2.3
The pH of pepsin in NaOH would depend on the concentration of NaOH added. Pepsin is an enzyme that functions best at acidic pH levels, around pH 2.0. Adding NaOH, a base, would increase the pH, potentially inactivating the pepsin enzyme as it moves away from its optimal pH range for activity.
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.
Pepsin is an enzyme that functions optimally in acidic pH environments, such as the stomach. In alkaline pH conditions, pepsin can become denatured or inactivated, leading to a loss of its ability to break down proteins effectively. This is why pepsin is most active in the acidic environment of the stomach, where it helps in digesting proteins.
Pepsin is an enzyme that functions optimally in acidic environments, such as the stomach's low pH. In high pH levels, like those found in the small intestine, pepsin becomes denatured and its enzymatic activity decreases or stops altogether.
No, optimal pH for pepsin is around 2.0 (acidic environment) while optimal pH for rennin is around 6.5-6.7 (slightly acidic to neutral environment). Each enzyme has a specific pH range at which it functions most efficiently due to its unique structure and function.
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 pH of pepsin in NaOH would depend on the concentration of NaOH added. Pepsin is an enzyme that functions best at acidic pH levels, around pH 2.0. Adding NaOH, a base, would increase the pH, potentially inactivating the pepsin enzyme as it moves away from its optimal pH range for activity.
The optimal pH for pepsin, an enzyme found in the stomach that helps in protein digestion, is around 2.0. This low pH is necessary for pepsin to be active and function effectively in breaking down proteins into smaller peptides.
Pepsin works best in acidic environments and it's optimal pH (the pH at which it works best) is 2.0
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 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 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.
pepsin
Pepsin is an enzyme that functions optimally in acidic pH environments, such as the stomach. In alkaline pH conditions, pepsin can become denatured or inactivated, leading to a loss of its ability to break down proteins effectively. This is why pepsin is most active in the acidic environment of the stomach, where it helps in digesting proteins.
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.