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.
A very low pH can break the hydrogen bonds in an enzyme which causes the shape of the enzyme to change shape making the enzyme unable to do it's job. This is called "denaturation" However some enzymes such as pepsin only work in a low pH (pepsin works best in a pH of about 3) so it does depend on the enzyme.
Enzymes have an individual optimum pH, such as pepsin has a very low optimum pH
2.3
The optimal pH for pepsin and rennin is about the same, 2.0 and 3.4 respectively. Pepsin is slightly more acidic.
it depends on the concentration of NaOH, pepsin, buffer used, ... that cannot be answered in that way...
It is most effective at around pH 2, and becomes inactive over 5.
pepsin is activated from pepsinogen in stomach. the pH range for its optimal ativity is at acidic pH between 1.5 to 2. It is also stable upto pH8 and can be inactivated at basic pH from 8.5,
Pepsin doesn't affect the pH but it is active in an acidic environment.
Pepsin secreted in the stomach, works at highly acidic pH and the pH could be as low as 2. The optimal pH for pepsin is thus near about 2. This pH is maintained by HCl secreted by the gastric glands in the stomach.
A very low pH can break the hydrogen bonds in an enzyme which causes the shape of the enzyme to change shape making the enzyme unable to do it's job. This is called "denaturation" However some enzymes such as pepsin only work in a low pH (pepsin works best in a pH of about 3) so it does depend on the enzyme.
Enzymes have an individual optimum pH, such as pepsin has a very low optimum pH
pH 2This is because pepsin, the primary digestive enzyme found within the stomach, functions optimally at a low pH.
No quite the opposite the low pH allows the autocleavage of pepsins zymogen pepsinogen into the active form pepsin.
Yes. The precursor of pepsin is called pepsinogen; it is produced by stomach cells and then activated by the HCl in the stomach. Pepsin works best at very low pH.... e.g. acid conditions of the stomach. The small intestine has glands that produce neutralize the acid. Pepsin denatures at pH's of 5,0 or higher..... so effectively it is neutralized when the chyme enters the small intestine.
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
6.30-6.50 may be optimum pH for the fungal diastase....