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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...

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Detalles Bibliográficos
Autores principales: Lugtenburg, Tim, Gran-Scheuch, Alejandro, Drienovská, Ivana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2023
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.
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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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