Abstract
Phytases play important roles in agricultural and feed industries. In this study, the stability of a beta-propeller phytase, PhyL, from Bacillus licheniformis was successfully improved by introducing Xaa→Pro and Gly→Ala substitutions at consensus positions. Our results suggest that Gly→Ala substitution is a more promising strategy to improve protein stability.
Keywords: Beta-propeller phytase, protein engineering, proline, unfolding entropy, protein stability