• Chemistry, Medicine
  • Published in
    Biotechnology and applied…
    2018
  • DOI:10.1002/bab.1576

Role of Q177A and K173A/Q177A substitutions in thermostability and activity of the ELBn12 lipase.

@article{Farrokh2018RoleOQ,
  title={Role of Q177A and K173A/Q177A substitutions in thermostability and activity of the ELBn12 lipase.},
  author={Parisa Farrokh and Bagher Yakhchali and Ali Asghar Karkhane},
  journal={Biotechnology and applied biochemistry},
  year={2018},
  volume={65 2},
  pages={
          203-211
        }
}
Thermostable lipases have many applications in detergent industries and in organic synthesis. There are many ways to improve thermal stability of enzymes, for example, higher hydrophobicity, greater structural packing, higher content of the charged residues, and lower thermolabile ones. In this study, thermolabile Gln (sensitive to higher temperatures) was substituted with Ala in native ELBn12 and mutated K173A lipases to examine its effect on thermal stability and activity of the lipases… CONTINUE READING

Figures, Tables, and Topics from this paper.

Citations

Publications citing this paper.

References

Publications referenced by this paper.
SHOWING 1-2 OF 2 REFERENCES

Article ID 684506

C. D. Anobom, A. S. Pinheiro, +5 authors D. M. Freire
  • Biomed. Res. Int
  • 2014
VIEW 2 EXCERPTS

Role of Q177 Substitution in ELBn12 Lipase

E. H. Ahmed, T. Raghavendra, D. Madamwar
  • Appl. Biochem. Biotechnol
  • 2010
VIEW 2 EXCERPTS