2.3
The optimal pH for pepsin and rennin is about the same, 2.0 and 3.4 respectively. Pepsin is slightly more acidic.
The value of high pH indicates the basicity of that substance.
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.
The stomach contains hydrochloric acid, which has a pH of generally 1-3. These optimal pH levels must be present in order for pepsin (a protein-digesting enzyme) to function. If the pH is not acidic, pepsin will only be present in its inactive form, pepsinogen, and protein digestion will effectively occur. Uhh.. hope that's what you were looking for. The second part is just a bit more detail as to why the pH of stomach is important.
it decreases
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.
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
It denatures (enzyme breaks down) because pepsin is best operational in a pH of around 2 or 3 in the stomach juices.
It is most effective at around pH 2, and becomes inactive over 5.
no they can not because they at completely different pH levels.
Enzymes work within a range of pH levels. Pepsin, which is found in the stomach works in an acidic environment, while trypsin functions in a basic surrounding in the intestines. Increasing or decreasing the pH levels can stop the activity of these enzymes.
Pepsin doesn't affect the pH but it is active in an acidic environment.
Pepsin is therefore acidic since the pH in the stomach is 2
the pepsin would become innactive
2.3