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Updated: Jan 2, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Modulation of enzymatic activity by aqueous two-phase systems and pressure - rivalry between kinetic constants
Rosario Oliva1, Sudeshna Banerjee, Hasan Cinar
1Physical Chemistry I - Biophysical Chemistry, Faculty of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn Strasse 4a, D-44227 Dortmund, Germany. roland.winter@tu-dortmund.de.
Abstract:
We studied the combined effects of an aqueous two-phase system (ATPS) invoking liquid-liquid phase separation and pressure on an enzymatic hydrolysis reaction. We show that simple steric crowding effects are not able to explain the kinetic constants and their pressure dependence in the ATPS. Additional contributions, such as changes in water activity and non-specific weak interactions with ATPS components have to be invoked to explain the results obtained. The findings are relevant for understanding cellular processes of piezophiles and might have significant bearings on biotechnological applications using liquid-liquid phase separation and pressure in concert for modulating enzymatic reactions.
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