Understanding the Effect of Non-natural Fluid Environments on Enzyme Stability

Enzymes are the protein-based catalysts found throughout nature and are of immense scientific importance, and of great practical value in medicine, chemistry and biotechnology.

In most practical applications (such as industrial biocatalysis), enzymes are exposed to non-natural conditions, resulting in a loss of stability.

Our understanding of what leads to a loss in enzyme stability under these conditions is very poor and therefore the aim of this project is to obtain such understanding.

Current studies on enzyme stability mostly measure thermodynamic stability, and in some more limited cases operational stability, after exposure to different conditions (such as different temperatures and pH values).

However, they overlook the effect of mixing, exposure to high concentrations of reactant and product as well as to dynamic fluid-fluid interfaces, all of which are common in a most practical applications.

This project aims to understand the effect on enzyme stability of exposure to such non-natural conditions, using designed experiments in novel apparatus (mimicking industrial conditions), complemented by a suite of analytical characterization tools.

The result of such studies will firstly enable the re-design of suitable equipment for industrial biocatalysis, which is of increasing interest as an alternative catalytic method for the synthesis and production of a vast array of valuable products.

Secondly, the knowledge gained will be of great importance for protein engineering, providing the basis for pre-screening of enzymes on the basis of stability.

Finally, the results will also have implications for other areas of bioprocessing, including microbial fermentation for the extracellular to produce enzymes and cell culture to produce therapeutic proteins.