Publicação: Enzimas termoestáveis: fontes, produção e aplicação industrial
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Data
2007-02-01
Orientador
Coorientador
Pós-graduação
Curso de graduação
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ISSN da Revista
Título de Volume
Editor
Sociedade Brasileira de Química
Tipo
Artigo
Direito de acesso
Acesso aberto
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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Português
Como citar
Química Nova. Sociedade Brasileira de Química, v. 30, n. 1, p. 136-145, 2007.
