Non-canonical amino acids as a tool for the thermal stabilization of enzymes

Tim Lugtenburg, Alejandro Gran-Scheuch, Ivana Drienovská*

*Corresponding author for this work

Research output: Contribution to JournalReview articleAcademicpeer-review

Abstract

Biocatalysis has become a powerful alternative for green chemistry. Expanding the range of amino acids used in protein biosynthesis can improve industrially appealing properties such as enantioselectivity, activity and stability. This review will specifically delve into the thermal stability improvements that non-canonical amino acids (ncAAs) can confer to enzymes. Methods to achieve this end, such as the use of halogenated ncAAs, selective immobilization and rational design, will be discussed. Additionally, specific enzyme design considerations using ncAAs are discussed along with the benefits and limitations of the various approaches available to enhance the thermal stability of enzymes.

Original languageEnglish
Article numbergzad003
Pages (from-to)1-10
Number of pages10
JournalProtein Engineering, Design and Selection
Volume36
Early online date10 Mar 2023
DOIs
Publication statusPublished - 2023

Bibliographical note

Publisher Copyright:
© 2023 The Author(s). Published by Oxford University Press.

Keywords

  • biocatalysis
  • enzyme stability
  • halogenated ncAAs
  • ncAAs
  • selective pressure incorporation
  • stop codon suppression
  • unnatural amino acid

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