Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case.

@article{Jermutus2001StructurebasedCE,
  title={Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case.},
  author={L Jermutus and Michel Tessier and Luis Pasamontes and Adolphus P G M van Loon and Martin Lehmann},
  journal={Journal of biotechnology},
  year={2001},
  volume={85 1},
  pages={15-24}
}
Thermostability is a key feature for commercially attractive variants of the fungal enzyme phytase. In an initial set of experiments, we restored ionic interactions and hydrogen bonds on the surface of Aspergillus terreus phytase, which are present in the homologous but more thermostable enzyme from A. niger. Since these mutations turned out to be neutral, we replaced-in the same region and based on the crystal structure of A. niger phytase-entire secondary structure elements. The replacement… CONTINUE READING

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