What are the characteristic of enzymes that prevents pytalin and trypsin from digesting same food?

The characteristic of enzymes that prevents pepsin and trypsin from digesting the same food depend on the following:

Optimum pH: Pepsin and trypsin have different optimum pH ranges for their catalytic activity. Pepsin works best in acidic conditions, with an optimum pH of around 1.5-2.0, which is found in the stomach. Trypsin, on the other hand, functions optimally in a slightly alkaline environment, with an optimum pH of around 7.5-8.0, which is characteristic of the small intestine.

Temperature: Pepsin and trypsin also have different temperature ranges within which they exhibit maximum activity. Pepsin is most active at body temperature (around 37 degrees Celsius), which is the temperature inside the stomach. Trypsin, however, is most active at slightly higher temperatures, around 40-45 degrees Celsius, which corresponds to the temperature in the small intestine.

Substrate specificity: Pepsin and trypsin have different substrate specificities, meaning they preferentially digest different types of proteins. Pepsin is mainly involved in the initial breakdown of proteins in the stomach, and it has a preference for cleaving peptide bonds involving aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan. Trypsin, on the other hand, works further along the digestive process in the small intestine, and it has specificity for cleaving peptide bonds involving basic amino acids, such as lysine and arginine.

These differences in optimum pH, temperature, and substrate specificity ensure that pepsin and trypsin act on proteins sequentially and selectively during the digestive process. Pepsin starts the digestion of proteins in the acidic environment of the stomach, breaking them down into smaller peptide fragments. As the stomach contents move into the small intestine, the pH becomes more alkaline, and trypsin becomes active. Trypsin further breaks down the peptide fragments generated by pepsin and other digestive enzymes, eventually leading to the absorption of amino acids into the bloodstream.