Four Challenges for Better Biocatalysts

Research output: Contribution to journalArticleResearchpeer-review

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.
Original languageEnglish
Article number39
Number of pages9
JournalFermentation
Volume5
Issue number2
DOIs
Publication statusPublished - 9 May 2019

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Enzymes
Protein folding
Biochemistry
Molecules
Biomolecules
Organic solvents
Catalysis
Chemical reactions
Catalysts
Substrates
Biocatalysis
Proteins

Bibliographical note

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Keywords

  • protein folding
  • enzyme engineering
  • hydrophobic effect
  • chaotropicity
  • enzyme mechanism
  • water activity
  • green chemistry
  • enzyme specificity
  • biotechnology
  • protein structure
  • Biotechnology
  • Chaotropicity
  • Enzyme engineering
  • Enzyme mechanism
  • Water activity
  • Protein folding
  • Hydrophobic effect
  • Green chemistry
  • Protein structure
  • Enzyme specificity

Cite this

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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.",
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Four Challenges for Better Biocatalysts. / Timson, David J.

In: Fermentation, Vol. 5, No. 2, 39, 09.05.2019.

Research output: Contribution to journalArticleResearchpeer-review

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