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

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 stabilit...

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Published inProtein engineering, design and selection Vol. 36
Main Authors Lugtenburg, Tim, Gran-Scheuch, Alejandro, Drienovská, Ivana
Format Journal Article
LanguageEnglish
Published England Oxford University Press 21.01.2023
Subjects
Amino Acids - chemistry
Biocatalysis
Short Review
enzyme stability
ncAAs
selective pressure incorporation
unnatural amino acid
halogenated ncAAs
stop codon suppression
biocatalysis
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Summary: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. Graphical abstract
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Tim Lugtenburg and Alejandro Gran-Scheuch contributed equally to this work.Edited by Prof. Dr. Christopher Snow.
ISSN:1741-0126
1741-0134
1741-0134
DOI:10.1093/protein/gzad003