作者: N. A. Turner , D. B. Duchateau , E. N. Vulfson
DOI: 10.1007/BF00130792
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摘要: The thermostability of several serine esterases has been studied using differential scanning calorimetry. denaturation temperature (Tm) was found to be 30–50°C higher in anhydrous environments than aqueous solution. An almost linear decrease Tm as a function water activity (Aw) observed. It is concluded that the highest productivity an enzyme bioreactor would obtained at hydration level below optimal for catalytic activty. data also indicates significant destabilisation protein's unfolded state occurs low values Aw.