Key result
Endothia parasitica protease exhibited maximum stability at pH 3.8 to 4.5, with its stability significantly influenced by temperature, ionic strength, buffer type, and urea concentration.
Endothia parasitica protease exhibits distinct pH-dependent inactivation mechanisms, with maximum stability between pH 3.8 and 4.5.
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May guide dairy enzyme handling; leaves open any relevance to cardiovascular practice or research.
Larson et al. (1970) studied Endothia parasitica protease stability. Physicochemical conditions (pH, temperature, ionic strength, buffers, urea) was evaluated on Enzyme stability and inactivation. Endothia parasitica protease exhibited maximum stability at pH 3.8 to 4.5, with its stability significantly influenced by temperature, ionic strength, buffer type, and urea concentration.
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