Abstract
Biocatalysis (the use of biological molecules or materials to catalyse chemical reactions) has considerable potential. The use of biological molecules as catalysts enables new and more specific syntheses. It also meets many of the core principles of “green chemistry”. While there have been some considerable successes in biocatalysis, the full potential has yet to be realised. This results, partly, from some key challenges in understanding the fundamental biochemistry of enzymes. This review summarises four of these challenges: the need to understand protein folding, the need for a qualitative understanding of the hydrophobic effect, the need to understand and quantify the effects of organic solvents on biomolecules and the need for a deep understanding of enzymatic catalysis. If these challenges were addressed, then the number of successful biocatalysis projects is likely to increase. It would enable accurate prediction of protein structures, and the effects of changes in sequence or solution conditions on these structures. We would be better able to predict how substrates bind and are transformed into products, again leading to better enzyme engineering. Most significantly, it may enable the de novo design of enzymes to catalyse specific reactions.
Highlights
Biocatalysis can be defined as the use of biological molecules or materials to accelerate the rate of chemical processes
This review focuses on four of these key areas and explains how solving some key biochemical problems would enable better biocatalysis in the future
In many systems, entropy is a key driver of the process and a major contributor to the overall free energy. This matters in biocatalysis partly because the hydrophobic effect is so important in directing protein folding
Summary
Biocatalysis can be defined as the use of biological molecules or materials to accelerate the rate of chemical processes. Biocatalysis allows the elimination of high temperatures and pressures It moves reactions away from organic solvents towards working in aqueous solutions. The high specificity of enzymes means that they often catalyse commercially interesting reactions at negligible rates, or not at all Their ability to work at modest temperatures and pressures means that they are often denatured if exposed to conditions outside their normal range. These include predicting the effects on yield of recombinant proteins when scaling up from laboratory-scale fermentations to industrial-scale ones and our lack of ability to culture many micro-organisms in the laboratory [7,8] This makes it difficult to study their biology and biochemistry and greatly hinders their use as cellular biocatalysts. Other challenges include societal and economic issues, including public acceptance of the use of genetically modified organisms as well as the time and costs associated with enzyme engineering projects
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