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