Abstract
1. 1. Collagenolytic protease A from the crab Paralithodes camtschatica has been shown to be stable under neutral and alkaline conditions and rapidly inactivated at pH < 6. 2. 2. Heat denaturation at pH 7.8 revealed a sharp decrease in its stability (40–50°C). 3. 3. Under mild alkaline conditions in the presence of 1 M NaCl and detergents the protease A stability remained unchanged and was independent of the enzyme concentration. However, the enzyme readily inactivates in the presence of 2 M guanidine/HCl and 1% 2-mercaptoethanol. 4. 4. Autolysis, though not exhibited at neutral pH, was demonstrated under acidic conditions. 5. 5. Effect of protein-protein interactions on the enzyme stability at pH 3.5 has been studied.
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