Chemical modification of enzymes to improve biocatalytic performance

Improvement in intrinsic enzymatic features is in many instances a prerequisite for the scalable applicability of many industrially important biocatalysts. To this end, various strategies of chemical modification of enzymes are maturing and now considered as a distinct way to improve biocatalytic pr...

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Bibliographic Details
Published in:Biotechnology advances 2021-12, Vol.53, p.107868-107868, Article 107868
Main Authors: Giri, Pritam, Pagar, Amol D., Patil, Mahesh D., Yun, Hyungdon
Format: Article
Language:English
Subjects:
Amines
Amino Acids
Biocatalysis
Biocatalysts
Canonical amino acids
Chemical modification
Dehydroalanine
Enzyme engineering
Enzymes
Enzymes - metabolism
Non-canonical amino acids
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Summary:Improvement in intrinsic enzymatic features is in many instances a prerequisite for the scalable applicability of many industrially important biocatalysts. To this end, various strategies of chemical modification of enzymes are maturing and now considered as a distinct way to improve biocatalytic properties. Traditional chemical modification methods utilize reactivities of amine, carboxylic, thiol and other side chains originating from canonical amino acids. On the other hand, noncanonical amino acid- mediated ‘click’ (bioorthogoal) chemistry and dehydroalanine (Dha)-mediated modifications have emerged as an alternate and promising ways to modify enzymes for functional enhancement. This review discusses the applications of various chemical modification tools that have been directed towards the improvement of functional properties and/or stability of diverse array of biocatalysts.
ISSN:0734-9750
1873-1899
DOI:10.1016/j.biotechadv.2021.107868