Skip to main content
padlock icon - secure page this page is secure

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

Buy Article:

$68.00 + tax (Refund Policy)

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.

No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Beta-propeller phytase; proline; protein engineering; protein stability; unfolding entropy

Document Type: Research Article

Publication date: March 1, 2008

More about this publication?
  • 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.
  • Editorial Board
  • Information for Authors
  • Subscribe to this Title
  • Ingenta Connect is not responsible for the content or availability of external websites
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more