Enzyme Engineering: From Chemically Induced Modifications to Genetic Code Expansion
A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".
Deadline for manuscript submissions: closed (30 November 2021) | Viewed by 5914

Special Issue Editors
Interests: protein engineering; chemical biology; proteomics and drug discovery
Special Issue Information
Dear Colleagues,
Enzyme engineering has become extremely important for biocatalytic processes, which is observed by the amount of research that has been dedicated to this field in the past decade. This interest is due to the intrinsic features of enzymes and their advantages over chemical catalysts such as high productivity, specificity, and catalytic efficiency, but it is also faced with high cost and low stability issues. These drawbacks have propelled the development of several methods to tackle these problems while also avoiding the cost and waste associated with single-use and throwaway practices. Traditional methods of enzyme engineering have enabled the production of stable and highly efficient enzymes as well as entirely new functionalities, but they have also started to concede space to more advanced approaches. Recent efforts have focused on induced chemical modifications and genetic code expansion to install new catalytic modalities, expand acceptable substrates, and increase thermostability amongst other features. This Special Issue aims to cover the progress and trends in traditional enzyme engineering, new chemical methods to modify and modulate enzyme activity and structure, genetic code expansion by insertion of noncannocial amino acids (ncAA), and other strategies to develop innovative biocatalysts.
Dr. Jean Bertoldo
Prof. Dr. Hernán Terenzi
Guest Editors
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Keywords
- Noncanonical amino acids (ncAAs)
- Genetic code expansion
- Directed evolution
- Site-directed mutagenesis
- Posttranslational chemical mutagenesis
- New enzyme modalities
- Site-specific protein modification
- Unnatural amino acids (UAAs)
- Protein functionalization
- Reusable biocatalysts
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