4.6 Review

Four Challenges for Better Biocatalysts

Journal

FERMENTATION-BASEL
Volume 5, Issue 2, Pages -

Publisher

MDPI
DOI: 10.3390/fermentation5020039

Keywords

protein folding; enzyme engineering; hydrophobic effect; chaotropicity; enzyme mechanism; water activity; green chemistry; enzyme specificity; biotechnology; protein structure

Funding

  1. Department of Employment and Learning, Northern Ireland (DELNI, UK)
  2. Environmental Protection Agency (Ireland) [2007-PhD-ET-9]
  3. Environmental Protection Agency Ireland (EPA) [2007-PhD-ET-9] Funding Source: Environmental Protection Agency Ireland (EPA)

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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.

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