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 -