Picture of Open Access badges

Discover Open Access research at Strathprints

It's International Open Access Week, 24-30 October 2016. This year's theme is "Open in Action" and is all about taking meaningful steps towards opening up research and scholarship. The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. Explore recent world leading Open Access research content by University of Strathclyde researchers and see how Strathclyde researchers are committing to putting "Open in Action".


Image: h_pampel, CC-BY

Control of acid-base conditions in low-water media

Partridge, J. and Harper, N. and Moore, B.D. and Halling, P.J. (2001) Control of acid-base conditions in low-water media. In: Methods in Biotechnology: Enzymes in Nonaqueous Solvents. Methods in Biotechnology (15). Humana Press, NJ, USA, pp. 227-234. ISBN 0896039293

[img] HTML (strathprints000278.htm)

Download (21kB)


The catalytic activity of an enzyme is profoundly affected by its ionisation state, whether it is dissolved in aqueous solution or suspended in low water organic media. In aqueous solution, counter ions can freely move around in solution. Since they are not closely associated with opposite charges, their identity does not effect the protonation state of the enzyme and so pH alone governs the protonation state. When a biocatalyst is suspended in low water organic solvent, the situation is more complex. In this case, counter ions are in closer contact with the opposite charges on the enzyme because of the lower dielectric constant of the medium. Thus, protonation of ionisable groups on the enzyme will be controlled by the type and availability of these ions as well as hydrogen ions. Changes in ionisation state of the protein can therefore be described by 2 equilibria which can, in theory, be controlled independently.