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
Protein & Peptide Letters
Title: Stabilization of Beta-Propeller Phytase by Introducing Xaa→Pro and Gly→Ala Substitutions at Consensus Positions
Volume: 15 Issue: 3
Author(s): Kam-Bo Wong, Edward T.K. Tung, Hoi-Wah Ma, Chiwai Cheng and Boon L. Lim
Affiliation:
Keywords: Beta-propeller phytase, protein engineering, proline, unfolding entropy, protein stability
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.
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Cite this article as:
Wong Kam-Bo, Tung T.K. Edward, Ma Hoi-Wah, Cheng Chiwai and Lim L. Boon, Stabilization of Beta-Propeller Phytase by Introducing Xaa→Pro and Gly→Ala Substitutions at Consensus Positions, Protein & Peptide Letters 2008; 15 (3) . https://dx.doi.org/10.2174/092986608783744216
DOI https://dx.doi.org/10.2174/092986608783744216 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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