ŠTĚPÁNKOVÁ, Veronika, Šárka BIDMANOVÁ, Táňa KOUDELÁKOVÁ, Zbyněk PROKOP, Radka CHALOUPKOVÁ and Jiří DAMBORSKÝ. Strategies for Stabilization and Activation of Biocatalysts in Organic Solvents. ACS Catalysis. 2013, vol. 3, No 12, p. 2823-2836. ISSN 2155-5435. Available from: https://dx.doi.org/10.1021/cs400684x.
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Basic information
Original name Strategies for Stabilization and Activation of Biocatalysts in Organic Solvents
Authors ŠTĚPÁNKOVÁ, Veronika (203 Czech Republic, belonging to the institution), Šárka BIDMANOVÁ (203 Czech Republic, belonging to the institution), Táňa KOUDELÁKOVÁ (203 Czech Republic, belonging to the institution), Zbyněk PROKOP (203 Czech Republic, belonging to the institution), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution).
Edition ACS Catalysis, 2013, 2155-5435.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 7.572
RIV identification code RIV/00216224:14310/13:00067016
Organization unit Faculty of Science
Doi http://dx.doi.org/10.1021/cs400684x
UT WoS 000328231400019
Keywords in English biocatalysis;enzyme stability; organic solvents; chemical modi fi cations; enzyme immobilization; protein engineering
Tags AKR, rivok
Changed by Changed by: Ing. Andrea Mikešková, učo 137293. Changed: 29/4/2014 11:24.
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 can become thermodynamically favourable in organic solution. 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 towards non-conventional 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 semi-rational prediction of stabilizing mutations, knowledge-driven modification of key structural elements learned from successfully engineered proteins or replacement of volatile organic solvents by ionic liquids and deep eutectic solvents.
Links
CZ.1.05/2.1.00/01.0001, interní kód MUName: Centrum pro výzkum toxických látek v prostředí (Acronym: CETOCOEN)
Investor: Ministry of Education, Youth and Sports of the CR, 2.1 Regional R&D Centres
GAP207/12/0775, research and development projectName: Strukturně-funkční vztahy haloalkan dehalogenas
Investor: Czech Science Foundation
GAP503/12/0572, research and development projectName: Konstrukce syntetické metabolické dráhy pro degradaci důležitého environmentálního polutantu proteinovým a metabolickým inženýrstvím
Investor: Czech Science Foundation
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