A new method to evaluate the thermal stability of lyophilized enzymes |
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Authors: | Ernst Wehtje Hugo de Wit Patrick Adlercreutz |
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Institution: | (1) Department of Biotechnology, Center for Chemistry and Chemical Engineering, Lund University, POBox 124, S-221 00 Lund, Sweden |
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Abstract: | Summary 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. |
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