Thermodynamic activity-based intrinsic enzyme kinetic sheds light on enzyme-solvent interactions.
The reaction medium has major impact on biocatalytic reaction systems and on their economic significance. To allow for tailored medium engineering, thermodynamic phenomena, intrinsic enzyme kinetics, and enzyme-solvent interactions have to be discriminated. To this end, enzyme reaction kinetic modeling was coupled with thermodynamic calculations based on investigations of the alcohol dehydrogenase from Lactobacillus brevis (LbADH) in monophasic water/methyl tert-butyl ether (MTBE) mixtures as a model solvent. Substrate concentrations and substrate thermodynamic activities were varied separately to identify the individual thermodynamic and kinetic effects on the enzyme activity. Microkinetic parameters based on concentration and thermodynamic activity were derived to successfully identify a positive effect of MTBE on the availability of the substrate to the enzyme, but a negative effect on the enzyme performance. In conclusion, thermodynamic activity-based kinetic modeling might be a suitable tool to initially curtail the type of enzyme-solvent interactions and thus, a powerful first step to potentially understand the phenomena that occur in nonconventional media in more detail. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:96-103, 2017.
RWTH Aachen University, AVT - Enzyme Process Technology, Worringer Weg 1, Aachen, 52074, Germany.|Institute of Biochemical Engineering, TU Braunschweig, Rebenring 56, Braunschweig, 38106, Germany.
Jan-Hendrik
JH
Grosch
RWTH Aachen University, AVT - Enzyme Process Technology, Worringer Weg 1, Aachen, 52074, Germany.|DWI-Leibniz-Institute for Interactive Materials, Forckenbeckstraße 50, Aachen, 52074, Germany.
David
D
Wagner
RWTH Aachen University, AVT - Enzyme Process Technology, Worringer Weg 1, Aachen, 52074, Germany.
Vasilios
V
Nistelkas
RWTH Aachen University, AVT - Enzyme Process Technology, Worringer Weg 1, Aachen, 52074, Germany.|Institute of Biochemical Engineering, TU Braunschweig, Rebenring 56, Braunschweig, 38106, Germany.|DWI-Leibniz-Institute for Interactive Materials, Forckenbeckstraße 50, Aachen, 52074, Germany.
Antje C
AC
Spieß
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D055162:Biocatalysis; D007700:Kinetics; D052196:Levilactobacillus brevis / Q000201:enzymology; D008738:Methyl Ethers / Q000737:chemistry; D012997:Solvents / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
D008738:Methyl Ethers; D012997:Solvents; D014867:Water; C043243:methyl tert-butyl ether; D000426:Alcohol Dehydrogenase
COSMO-RS; intrinsic enzyme kinetics; lactobacillus brevis ADH (LbADH); organic solvent; solvation correction