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Unlike pepsin, trypsin is secreted by the pancreas into the small intestine, explains Dr. Gary Thibodeau in his book "Anatomy and Physiology." It also breaks the bonds between amino acids, but it focuses on different amino acid bonds. Specifically, trypsin breaks the bonds that follow the amino acids lysine and arginine. Since different proteolytic enzymes can break different bonds, many enzymes have to work together to break a protein down completely.

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What enzymes perform major proteolytic activities in the digestive tract?

The major proteolytic enzymes in the digestive tract are pepsin, trypsin, chymotrypsin, and elastase. Pepsin is mainly found in the stomach, while trypsin, chymotrypsin, and elastase are produced in the pancreas and released into the small intestine to further break down proteins into smaller peptides and amino acids for absorption.


The part of alimentary canal where protein is digested?

Protein is digested both in the stomach (by pepsin and trypsin) and in the small intestine.


The enzyme pepsin is produced in the cells of the stomach but not in the cells of the small intestine The small intestine produces a different enzyme trypsin The reason that the stomach what?

The reason the stomach produces pepsin is because pepsin is active in the acidic environment of the stomach, which is needed to break down proteins into peptides. Trypsin, produced in the small intestine, functions in a less acidic environment and helps further break down peptides into smaller molecules for absorption. This specialization allows the different digestive enzymes to work effectively in their respective environments.


What breaks down protein into amino acids?

Protease in general. Pepsin in the stomach and trypsin in the small intestine in mammals break down protein into polypeptide chains and erepsin in the small intestine break down polypeptide chains into amino acids.


Compare the optimum pH levels for trypsin and pepsin. how is the optimal pH level of pepsin relevant to it's particular location in the body?

pepsin is found in the stomach and the pH there is 2 while trypsin is found in the small intestine (duodenum and jejunum) and the pH there is 8-9. Thus, the optimum pH levels for pepsin and trypsin are 2 and 8-9 respectively.


In the small intestine proteins are digested by?

Trypsin and Peptidases


Would trypsin work well in the stomach?

No, trypsin is a digestive enzyme produced in the pancreas that functions in the small intestine to break down proteins. It would not work well in the stomach due to the acidic environment and presence of other digestive enzymes like pepsin that are better suited for protein digestion in the stomach.


What happen to the pepsin that enters to the small intestine?

Pepsin becomes inactive when it reaches the small intestine where the pH is between 7 and 9. It functions best when in an acidic environment like the stomach.


What enzymes speeds up the breakdown of protein in food?

Protease enzymes, such as pepsin and trypsin, are responsible for breaking down proteins in food into smaller peptides and amino acids. These enzymes work in the stomach and small intestine to facilitate the digestion of proteins.


Trypsin is secreted from?

Trypsin is secreted from the pancreas as an inactive zymogen called trypsinogen. It is activated in the small intestine by enteropeptidase enzyme into its active form, trypsin. Trypsin plays a crucial role in the digestion of proteins by breaking down peptides into smaller amino acids.


Proteins are broken down by pepsin Why is trypsin needed?

Trypsin is needed because it breaks down proteins into smaller peptides and amino acids, further digesting protein molecules that were partially broken down by pepsin. It is produced by the pancreas and works in the small intestine to aid in protein digestion.


The enzyme that catalyzes the digestion of peptides in the small intestine is?

The enzyme that catalyzes the digestion of peptides in the small intestine is pepsin. Pepsin is released by the mucosal lining of the stomach.