Related Experiment Video
Updated: Aug 16, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Evolution in the test tube as a means to create enantioselective enzymes for use in organic synthesis
1Max-Planck-Institut für Kohlenforschung, Mülheim/Ruhr, Germany.
Abstract:
A novel method for the creation of mutant enzymes showing increased levels of enantioselectivity in a given synthetic organic reaction is reviewed. It makes use of directed evolution and is therefore independent of structural or mechanistic aspects. Accordingly, known molecular biological methods for random mutagenesis coupled with the proper expression system and high-throughput screening methods for enantioselectivity form the basis of this new approach. An example is the lipase-catalyzed hydrolytic kinetic resolution of a chiral ester in which the original enantioselectivity of 2% ee is increased to > 90% ee in just a few rounds of mutagenesis.
Related Concept Videos
Enzyme Inhibition
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Catalytically Perfect Enzymes
Regioselective Formation of Enolates
Enzyme-Linked Immunosorbent Assay
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen. Enzyme-substrate reaction allows the antigen to be visualized or quantified.
Evolution of New Traits in Microbes

