title: Stabilization of beta-propeller phytase by introducing Xaa-->Pro and Gly-->Ala substitutions at consensus positions.
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.
authors.affiliation: School of Biological Sciences, University of Hong Kong, Pokfulam Road, Hong Kong, China.
authors.forename: Edward T K
authors.initials: ET
authors.lastname: Tung
authors.forename: Hoi-Wah
authors.initials: HW
authors.lastname: Ma
authors.forename: Chiwai
authors.initials: C
authors.lastname: Cheng
authors.forename: Boon L
authors.initials: BL
authors.lastname: Lim
authors.forename: Kam-Bo
authors.initials: KB
authors.lastname: Wong
mesh_terms: D010832:6-Phytase / Q000737:chemistry*; D000409:Alanine / Q000737:chemistry*; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001407:Bacillus / Q000201:enzymology; D016384:Consensus Sequence; D005998:Glycine / Q000737:chemistry*; D008969:Molecular Sequence Data; D011392:Proline / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D011392:Proline; D010832:6-Phytase; D000409:Alanine; D005998:Glycine