Enzymes are large complex protein molecules, which fold in a specific three dimensional structure to confer catalytic activity. They are therefore of great importance to our understanding of medicine, biochemistry and microbiology. We often refer to such catalysts as Nature’s catalysts, since they are the catalysts found in all living things. As catalysts, they are responsible for speeding up chemical reactions, meaning that much of Nature can exist under relatively mild conditions (usually ambient conditions). Without enzymes many reactions essential to life would be so slow as to require higher temperatures. Indeed synthetic catalysts (often based on metals) operate under more extreme conditions such as high temperature and pressure which also makes them expensive and hardly sustainable. Therefore, the incentive to use enzymes is driven primarily by sustainability, and this is further complemented by their excellent selectivity, meaning reactions have few side reactions and can thereby achieve a high yield (mass product/mass reactant). Today we know a great deal about enzymes, and their mechanism of action, but we also have some gaps in our knowledge. For example we understand well the kinetics (how fast an enzyme works), and thermodynamics (how far a reaction can proceed towards the product). A third area of importance is understanding the stability of an enzyme, how well the enzyme maintains its structure and speed (termed its activity) over time. Here we know well about structure, and in many cases also activity changes when enzymes are exposed to specific defined conditions. However, we know very little about what happens to enzymes when they are exposed to new-to-nature conditions. It is of course of great scientific interest to know this, simply as part of our understanding about all the conditions under which enzymes can work, but it can also have significant practical implications. For example reactors using enzymes operating in industrial biotechnological processes, used for the production of food ingredients, medicines and chemicals, are often exposed to radical new-to nature conditions. The overall objectives of this project are to identify such conditions, develop equipment to study the stability of enzymes in such conditions, collect data for different enzymes in such apparatus to understand the generality of the observations, and finally to build mathematical models to describe the mechanism through which stability is lost.
