Biotechnology Letters

, Volume 17, Issue 4, pp 371–376

Effect of hydration on thermostability

  • N. A. Turner
  • D. B. Duchateau
  • E. N. Vulfson
Article

DOI: 10.1007/BF00130792

Cite this article as:
Turner, N.A., Duchateau, D.B. & Vulfson, E.N. Biotechnol Lett (1995) 17: 371. doi:10.1007/BF00130792

Summary

The thermostability of several serine esterases has been studied using differential scanning calorimetry. The denaturation temperature (Tm) was found to be 30–50°C higher in anhydrous environments than in aqueous solution. An almost linear decrease in Tm as a function of water activity (Aw) was observed. It is concluded that the highest productivity of an enzyme in a bioreactor would be obtained at a hydration level below optimal for catalytic activty. The data also indicates that a significant destabilisation of the protein's unfolded state occurs at low values of Aw.

Copyright information

© Chapman & Hall 1995

Authors and Affiliations

  • N. A. Turner
    • 1
  • D. B. Duchateau
    • 1
  • E. N. Vulfson
    • 1
  1. 1.BBSRC Institute of Food Research, Reading LaboratoryReadingUK