Stabilization of beta-propeller phytase by introducing Xaa-->Pro and Gly-->Ala substitutions at consensus positions.
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.
Tung
Edward T K
ET
School of Biological Sciences, University of Hong Kong, Pokfulam Road, Hong Kong, China.
Ma
Hoi-Wah
HW
Cheng
Chiwai
C
Lim
Boon L
BL
Wong
Kam-Bo
KB
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
D011392:Proline; D010832:6-Phytase; D000409:Alanine; D005998:Glycine