Abstract
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.
Original language | English |
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Pages (from-to) | 947-952 |
Number of pages | 6 |
Journal | Biotechnology Techniques |
Volume | 10 |
Issue number | 12 |
DOIs | |
Publication status | Published - 1996 Jan 1 |
Subject classification (UKÄ)
- Biocatalysis and Enzyme Technology