A new method to evaluate the thermal stability of lyophilized enzymes
Research output: Contribution to journal › Article
The thermal inactivation of lyophilized chymotrypsin was studied at controlled water activities. At 60 °C the enzyme showed good stability except at aw 0.97, whereas at 75 °C considerable inactivation occured at most water activities. Increasing the amount of buffer on the preparation decreased the stability significantly. The optimal temperature of enzymatic activity was increased 14 °C, when the water activity was decreased from 1 to 0.5.
|Research areas and keywords||
Subject classification (UKÄ) – MANDATORY
|Number of pages||6|
|Publication status||Published - 1996 Jan 1|