Effect of hydration on thermostability

Autor: E. N. Vulfson, N. A. Turner, D. B. Duchateau
Rok vydání: 1995
Předmět:
Zdroj: Biotechnology Letters. 17:371-376
ISSN: 1573-6776
0141-5492
DOI: 10.1007/bf00130792
Popis: 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.
Databáze: OpenAIRE
Externí odkaz: