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.
Pepsin doesn't affect the pH but it is active in an acidic environment.
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.
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.
The duodenum
Pepsinogen is activated in the stomach by the acidic environment, which triggers a change in its structure to become the active enzyme pepsin.
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stomach is dumped into the duodenum of the small intestine, the pH increases dramatically and the pepsin is denatured, no longer active to digest protein.
The carbohydrate molecule should not get fitted into the pepsin enzyme.
Because Pepsin is the active form of a protein manufactured in the stomach.
Pepsin is inactive in the absence of HCl because the acidic environment is necessary to convert pepsinogen into its active form, pepsin. HCl is needed to denature proteins and activate pepsin through a process called autocatalysis.
Pepsin has a optimum pH of 2, as found within the stomach. In the duodenum, the first part of the small intestine, the pH rises to 7.6. This relatively high pH damages the tertiary structure of the pepsin enzyme causing it to denature.
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.
peptic ulcer