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Stabilization of Beta-Propeller Phytase by Introducing Xaa→Pro and Gly→Ala Substitutions at Consensus Positions

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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; proline; protein engineering; protein stability; unfolding entropy

Document Type: Research Article


Publication date: 2008-03-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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