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.
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
Yes, pepsin can work under acidic conditions in the stomach because it is optimally active at a low pH. The acidic environment in the stomach helps activate pepsinogen, the precursor to pepsin, and maintains the pH range suitable for pepsin to function in breaking down proteins into smaller peptides.
It is most effective at around pH 2, and becomes inactive over 5.
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 an enzyme that functions optimally at acidic pH levels around 1.5-2. At a neutral pH of 7, pepsin becomes inactive or denatured because its active site structure is altered, affecting its ability to catalyze protein digestion.
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.
The pH of pepsin is around 1.5 to 2.5. Pepsin works optimally at this acidic pH environment in the stomach, breaking down proteins into peptides.
Pepsin is therefore acidic since the pH in the stomach is 2
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.
Yes, pepsin can work under acidic conditions in the stomach because it is optimally active at a low pH. The acidic environment in the stomach helps activate pepsinogen, the precursor to pepsin, and maintains the pH range suitable for pepsin to function in breaking down proteins into smaller peptides.
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.