Question

What converts pepsinogen to pepsin?

Answer 1

Hint: Pepsin is an endopeptidase that breaks down proteins into smaller peptides. It is produced inside the large intestinal cells in the stomach and is one of the most digestive enzymes within the digestive systems of humans and many other animals, where it helps digest food in the diet.

Complete answer:
Pepsinogen may be a progestin secreted by large cells in the stomach. Transformed into an active form, pepsin, by HCl, secreted by parietal cells inside the stomach. The ideal pH of pepsin is 1.8 and converts proteins into proteases and peptones.
Pepsin can be a protease, and pepsinogen can be a proenzyme. Pepsin is an active form of pepsinogen while pepsinogen is an inactive precursor of pepsin. Unlike pepsin, pepsinogen is secreted by key cells and pyloric glands. Unlike pepsinogen, pepsin can release hydrolyze proteins.
Pepsin can be a stomach enzyme that works to digest proteins found in processed foods. Large Gastric cells release pepsin as an inactive zymogen called pepsinogen. Parietal cells inside the stomach release an acid that lowers the pH of the stomach. The pH of coffee (1.5 to 2) uses pepsin.
The acid inside the digestive juice breaks down the food so the digestive enzymes break down the proteins. Acid digestive juices also kill germs. The mucus covers the abdominal wall with a protective layer.

Note:
this change in the enzyme reaction rate may also be due to the fact that pepsin is stored at low temperatures to stop harmful enzymes, so pepsin is a small amount that works at low temperatures until it reaches its activation capacity of about 30 ° c anything exceeding 50 ° c - 55 ° c will immediately release pepsin.