Effect of hydration on thermostability of serine esterases
1995
Turner, N.A. | Duchateau, D.B. | Vulfson, E.N.
The thermostability of several serine esterases has been studied using differential scanning calorimetry. The denaturation temperature (Tm) was found to be 30-50 degrees 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 activity. The data also indicates that a significant destabilisation of the protein's unfolded state occurs at low values of Aw.
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