yuppp that's why the stomach acid is so acidic, it will only work in a very acidic environment
it depends on the concentration of NaOH, pepsin, buffer used, ... that cannot be answered in that way...
It depends of the enzyme. For instance. Amylase in the mouth has a higher pH than say pepsin in the stomach.
2.3
The optimal pH for pepsin and rennin is about the same, 2.0 and 3.4 respectively. Pepsin is slightly more acidic.
Pepsin is a an acidic proteolytic enzyme activated from its precursor pepsinogen. Pepsin exhibits optimal activit at pH 1.5 to 2. It is highly active and stable at acidic pH and can be inactivated by pH 8.5 -11. Their amino acid composition is the reason for its stability.
it depends on the concentration of NaOH, pepsin, buffer used, ... that cannot be answered in that way...
yuppp that's why the stomach acid is so acidic, it will only work in a very acidic environment
Pepsin doesn't affect the pH but it is active in an acidic environment.
It depends of the enzyme. For instance. Amylase in the mouth has a higher pH than say pepsin in the stomach.
Pepsin is a type of protease that works mainly in the stomach. As a result, its optimum pH is around 2. The high acidity is provided by the hydrochloric acid in the stomach.
Pepsin is therefore acidic since the pH in the stomach is 2
2.3
The optimum PH of pepsin ranges between 1.0 and 4.0. Pepsin exhibits about 90 percent of the maximum activity and about 35% of the maximum activity.
The optimal pH for pepsin and rennin is about the same, 2.0 and 3.4 respectively. Pepsin is slightly more acidic.
pepsin is found in the stomach and the pH there is 2 while trypsin is found in the small intestine (duodenum and jejunum) and the pH there is 8-9. Thus, the optimum pH levels for pepsin and trypsin are 2 and 8-9 respectively.
It is most effective at around pH 2, and becomes inactive over 5.
Pepsin is a an acidic proteolytic enzyme activated from its precursor pepsinogen. Pepsin exhibits optimal activit at pH 1.5 to 2. It is highly active and stable at acidic pH and can be inactivated by pH 8.5 -11. Their amino acid composition is the reason for its stability.