Article
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.
Protein science : a publication of the Protein Society - 1 Apr 2012
Augustyniak Wojciech, Brzezinska Agnieszka A, Pijning Tjaard, Wienk Hans, Boelens Rolf, Dijkstra Bauke W, Reetz Manfred T
Abstract excerpt
Previously, Lipase A from Bacillus subtilis was subjected to in vitro directed evolution using iterative saturation mutagenesis, with randomization sites chosen on the basis of the highest B-factors available from the crystal structure of the wild-type (WT) enzyme. This provided mutants that, unl...
Topics
- Bacillus subtilis
- Bacterial Proteins
- Binding Sites
- Biophysical Phenomena
- Chemical Precipitation
- Circular Dichroism
- Crystallography, X-Ray
- Enzyme Activation
- Enzyme Stability
- Escherichia coli
- Evolution, Molecular
- Hot Temperature
- Lipase