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A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
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Capitoli
- 00:05Titolo
- 01:25Determining Optimal Heating Conditions
- 06:15Generating the Mutant Library
- 08:44Soluble Lysate Heat Treatment
- 10:49Results: Directed Evolution to Increase the Thermostability of PlyC
- 13:07Conclusion
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.
