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: | Química Nova (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422007000100025 |
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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Enzimas termoestáveis: fontes, produção e aplicação industrialthermostable 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.Sociedade Brasileira de Química2007-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422007000100025Química Nova v.30 n.1 2007reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0100-40422007000100025info:eu-repo/semantics/openAccessGomes,EleniGuez,Marcelo Andrés UmszaMartin,NataliaSilva,Roberto dapor2007-02-23T00:00:00Zoai:scielo:S0100-40422007000100025Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2007-02-23T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
title |
Enzimas termoestáveis: fontes, produção e aplicação industrial |
spellingShingle |
Enzimas termoestáveis: fontes, produção e aplicação industrial Gomes,Eleni 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 |
author_facet |
Gomes,Eleni Guez,Marcelo Andrés Umsza Martin,Natalia Silva,Roberto da |
author_role |
author |
author2 |
Guez,Marcelo Andrés Umsza Martin,Natalia Silva,Roberto da |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Gomes,Eleni Guez,Marcelo Andrés Umsza Martin,Natalia Silva,Roberto da |
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 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422007000100025 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422007000100025 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
10.1590/S0100-40422007000100025 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
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 |
Química Nova v.30 n.1 2007 reponame:Química Nova (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Química Nova (Online) |
collection |
Química Nova (Online) |
repository.name.fl_str_mv |
Química Nova (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
quimicanova@sbq.org.br |
_version_ |
1750318105793396736 |