle.net/11449/21440 |
Resumo: | REVIEW: Living organisms encountered in hostile environments that are characterized by extreme temperatures rely on novel molecular mechanisms to enhance the thermal stability of their proteins, nucleic acids, lipids and cell membranes. Proteins isolated from thermophilic organisms usually exhibit higher intrinsic thermal stabilities than their counterparts isolated from mesophilic organisms. Although the molecular basis of protein thermostability is only partially understood, structural studies have suggested that the factors that may contribute to enhance protein thermostability mainly include hydrophobic packing, enhanced secondary structure propensity, helix dipole stabilization, absence of residues sensitive to oxidation or deamination, and increased electrostatic interactions. Thermostable enzymes such as amylases, xylanases and pectinases isolated from thermophilic organisms are potentially of interest in the optimization of industrial processes due to their enhanced stability. In the present review, an attempt is made to delineate the structural factors that increase enzyme thermostability and to document the research results in the production of these enzymes. |
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Repositório Institucional da UNESP |
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Enzimas termoestáveis: fontes, produção e aplicação industrialThermostable enzymes: sources, production and industrial applicationsThermostable enzymethermophilic microorganismthermal adaptationREVIEW: Living organisms encountered in hostile environments that are characterized by extreme temperatures rely on novel molecular mechanisms to enhance the thermal stability of their proteins, nucleic acids, lipids and cell membranes. Proteins isolated from thermophilic organisms usually exhibit higher intrinsic thermal stabilities than their counterparts isolated from mesophilic organisms. Although the molecular basis of protein thermostability is only partially understood, structural studies have suggested that the factors that may contribute to enhance protein thermostability mainly include hydrophobic packing, enhanced secondary structure propensity, helix dipole stabilization, absence of residues sensitive to oxidation or deamination, and increased electrostatic interactions. Thermostable enzymes such as amylases, xylanases and pectinases isolated from thermophilic organisms are potentially of interest in the optimization of industrial processes due to their enhanced stability. In the present review, an attempt is made to delineate the structural factors that increase enzyme thermostability and to document the research results in the production of these enzymes.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Universidade Estadual Paulista Instituto de Biociências, Letras e Ciências ExatasUniversidade Estadual Paulista Instituto de Biociências, Letras e Ciências ExatasSociedade Brasileira de QuímicaUniversidade Estadual Paulista (Unesp)Gomes, Eleni [UNESP]Guez, Marcelo Andrés Umsza [UNESP]Martin, Natalia [UNESP]Silva, Roberto da [UNESP]2014-05-20T14:00:39Z2014-05-20T14:00:39Z2007-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article136-145application/pdfhttp://dx.doi.org/10.1590/S0100-40422007000100025Química Nova. Sociedade Brasileira de Química, v. 30, n. 1, p. 136-145, 2007.0100-4042http://hdl.handle.net/11449/2144010.1590/S0100-40422007000100025S0100-40422007000100025S0100-40422007000100025.pdf70912417428519209424175688206545SciELOreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPporQuímica Nova0.6460,255info:eu-repo/semantics/openAccess2023-12-08T06:18:28Zoai:repositorio.unesp.br:11449/21440Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T19:45:33.683144Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Enzimas termoestáveis: fontes, produção e aplicação industrial Thermostable enzymes: sources, production and industrial applications |
title |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
spellingShingle |
Enzimas termoestáveis: fontes, produção e aplicação industrial Gomes, Eleni [UNESP] Thermostable enzyme thermophilic microorganism thermal adaptation |
title_short |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
title_full |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
title_fullStr |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
title_full_unstemmed |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
title_sort |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
author |
Gomes, Eleni [UNESP] |
author_facet |
Gomes, Eleni [UNESP] Guez, Marcelo Andrés Umsza [UNESP] Martin, Natalia [UNESP] Silva, Roberto da [UNESP] |
author_role |
author |
author2 |
Guez, Marcelo Andrés Umsza [UNESP] Martin, Natalia [UNESP] Silva, Roberto da [UNESP] |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Gomes, Eleni [UNESP] Guez, Marcelo Andrés Umsza [UNESP] Martin, Natalia [UNESP] Silva, Roberto da [UNESP] |
dc.subject.por.fl_str_mv |
Thermostable enzyme thermophilic microorganism thermal adaptation |
topic |
Thermostable enzyme thermophilic microorganism thermal adaptation |
description |
REVIEW: Living organisms encountered in hostile environments that are characterized by extreme temperatures rely on novel molecular mechanisms to enhance the thermal stability of their proteins, nucleic acids, lipids and cell membranes. Proteins isolated from thermophilic organisms usually exhibit higher intrinsic thermal stabilities than their counterparts isolated from mesophilic organisms. Although the molecular basis of protein thermostability is only partially understood, structural studies have suggested that the factors that may contribute to enhance protein thermostability mainly include hydrophobic packing, enhanced secondary structure propensity, helix dipole stabilization, absence of residues sensitive to oxidation or deamination, and increased electrostatic interactions. Thermostable enzymes such as amylases, xylanases and pectinases isolated from thermophilic organisms are potentially of interest in the optimization of industrial processes due to their enhanced stability. In the present review, an attempt is made to delineate the structural factors that increase enzyme thermostability and to document the research results in the production of these enzymes. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-02-01 2014-05-20T14:00:39Z 2014-05-20T14:00:39Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1590/S0100-40422007000100025 Química Nova. Sociedade Brasileira de Química, v. 30, n. 1, p. 136-145, 2007. 0100-4042 http://hdl.handle.net/11449/21440 10.1590/S0100-40422007000100025 S0100-40422007000100025 S0100-40422007000100025.pdf 7091241742851920 9424175688206545 |
url |
http://dx.doi.org/10.1590/S0100-40422007000100025 http://hdl.handle.net/11449/21440 |
identifier_str_mv |
Química Nova. Sociedade Brasileira de Química, v. 30, n. 1, p. 136-145, 2007. 0100-4042 10.1590/S0100-40422007000100025 S0100-40422007000100025 S0100-40422007000100025.pdf 7091241742851920 9424175688206545 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
Química Nova 0.646 0,255 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
136-145 application/pdf |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
SciELO reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129114382532608 |