What activates pepsinogen to pepsin?

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Multiple Choice

What activates pepsinogen to pepsin?

Explanation:
Acid in the stomach activates pepsinogen to pepsin. Pepsinogen is an inactive precursor released by chief cells, and the acidic environment created by hydrochloric acid lowers the pH enough to trigger a proteolytic change that converts it into the active enzyme pepsin. Once activated, pepsin functions best in this acidic milieu and can even help activate more pepsinogen in a self-amplifying loop. Other substances listed don’t initiate this conversion: lingual lipase acts in saliva on fats, pancreatic enzymes work in the small intestine, and trypsin is a pancreatic protease that activates other proenzymes later in digestion.

Acid in the stomach activates pepsinogen to pepsin. Pepsinogen is an inactive precursor released by chief cells, and the acidic environment created by hydrochloric acid lowers the pH enough to trigger a proteolytic change that converts it into the active enzyme pepsin. Once activated, pepsin functions best in this acidic milieu and can even help activate more pepsinogen in a self-amplifying loop. Other substances listed don’t initiate this conversion: lingual lipase acts in saliva on fats, pancreatic enzymes work in the small intestine, and trypsin is a pancreatic protease that activates other proenzymes later in digestion.

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