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Non-canonical amino acids as a tool for the thermal stabilization of enzymes
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 improve...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10064326/ https://www.ncbi.nlm.nih.gov/pubmed/36897290 http://dx.doi.org/10.1093/protein/gzad003 |
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author | Lugtenburg, Tim Gran-Scheuch, Alejandro Drienovská, Ivana |
author_facet | Lugtenburg, Tim Gran-Scheuch, Alejandro Drienovská, Ivana |
author_sort | Lugtenburg, Tim |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-10064326 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-100643262023-04-01 Non-canonical amino acids as a tool for the thermal stabilization of enzymes Lugtenburg, Tim Gran-Scheuch, Alejandro Drienovská, Ivana Protein Eng Des Sel Short Review 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. Oxford University Press 2023-03-10 /pmc/articles/PMC10064326/ /pubmed/36897290 http://dx.doi.org/10.1093/protein/gzad003 Text en © The Author(s) 2023. Published by Oxford University Press. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Short Review Lugtenburg, Tim Gran-Scheuch, Alejandro Drienovská, Ivana Non-canonical amino acids as a tool for the thermal stabilization of enzymes |
title | Non-canonical amino acids as a tool for the thermal stabilization of enzymes |
title_full | Non-canonical amino acids as a tool for the thermal stabilization of enzymes |
title_fullStr | Non-canonical amino acids as a tool for the thermal stabilization of enzymes |
title_full_unstemmed | Non-canonical amino acids as a tool for the thermal stabilization of enzymes |
title_short | Non-canonical amino acids as a tool for the thermal stabilization of enzymes |
title_sort | non-canonical amino acids as a tool for the thermal stabilization of enzymes |
topic | Short Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10064326/ https://www.ncbi.nlm.nih.gov/pubmed/36897290 http://dx.doi.org/10.1093/protein/gzad003 |
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