Combined co-solvent and pressure effect on kinetics of a peptide hydrolysis: an activity-based approach
Autor: | Gabriele Sadowski, Michael Knierbein, Christoph Held, Anton Wangler, Roland Winter, Trung Quan Luong |
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Rok vydání: | 2019 |
Předmět: |
Activity coefficient
Phenylalanine Kinetics General Physics and Astronomy Thermodynamics 02 engineering and technology 010402 general chemistry 01 natural sciences Michaelis–Menten kinetics Enzyme catalysis Catalysis Reaction rate Methylamines Pressure Chymotrypsin Urea Dimethyl Sulfoxide Enzyme kinetics Physical and Theoretical Chemistry Chemistry Hydrolysis Water Substrate (chemistry) 021001 nanoscience & nanotechnology 0104 chemical sciences Solvents 0210 nano-technology |
Zdroj: | Physical Chemistry Chemical Physics. 21:22224-22229 |
ISSN: | 1463-9084 1463-9076 |
DOI: | 10.1039/c9cp03868j |
Popis: | The application of co-solvents and high pressure has been reported to be an efficient means to tune the kinetics of enzyme-catalyzed reactions. Co-solvents and pressure can lead to increased reaction rates without sacrificing enzyme stability, while temperature and pH operation windows are generally very narrow. Quantitative prediction of co-solvent and pressure effects on enzymatic reactions has not been successfully addressed in the literature. Herein, we are introducing a thermodynamic approach that is based on molecular interactions in the form of activity coefficients of substrate and of enzyme in the multi-component solution. This allowed us to quantitatively predict the combined effect of co-solvent and pressure on the kinetic constants, i.e. the Michaelis constant KM and the catalytic constant kcat, of an α-CT-catalyzed peptide hydrolysis reaction. The reaction was studied in the presence of different types of co-solvents and at pressures up to 2 kbar, and quantitative predictions could be obtained for KM, kcat, and finally even primary Michaelis–Menten plots using activity coefficients provided by the thermodynamic model PC-SAFT. |
Databáze: | OpenAIRE |
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