Details
| Original language | English |
|---|---|
| Pages (from-to) | 811-817 |
| Number of pages | 7 |
| Journal | CHEMBIOCHEM |
| Volume | 21 |
| Issue number | 6 |
| Early online date | 12 Oct 2019 |
| Publication status | Published - 16 Mar 2020 |
| Externally published | Yes |
Abstract
The use of oxidoreductases (EC1) in non-conventional reaction media has been increasingly explored. In particular, deep eutectic solvents (DESs) have emerged as a novel class of solvents. Herein, an in-depth study of bioreduction with an alcohol dehydrogenase (ADH) in the DES glyceline is presented. The activity and stability of ADH in mixtures of glyceline/water with varying water contents were measured. Furthermore, the thermodynamic water activity and viscosity of mixtures of glyceline/water have been determined. For a better understanding of the observations, molecular dynamics simulations were performed to quantify the molecular flexibility, hydration layer, and intraprotein hydrogen bonds of ADH. The behavior of the enzyme in DESs follows the classic dependence of water activity (aW) in non-conventional media. At low aW values (<0.2), ADH does not show any activity; at higher aW values, the activity was still lower than that in pure water due to the high viscosities of the DES. These findings could be further explained by increased enzyme flexibility with increasing water content.
Keywords
- alcohol dehydrogenase, deep eutectic solvents, molecular dynamics, solvent effects, thermodynamics
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Medicine
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Chemistry(all)
- Organic Chemistry
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In: CHEMBIOCHEM, Vol. 21, No. 6, 16.03.2020, p. 811-817.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Modeling Alcohol Dehydrogenase Catalysis in Deep Eutectic Solvent/Water Mixtures
AU - Huang, Lei
AU - Bittner, Jan Philipp
AU - Domínguez de María, Pablo
AU - Jakobtorweihen, Sven
AU - Kara, Selin
N1 - Funding Information: We thank Assoc. Prof. Dr. Diederik Johannes Opperman (University of the Free State, South Africa) for the recombinant plasmid containing HLADH gene. Assist. Prof. Kasper R?jkj?r Andersen (Aarhus University, Denmark) is gratefully acknowledged for the use of Tycho NT.6. Assoc. Prof. Menglin Chen (Aarhus University, Denmark) is gratefully thanked for the use of a rheometer. Furthermore, we would also like to thank Kim M?ller Johansen for technical assistance. This work was financially supported by Deutsche Forschungsgemeinschaft (DFG) grant nos. KA 4399/3-1 and JA 2500/5-1; jointly acquired project. Computational resources were provided by The North-German Supercomputing Alliance (HLRN).
PY - 2020/3/16
Y1 - 2020/3/16
N2 - The use of oxidoreductases (EC1) in non-conventional reaction media has been increasingly explored. In particular, deep eutectic solvents (DESs) have emerged as a novel class of solvents. Herein, an in-depth study of bioreduction with an alcohol dehydrogenase (ADH) in the DES glyceline is presented. The activity and stability of ADH in mixtures of glyceline/water with varying water contents were measured. Furthermore, the thermodynamic water activity and viscosity of mixtures of glyceline/water have been determined. For a better understanding of the observations, molecular dynamics simulations were performed to quantify the molecular flexibility, hydration layer, and intraprotein hydrogen bonds of ADH. The behavior of the enzyme in DESs follows the classic dependence of water activity (aW) in non-conventional media. At low aW values (<0.2), ADH does not show any activity; at higher aW values, the activity was still lower than that in pure water due to the high viscosities of the DES. These findings could be further explained by increased enzyme flexibility with increasing water content.
AB - The use of oxidoreductases (EC1) in non-conventional reaction media has been increasingly explored. In particular, deep eutectic solvents (DESs) have emerged as a novel class of solvents. Herein, an in-depth study of bioreduction with an alcohol dehydrogenase (ADH) in the DES glyceline is presented. The activity and stability of ADH in mixtures of glyceline/water with varying water contents were measured. Furthermore, the thermodynamic water activity and viscosity of mixtures of glyceline/water have been determined. For a better understanding of the observations, molecular dynamics simulations were performed to quantify the molecular flexibility, hydration layer, and intraprotein hydrogen bonds of ADH. The behavior of the enzyme in DESs follows the classic dependence of water activity (aW) in non-conventional media. At low aW values (<0.2), ADH does not show any activity; at higher aW values, the activity was still lower than that in pure water due to the high viscosities of the DES. These findings could be further explained by increased enzyme flexibility with increasing water content.
KW - alcohol dehydrogenase
KW - deep eutectic solvents
KW - molecular dynamics
KW - solvent effects
KW - thermodynamics
UR - http://www.scopus.com/inward/record.url?scp=85076553290&partnerID=8YFLogxK
U2 - 10.1002/cbic.201900624
DO - 10.1002/cbic.201900624
M3 - Article
C2 - 31605652
AN - SCOPUS:85076553290
VL - 21
SP - 811
EP - 817
JO - CHEMBIOCHEM
JF - CHEMBIOCHEM
SN - 1439-4227
IS - 6
ER -