Evolving esterases and other hydrolytic enzymes for increased stability and activity.

Enzymes represent a safe and clean way of doing chemistry - they facilitate most of the reactions that occur in nature.  At any given time enzymes are responsible for more chemistry than the combined output of the chemical industry. If enzymes are safe an efficient, why not use them to catalyse reactions of interest to the chemical industry? The answer to this question probably can be found by looking at the properties of enzymes. Enzymes have evolved over millions of years to carry out a specific function and are therefore efficient catalyst for particular substrates. Unfortunately, industrial chemists cannot always find an enzyme that may be useful to them. This then leads to the question: how can we modify enzymes to facilitate reactions of industrial interest?

There are two approaches to improving enzyme function – one can use rational design or evolutionary techniques. The later approach that seems to dominate the literature and appears to be the most effective way of producing new enzymes – it is the process that I would like to use to produce new enzymes.

Hydrolytic enzymes are the most common type of enzyme found in nature. They have numerous functions – most are involved in the degradation and recycling of biological materials. Their natural functions can be adapted for a variety of practical purposes that range from the catalysis of industrially important reactions to the bioremediations and include a variety of medical applications. One important group of hydrolytic enzymes are the esterases that can be evolved for improved thermal stability. Projects in this area are frequently used to develop new methods, but these new methods can be applied to evolve enzymes to make useful reagents for the production of biodiesel and for the modification of food oils. 

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Updated:  21 November 2017/Responsible Officer:  Director, RSC/Page Contact:  Web Admin, RSC