Substitution of Asp189 residue alters the activity and thermostability of Geobacillus sp. NTU 03 lipase

@article{Shih2011SubstitutionOA,
  title={Substitution of Asp189 residue alters the activity and thermostability of Geobacillus sp. NTU 03 lipase},
  author={Tsung-Wei Shih and Tzu-Ming Pan},
  journal={Biotechnology Letters},
  year={2011},
  volume={33},
  pages={1841-1846}
}
Error-prone PCR was used to create more thermoactive and/or thermostable variants of thermoalkalophilic lipases. A variant of the α6 helix (lid domain), with an 189E to V substitution at residue 189, lost its thermostability but exhibited higher activity than that of its wild-type predecessor (r03Lip). Site-saturation mutagenesis was used to explore the sequence-function relationship. Five other mutants also lost thermostability (20–40%) but exhibited enhanced thermoactivity (6.3–79-fold). The… CONTINUE READING

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