Proteases are widely found in animal livers, plant stems, leaves and fruits, and microorganisms. Proteases have many functions. Now proteases have been widely used in fur, leather, silk, food, medicine, and brewing, and can create great productivity. There are many types of proteases, the most common ones are trypsin and pepsin. Protease has many uses and its medicinal function is also very powerful. Pepsin is very effective in treating indigestion, and acidic protease can effectively treat bronchitis. Let's take a look at the role of protease, especially trypsin. The role of trypsin The role of trypsin is to hydrolyze the proteins between cells, thereby separating the cells. Different tissues or cells respond differently to the action of pancreatic enzymes. The activity of pancreatic enzyme in dispersing cells is also related to its concentration, temperature and action time. When the pH is 8.0 and the temperature is 37°C, the pancreatic enzyme solution has the strongest action ability. When using pancreatic enzymes, the concentration, temperature and time should be properly controlled to avoid excessive digestion and cell damage. Because Ca2+, Mg2+, serum and protein can reduce the activity of pancreatic enzymes, BSS that does not contain Ca2+ and Mg2+, such as D-Hanks solution, should be used when preparing pancreatic enzyme solution. When terminating digestion, serum-containing culture medium or trypsin inhibitor can be used to terminate the effect of trypsin on cells. 1. Weigh trypsin: Based on a trypsin solution concentration of 0.25%, accurately weigh the powder using an electronic balance and dissolve it in double distilled water (if double distilled water is used, the pH needs to be adjusted to about 7.2) or PBS (D-hanks) solution in a small beaker. Stir to mix and place at 4°C overnight. 2. Filter and sterilize with a syringe filter: The prepared pancreatic enzyme solution should be filtered and sterilized with a syringe filter (0.22 micron microporous filter membrane) in an ultra-clean bench. Then the solution was divided into vials and stored at -20℃ for future use. Trypsin can catalyze the hydrolysis of specific peptide bonds in proteins. This catalytic process does not require energy, will not cause the enzyme to lose its activity, change its shape, or cause itself to hydrolyze. The binding of the substrate to the active center of the enzyme is reversible. This binding causes specific peptide bonds of the protein to be activated due to bending and deformation, making them more susceptible to attack by water molecules, forming amino and carboxyl groups respectively and breaking to obtain small molecule polypeptides or amino acids. Different proteases can act on peptide bonds composed of different amino acids, so trypsin cannot act on all peptide bonds. The role of pepsin Pepsin (Gastric protein enzyme): Pharmacological action : This product is a digestive enzyme. Under gastric acid conditions, coagulated proteins are broken down into peptones, but cannot be further broken down into amino acids, thus promoting protein digestion. Indications : Pepsin is mainly used for indigestion caused by excessive consumption of protein, decreased digestive function during the recovery period after illness, chronic atrophic gastritis, gastric cancer, and pepsin deficiency caused by pernicious anemia. Dosage form and specifications : Tablets: 0.1 g (120 units)/tablet; Granules: 0.4 g (480 units)/bag. Usage and Dosage : Oral administration, 0.3-0.6 g during or before meals. Note : ① It is contraindicated for those who are allergic to pepsin. ②It should not be taken together with antacids and sucralfate. Protease has been widely used now. Maybe everyone is not very familiar with this knowledge, but we cannot deny the contribution of protease to our daily life and social development. Pepsin is very effective in treating some stomach diseases, especially for the treatment of digestive function. |
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