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Updated: Sep 28, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Operational stability of high initial activity protease catalysts in organic solvents
João F Amorim Fernandes1, Peter J Halling
1Department of Pure and Applied Chemistry, University of Strathclyde, Glasgow G1 1XW, Scotland, UK.
Abstract:
The first studies on the operational stability of cross-linked enzyme crystals (CLECs) in organic media are described. Although these catalysts display high initial specific activity, they inactivate rapidly, losing more than 50% of the initial activity within the first 4 h under continuous flow. Furthermore, the inactivation is not reversible when returned to an aqueous medium. The same rapid inactivation occurs with adsorbed protease preparations that show similar high initial specific activity (propanol-rinsed enzyme preparations (PREPs) of subtilisin and alpha-chymotrypsin).
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