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All proteins have a pH at which they work best. Pepsin is one of the few enzymes that work best at an acidic pH (about pH 2 to 3) like that in our stomach. When food moves from the stomach to the small intestine, bicarbonate is added to the mix to change the pH closer to neutral. This change in the pH changes the physical conformation of the pepsin, so it can no longer function.

2007-03-28 06:35:46 · answer #1 · answered by kt 7 · 0 0

Pepsin is a digestive protease. released by the chief cells in the stomach that functions to degrade food proteins into peptides.Once the peptides are formed,pepsin cannot break them down into further more simpler compounds so they reach intestine acted upon by enzymes proteases present in intestine.

Pepsin will digest up to 20% of ingested carbon bonds by cleaving preferentially after the N-terminal of aromatic amino acids such as phenylalanine and tyrosine. It will not cleave at bonds containing valine, alanine or glycine.

Peptides may be further digested by other proteases (in the duodenum) and eventually absorbed by the body

2007-03-28 10:37:59 · answer #2 · answered by ANITHA 3 · 0 0

Pepsin is active mainly in stomach in presence of HCL.It converts proteins into peptons.In small intestine completer digestion take place by conversion into ammino acid by succus interricus.

2007-03-28 05:34:35 · answer #3 · answered by Mayank Sharma 2 · 0 0

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