Strategies for Stabilization of Enzymes in Organic Solvents
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F13%3A00063739" target="_blank" >RIV/00159816:_____/13:00063739 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/cs400684x" target="_blank" >http://dx.doi.org/10.1021/cs400684x</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/cs400684x" target="_blank" >10.1021/cs400684x</a>
Alternative languages
Result language
angličtina
Original language name
Strategies for Stabilization of Enzymes in Organic Solvents
Original language description
One of the major barriers to the use of enzymes in industrial biotechnology is their insufficient stability under processing conditions. The use of organic solvent systems instead of aqueous media for enzymatic reactions offers numerous advantages, suchas increased solubility of hydrophobic substrates or suppression of water-dependent side reactions. For example, reverse hydrolysis reactions that form esters from acids and alcohols become thermodynamically favorable. However, organic solvents often inactivate enzymes. Industry and academia have devoted considerable effort into developing effective strategies to enhance the lifetime of enzymes in the presence of organic solvents. The strategies can be grouped into three main categories: (i) isolation of novel enzymes functioning under extreme conditions, (ii) modification of enzyme structures to increase their resistance toward nonconventional media, and (iii) modification of the solvent environment to decrease its denaturing effect on
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/ED1.100%2F02%2F0123" target="_blank" >ED1.100/02/0123: St. Anne´s University Hospital Brno - International Clinical Research Center (FNUSA-ICRC)</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2013
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACS Catalysis
ISSN
2155-5435
e-ISSN
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Volume of the periodical
3
Issue of the periodical within the volume
12
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
2823-2836
UT code for WoS article
000328231400019
EID of the result in the Scopus database
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