The optimal pH for gastric protease, primarily pepsin, is around 1.5 to 2.0. This highly acidic environment is necessary for the activation of pepsinogen into pepsin and facilitates the enzyme's ability to break down proteins in the stomach. Such acidity is crucial for effective digestion and helps kill pathogens present in food.
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Pepsin
The optimum pH for proteases can vary significantly depending on the specific enzyme and its source. Generally, most proteases function best in the acidic to neutral range, with many serine proteases operating optimally around pH 7-8, while pepsin, a gastric protease, works best at a pH of around 1.5-2.0. It's essential to consider the specific protease being studied, as its activity and stability can be highly pH-dependent.
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breaks down proteins in the stomach
Yes, gastric protease
Gastric protease, primarily pepsin, is located in the stomach. It is secreted by the gastric glands as an inactive precursor called pepsinogen, which is activated by the acidic environment of gastric juice. This enzyme plays a crucial role in the digestion of proteins, breaking them down into smaller peptides.
The optimum PH of pepsin ranges between 1.0 and 4.0. Pepsin exhibits about 90 percent of the maximum activity and about 35% of the maximum activity.
It is about pH 1 to 2. The gastric acid in our stomach (mainly consisting of hydrochloric acid, HCl) is at this pH level. The acidic medium is necessary for the digestive enzymes, such as those involved in the digestion of proteins, in gastric juice to work.
A gastric protease is an enzyme found in the stomach that breaks down proteins into smaller peptides and amino acids that can be absorbed by the body. One example of a gastric protease is pepsin, which is produced by the chief cells in the stomach lining and is activated by the acidic environment of the stomach.
Gastric protrease is produced by the walls of the stomach. It breaks down proteins to amino acids in the stomach (a highly acidic place).
Pepsin is one. http://en.wikipedia.org/wiki/Pepsin