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, unlike WT enzyme, retained a large part of their activity after heating above 65 °C and cooling down. Here, we subjected...
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