Iterative key-residues interrogation of a phytase with thermostability increasing substitutions identified in directed evolution

Title
Iterative key-residues interrogation of a phytase with thermostability increasing substitutions identified in directed evolution
Authors
Keywords
Directed evolution, KeySIDE, Molecular dynamics simulations, Phytase, Thermostability, Protein engineering
Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 100, Issue 1, Pages 227-242
Publisher
Springer Nature
Online
2015-09-25
DOI
10.1007/s00253-015-6959-5

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