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it depends on the concentration of NaOH, pepsin, buffer used, ... that cannot be answered in that way...

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What happens if pepsin is added to NaOH?

If pepsin, an enzyme that breaks down proteins, is added to sodium hydroxide (NaOH), a strong base, the high pH of the NaOH will denature and inactivate the pepsin enzyme. Denaturation is the process where the protein loses its shape and function due to changes in pH, temperature, or other conditions. This would prevent pepsin from being able to digest proteins in the presence of NaOH.


What happens to solid egg white when pepsin and NaOH added?

Hey, I'm still a student, so I cannot guarantee that my answer is entirely correct, however, this is what my answer was on a similar question in a matsec paper: > Since pepsin is an enzyme, which works best in acidic environment, such as the one provided i the stomach, no change/ reaction would be observed, because NaOH is an alkaline solution. Therefore, pepsin would not be able to work in an environment with such great pH difference to its optimum. I hope that helped somehow although my answer is probably very late :P Good luck, Angelina


What is the pH of pepsin?

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.


What is the PH of 0.001N NaOH?

The pH of a 0.001N NaOH solution is around 11.9. NaOH is a strong base, and at this concentration, it will result in a highly alkaline solution.


Why is pepsin stable at a low pH?

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.

Related Questions

What happens if pepsin is added to NaOH?

If pepsin, an enzyme that breaks down proteins, is added to sodium hydroxide (NaOH), a strong base, the high pH of the NaOH will denature and inactivate the pepsin enzyme. Denaturation is the process where the protein loses its shape and function due to changes in pH, temperature, or other conditions. This would prevent pepsin from being able to digest proteins in the presence of NaOH.


What happens to solid egg white when pepsin and NaOH added?

Hey, I'm still a student, so I cannot guarantee that my answer is entirely correct, however, this is what my answer was on a similar question in a matsec paper: > Since pepsin is an enzyme, which works best in acidic environment, such as the one provided i the stomach, no change/ reaction would be observed, because NaOH is an alkaline solution. Therefore, pepsin would not be able to work in an environment with such great pH difference to its optimum. I hope that helped somehow although my answer is probably very late :P Good luck, Angelina


Can NaOH and pepsin cause digestion?

No is the answer. Sodium hydroxide is is such a strong alkali that it will 'burn' the cells just like acid does. So it is not found in body. Instead you have sodium bi carbonate. But you have very strong acid in stomach. Hydrochloric acid. Imagine acidity go on increasing ten times as you go from 6 to 5 and 5 to 4. And pH in stomach is 1 to 2. (Why does not stomach is 'not' charred at this pH ?) Pepsin works in high acidic pH only and almost stop working at 5.5 pH. So no question of digestion in sodium hydroxide, which is strong alkali with very high pH. If you lower the pH pepsin starts working again.


Does pepsin affect pH?

Pepsin doesn't affect the pH but it is active in an acidic environment.


What is the pH of pepsin?

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.


During digestion the pH in the stomach is 2 What does this indicate about the optimum pH of pepsin?

Pepsin is therefore acidic since the pH in the stomach is 2


What is the pH for pepsin?

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.


How much NaOH do you use to lower pH?

You dont - adding NaOH increases pH.


Pepsin a digestive enzyme found in the stomach works best at a pH near?

Pepsin works best in acidic environments and it's optimal pH (the pH at which it works best) is 2.0


Compare the optimum pH levels for trypsin and pepsin. how is the optimal pH level of pepsin relevant to it's particular location in the body?

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.


What effect the pH have on protein digestion with pepsin?

It is most effective at around pH 2, and becomes inactive over 5.


What is the pH of a 1 millimolar NaOH soluiton?

The pH of a 1 millimolar NaOH solution is approximately 11. The concentration of a 1 millimolar solution is 0.001 mol/L, and NaOH is a strong base that completely dissociates in water to produce hydroxide ions, leading to a basic pH.