Affiliation:
1. Vrije Universiteit Amsterdam Department of Chemistry & Pharmaceutical Sciences, , 1081 HZ Amsterdam, The Netherlands
Abstract
AbstractBiocatalysis 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.
Funder
Netherlands Organization for Scientific Research
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Cited by
8 articles.
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