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November 07, 2012
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A novel directed evolution method specific to the field of thermostability engineering was developed and consequently validated for bacteriolytic enzymes. After only one round of random mutagenesis, an evolved bacteriolytic enzyme, PlyC 29C3, displayed greater than twice the residual activity when compared to the wild-type protein after elevated temperature incubation.
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Heselpoth, R. D., Nelson, D. C. A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes. J. Vis. Exp. (69), e4216, doi:10.3791/4216 (2012).
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