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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.
Wiki User
∙ 10y ago
Wiki User
∙ 15y agoThe pH level is not optimal for pepsin to work
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Does pepsin affect pH?
Pepsin doesn't affect the pH but it is active in an acidic environment.
Why arn't lipase and amylase secreted into the stomach with pepsin?
Lipase and amylase require an alkaline environment such as what is found in the duodenum of the small intestine. Pepsin functions in the acidic environment of the stomach.
What is the difference between pepsin and pepsinogen?
Pepsin is a powerful protein digesting enzyme which is far too dangerous in its active form so it is released in an inactive pepsinogen form by the cell and activated only in the digestive tract where it is required to be active.
Why can pepsin not be produced in its active form?
Pepsin degrades proteins so if it was active it would immediately begin digesting all the proteins in the cell. Therefore it is produced from a precursor known as a zymogen or proenzyme. Pepsin's proenzyme form is pepsinogen which is transformed to the activated pepsin protein.
Where in the intestine sucrase is to be the most active?
The duodenum
Why H. pylori is not destroyed by stomach acid?
Granted pepsin could kill a cell by hydrolyzing crucial proteins, it doesn't specifically destroy cells. It is a protease, a protein-digesting enzyme. There are two reasons why pepsin does not, under normal conditions, turn around and start digesting the cells of the host. Pepsin is only present in the stomach, where it is compartmentalized from the rest of the body. The mucous membrane protects the lining of the stomach so the stomach is not degraded by the enzymes or the strong hydrochloric acid. Secondly, pepsin is only active as an enzyme in very acidic environments like that of the stomach. Once the chyme of the stomach is dumped into the duodenum of the small intestine, the pH increases dramatically and the pepsin is denatured, no longer active to digest protein.
Why it is so that pepsin enzyme will not act if its active site is occupied by carbohydrate molecules?
The carbohydrate molecule should not get fitted into the pepsin enzyme.
Why would you predict the pepsin would not digest starch?
Because Pepsin is the active form of a protein manufactured in the stomach.
In the stomach the protein is digested by?
That is a proteolytic enzyme. Name of the enzyme is pepsin. It is secreted as inactive pepsinogen, which become active when it comes in contact with the hydrochloric acid, in the stomach.
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 will happen if body just makes fully active form of enzymes?
Consider the stomach. The inactive form of the digestive enzyme pepsin is called pepsinogin. ( spelling may be wrong ) It takes the release of hydrochloric acid in the stomach to activate this pre-enzyme into pepsin, the active form. You would be digesting your own stomach tissue if pepsin was always active.
What is the ulcer occurring in the lower portion of the esophagus stomach and duodenum caused by the breakdown of the mucosa membrane by the acid of gastric juices and pepsin?
peptic ulcer
