enzimas termoestáveis: fontes, produção e aplicação industrial thermostable enzymes: sources, production and industrial applications

Clicks: 108
ID: 229612
2007
Free PDF
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Steady

Ranked #207 of 253 articles by views in greece and rome

Most read Least read

Bar heights use a square-root scale. Only the 120 most-read articles are drawn; the journal has 253 in total.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
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.
Reference Key
gomes2007qumicaenzimas Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Eleni Gomes;Marcelo Andrés Umsza Guez;Natalia Martin;Roberto da Silva
Journal greece and rome
Year 2007
DOI
10.1590/S0100-40422007000100025
URL
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422007000100025
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.