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Cited by 659

The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.

Strategies for Stabilization of Enzymes in Organic Solvents

Stepankova, Veronika, Bidmanova, Sarka, Koudelakova, Tana, Prokop, Zbynek, Chaloupkova, Radka, Damborsky, Jiri·2013·ACS Catalysis
DOI 10.1021/cs400684x
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Abstract

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, such as 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 enzymes. Here we discuss successful examples representing each of these categories and summarize their advantages and disadvantages. Finally, we highlight some potential future research directions in the field, such as investigation of novel nanomaterials for immobilization, wider application of computational tools for semirational prediction of stabilizing mutations, knowledge-driven modification of key structural elements learned from successfully engineered proteins, and replacement of volatile organic solvents by ionic liquids and deep eutectic solvents.

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Metadata

Authors
Stepankova, V., Bidmanova, S., Koudelakova, T., Prokop, Z., Chaloupkova, R., & Damborsky, J.
Venue
ACS Catalysis
Publisher
American Chemical Society (ACS)
Published
2013-11-05
Volume
3
Issue
12
Pages
2823-2836
ISSN
2155-5435 (ISSN-L)
DOI
10.1021/cs400684x
OpenAlex
W2157599742
Cited by
659
References
91
FWCI
16.94
Type
journal article
Language
en
Open access
closed

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