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Trypsin can be found in the small intestine. Trypsinogen is released by the pancreas into the duodenum or the small intestine where it reacts with enterokinase released by the intestinal glands which turns it into trypsin. this is so that the enzyme does not digest the tissues immediately after being released.
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∙ 12y ago
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Why would adult mosquitoes need trypsin?
to die
Would trypsin work well in the stomach?
No. The stomach is highly acidic (~2pH) while trypsin works well in the neutral/basic environment of the small intestine.
What do Trypsin and chymotrypsin digest?
Trypsin breaks down Peptides to Amino Acids
Are pepsin and trypsin classified as sugars?
pepsin and trypsin are classified as proteins
What pH does trypsin work at the best?
The optimal pH for trypsin is 8. It is found in the small intestine and digests proteins and polypeptides there.
What are the similarities of pepsin and trypsin?
Pepsin and trypsin both are protein digesting enzymes.
Where would the enzyme trypsin best function?
Enzyme trypsin is one of the enzymes that plays part during the process of digestion. Its site of action is in the small intestine where it breaks protein to large peptides.
Why trypsin is valuable?
Trypsin is a key digestive enzyme that assists with breaking down proteins and polypeptides. Trypsin also helps activate other enzymes like chymotrypsin.
How serum use to stop the trypsin action?
serum is going to stop the action of trypsin, because it contain the inhibitors of trypisn. Once you will inhit you can see the function of trypsin. SK
Name of the protein that can destroy protein?
An enzyme called a protease would digest proteins. Examples would be pepsin and trypsin.
What did the sodium carbonate do to the action of trypsin?
it makes the pH o the solution to 8.5 or above where trypsin is active.
What is the action of pancreatic trypsin on protein?
The digestive enzyme trypsin breaks down proteins found in the stomach.
