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Combined co-solvent and pressure effect on kinetics of a peptide hydrolysis: an activity-based approach

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Abstract

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.

Graphical abstract: Combined co-solvent and pressure effect on kinetics of a peptide hydrolysis: an activity-based approach

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Publication details

The article was received on 09 Jul 2019, accepted on 26 Sep 2019 and first published on 01 Oct 2019


Article type: Paper
DOI: 10.1039/C9CP03868J
Phys. Chem. Chem. Phys., 2019, Advance Article

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    Combined co-solvent and pressure effect on kinetics of a peptide hydrolysis: an activity-based approach

    M. Knierbein, A. Wangler, T. Q. Luong, R. Winter, C. Held and G. Sadowski, Phys. Chem. Chem. Phys., 2019, Advance Article , DOI: 10.1039/C9CP03868J

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