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What is the pH of Pepsin in NaOH?
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.
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
How would the digestion of food be affected if your stomach did not produce hydrochloric acid?
A person's inability to produce hydrochloric acid in the stomach is called achlorhydria. This condition affects the enzyme pepsin, which helps to break down proteins. Pepsin requires a low pH to be activated.
Why is pepsin a bad enzyme in washing powder?
Pepsin is a bad enzyme in washing powder because it can break down and damage fabrics, leading to the deterioration of clothing. In addition, pepsin is not effective in removing stains or dirt from clothes as it is specifically designed to digest proteins in the stomach rather than act as a cleaning agent.
What would happen to a newborn mammal if its body could not produce rennin?
The function of rennin is to curdle milk proteins by converting the soluble protein caesinogen into the insoluble protein caesinogen. If the new born mammal is unable to produce rennin, then the soluble milk proteins would just pass through the stomach into the duodenum like water. This is bad because the milk proteins would not be able to get digested by the pepsin. However, if there is rennin, the converted insoluble milk proteins would be abe to stay in the stomach long enough for the pepsin to digest it into polypeptides.
What is the pH of Pepsin in NaOH?
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.
What effect would decreased incubation temperature have on pepsin activity and why?
Decreased incubation temperature would likely decrease pepsin activity because enzymes generally have optimal temperature ranges for activity, and lower temperatures can slow down enzyme reactions. Pepsin is a digestive enzyme that functions optimally at around body temperature (37°C), so decreasing the temperature may reduce its efficiency in breaking down proteins.
What effect would decreased incubation temperatures have on pepsin?
Pepsin activity would decrease and at a very low temperature pepsin would be inactive.
What effect would decrease incubation temperature have on pepsin activity?
Pepsin activity would decrease and at a very low temperature pepsin would be inactive.
How would you describe the detection of rennin activity?
curds will appear
A baby dolphin would have rennin in its stomach?
A baby dolphin does indeed have rennin in i'ts stomach. This is because the dolphin is still developing and learning how to care for itself.
What would most likely happen to pepsin that traveled with the food from the stomach to the small intestines?
the pepsin would become innactive
Percentage of rennin needed to coagulate milk?
Any Percentage of Rennin, above none, will coagulate milk. More Rennin would increase the rate at which the milk is coagulated, obviously. Hydrophobic para-casein would join together, after bonds between hydrophobic and hydoophilic parts are broken. <As far as I can understand it,Berrik.> Any Percentage of Rennin, above none, will coagulate milk. More Rennin would increase the rate at which the milk is coagulated, obviously. Hydrophobic para-casein would join together, after bonds between hydrophobic and hydoophilic parts are broken. <As far as I can understand it,Berrik.>
Why would you predict the pepsin would not digest starch?
Because Pepsin is the active form of a protein manufactured in the stomach.
What would most likely happen to pepsin enzyme that traveled with the food from the stomach to the small intestines?
the pepsin would become innactive
What would happen when the enzyme pepsin that normally acts on protein in the stomach is pushed into the small intestine that has a relatively high pH?
the pepsin would become innactive
