Premium
Thermodynamic activity‐based intrinsic enzyme kinetic sheds light on enzyme–solvent interactions
Author(s) -
Grosch JanHendrik,
Wagner David,
Nistelkas Vasilios,
Spieß Antje C.
Publication year - 2016
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.2401
Subject(s) - chemistry , substrate (aquarium) , solvent , alcohol dehydrogenase , kinetics , kinetic energy , thermodynamics , solvent effects , enzyme kinetics , cosmo rs , enzyme , computational chemistry , organic chemistry , active site , catalysis , ecology , physics , ionic liquid , quantum mechanics , biology
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