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Updated: Jan 31, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Directed evolution of carbon-hydrogen bond activating enzymes
Raphael Frey1, Takahiro Hayashi1, Rebecca M Buller1
1Institute of Chemistry and Biotechnology, Department of Life Sciences and Facility Management, Zurich University of Applied Sciences, Einsiedlerstrasse 31, 8820 Waedenswil, Switzerland.
Abstract:
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.
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