Download Digestion of dietary proteins

Digestion of dietary proteins
Digestion of dietary proteins
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Most of the nitrogen in the diet is consumed
in the form of protein.
Protein are generally too large to be
absorbed by the intestine. They must be
hydrolyzed to yield their constituent amino
acid, which can be absorbed.
Proteolytic enzymes responsible for
Degrading proteins are produced by
three different organs:



The stomach
The pancreas
and the small intestine
Digestion of proteins by gastric
secretion
The digestion of proteins begins in the
stomach, which secretes gastric juiceaunique solution containing:
1- Hydrochloric acid
2- Proenzyme, Pepsinogen.

Hydrochloric acid


Stomach acid is too dilute (PH 2 to 3) to
hydrolyze proteins.
The acid function instead to kill bacteria and
to denature proteins.
Pepsin
This acid –stable endopeptidase is sedreted by the
serous cells of stomach as an in active Proenzyme,
Pepsinogen.
 Pepsinogen is activated to pepsin either by:
1- HCl
2- autocatalytically by other pepsin molecules that have
already been activated.
Pepsin releases peptides and a few free amino acids
from dietary proteins.

Digestion of proteins by pancreatic
enzymes


The release and activation of the pancreatic
zymogens is mediated by secretion of
Cholecystokinin and Secretin, two
polypeptide hormones.
pancreatic enzymes has a different specificity
for the amino acid R-groups adjacent to the
susceptible peptide bond.
pancreatic enzymes

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Trypsin
Chymotrypsin
Elastase.
Carboxypeptidase A.
Carboxypeptidase B.
Trypsin
Enteropeptidase
Trypsinogen
Arg and Lys
Trypsin
Chymotrypsin
trypsin
Chymotrypsinogen
(Trp , Tyr, phe, Met, Leu COOH)
Chymotrypsin
Elastase
trypsin
Proelastase
(Ala,Gly, Ser COOH)
Elastase
Carboxypeptidase A
Carboxypeptidase B
ProCarboxypeptidase A.
ProCarboxypeptidase B.
A= (Ala,lle,Leu, Val, NH2)
trypsin
B= (Arg, Lys, NH2)
Carboxypeptidase A.
Carboxypeptidase B.
Digestion of oligopeptides by enzymes
of the small intestine

The luminnal surface of the intestine
contains aminopeptidase – an exopeptidase
that repeatedly cleaves the N-terminal
residue from oligopeptides to produce free
amino acids and smaller peptides.