The thermal stability of the Fusarium solani pisi cutinase as a function of pH

@article{Petersen2001TheTS,
  title={The thermal stability of the Fusarium solani pisi cutinase as a function of pH},
  author={Steffen B. Petersen and Peter Fojan and Evamaria I. Petersen and Maria Teresa Neves Petersen},
  journal={Journal of Biomedicine and Biotechnology},
  year={2001},
  volume={1},
  pages={62 - 69}
}
We have investigated the thermal stability of the Fusarium solani pisi cutinase as a function of pH, in the range from pH 2-12. Its highest enzymatic activity coincides with the pH-range at which it displays its highest thermal stability. The unfolding of the enzyme as a function of pH was investigated by microcalorimetry. The ratio between the calorimetric enthalpy (DeltaH(cal)) and the van't Hoff enthalpy (DeltaH(v)) obtained, is far from unity, indicating that cutinase does not exhibit a… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-7 of 7 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 21 references

Protein Electrostatics

  • P Martel, A Baptista, SB. Petersen
  • El Gewely MR, ed. Biotechnology Annual Reviews
  • 1996
2 Excerpts

Genome structure and nucleotide sequence of a lipolyitc enzyme gene of Aspergillus oryzae

  • Ohnishi
  • FEMS Microbiol Lett
  • 1995
1 Excerpt

Similar Papers

Loading similar papers…