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Directed evolution of carbon-hydrogen bond activating enzymes.
Journal article

Directed evolution of carbon-hydrogen bond activating enzymes.

  • Frey R Institute of Chemistry and Biotechnology, Department of Life Sciences and Facility Management, Zurich University of Applied Sciences, Einsiedlerstrasse 31, 8820 Waedenswil, Switzerland.
  • Hayashi T Institute of Chemistry and Biotechnology, Department of Life Sciences and Facility Management, Zurich University of Applied Sciences, Einsiedlerstrasse 31, 8820 Waedenswil, Switzerland.
  • Buller RM Institute of Chemistry and Biotechnology, Department of Life Sciences and Facility Management, Zurich University of Applied Sciences, Einsiedlerstrasse 31, 8820 Waedenswil, Switzerland. Electronic address: rebecca.buller@zhaw.ch.
  • 2018-12-25
Published in:
  • Current opinion in biotechnology. - 2019
Biocatalysis
Carbon
Catalysis
Directed Molecular Evolution
Enzymes
Hydrogen Bonding
Protein Engineering
English As industrial biocatalysis is maturing, access to enzymatic activities beyond chiral resolutions, asymmetric ketone reductions and reductive aminations is gradually becoming reality. Especially the utilization of carbon-hydrogen bond (C-H) activating enzymes is very attractive as they catalyze a variety of chemically extremely challenging transformations. Because of their intrinsic complexity, the use of these enzymes in manufacturing has been limited. However, recent advances in enzyme engineering and bioinformatics have led to activity improvements for native and non-native substrates, the introduction of new-to-nature chemistries and the identification of promising novel enzyme families. Looking forward, the use of automation and advanced computer algorithms will help to streamline the evolution process of C-H activating enzymes leading to more robust and active biocatalysts.
Language
  • English
Open access status
closed
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Persistent URL
https://sonar.ch/global/documents/279172
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