Azocasein was used as substrate and hydrolyzed under protease. The location of characteristic peaks was different under acidic and alkaline conditions. It was wondered under which conditions protease activity was more accurate
Hi there,
The biological activity of any protein is dependent on pH. So the difference you note may be due to the effect of pH on the protease activity. The substrate susceptibility to the protease might also be dependent on pH...
BTW, It's "pH", not "Ph".
Which protease? pI? denaturation state of the substrate? Concentrations and purposed stochiometry? the substrate is reduced or not? Buffer ingredient? Incubation time? Temperature? Any competitive or non-competitive inhibitor? Any activator? PTMs? AA sequence of substrate convenient or not for a particular enzyme ...and so on...
There are many critical aspects for enzyme activity but regarding the pH, you need to state the target enzyme first to verify its optimum activity pH...
The change in pH changes the shape of the enzyme which prevents the attachment of the substrate at the active site and terminates the reaction.
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