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What is needed for the stomach protein digesting enzymes to become active?
Wiki User
∙ 12y ago
Zymogens are stored in their inactive form and need the Hydrochloric acid (or HCl) to be activated. Specifically, HCl converts pepsinogen into pepsin which can then be used to convert more pepsinogen into pepsin.
Wiki User
∙ 12y ago
Wiki User
∙ 12y agoIn order for the stomach enzyme (pepsinegin) to become active (pepsin) it has to be introduced to a low pH environment. Your stomach uses HCl (hydrochloric acid) to do this, when the perpsonegin comes in contact with the HCl it transforms it into pepsin which can break down protine
Wiki User
∙ 14y agoi expect that normal body temperature is needed, that's all i know, sorry.
Wiki User
∙ 14y agothe hydrochloric acid that is produced by the stomach helps in activating protein digesting enzymes
Wiki User
∙ 11y agoPepsin digests protein in stomach.
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Why are protein digestive enzymes produced and released in an inactive form?
In the case of protein digesting enzymes, known as endopeptidases, such as those secreted in the stomach (pespin), it is obvious. If they were secreted active they would digest the glands which secrete the enzymes themselves (gastric glands). Instead they must be secreted in an inactive form, which once in the stomach and exposed to HCl acid and other pepsin enzymes the pepsinogen activates and begins digesting protein.
Why the protein digesting enzymes are released in their active form?
so thay can immidiatly digeste the food
What are the enzymes produced in the stomach?
The main enzyme in the Stomach is Pepsin which is used to digest protein. Only protein digestion occurs in the stomach and almostt no absorption, (only a little alcohol). This protein is not secreted as its active form (ie not as pepsin) but as the Zymogen (the inactive precursor to proteins) Pepsinogen which cleaves in a low pH to form the active enzyme.
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.
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.
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.
How long does the food stay in stomach?
If your asking how long does food stay in your stomach before digesting is 4-6 hours. Depending on if your active after eating or not.
How an inactive protein can be converted into active protein?
An inactive protein can be converted into an active protein through the process of proteolysis. This process happens through the hydrolysis of the peptide bond, which is aided by cellular enzymes.
Which organ secrets enzymes that are active at a low pH?
The stomach secretes protease enzymes that work best at a pH of around 2.
How proteins are digested?
Proteins are digested by proteasees (enzymes) in the digestive system. Trypsin, peps, chymotrypsis are the proteases of stomach that start digesting proteins in to peptides. Enteropeptidases further digest them to small peptides and finally amino acids.
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.
Where on protease does a protein bond itself to?
It depends on the protease, but as with all enzymes, the substrate binds to the active site.
