Digestion and

absorption of Proteins
Dietary proteins serve 3functions

1. Their constitutent aminoacids are used for

synthesis of body proteins

2. The carbon skeletons of the amino acids are

oxidized to yield energy

3. Their carbon & nitrogen atoms may be used to

synthesize other ‘N’ containing cellular
constituents as well as many non-nitrogen
containing metabolites
Digestion takes place with the help of
enzymes secreted by

1. Stomach
2. Pancreas
3. Small Intestine
 1.Digestion in stomach

Entering proteins (+) gastrin (+) gastric juice (ph

1.5 – 2.5) containing
1. Hcl
2. Pepsinogen
3. Rennin (in infants)
 Hydrochloric Acid

• Secreted by parietal cells

• Kills micro-organisms
• Denatures protein making internal peptide
bonds more susceptible to subsequent
hydrolysis by proteoses
• Provides acid environment for pepsin action
 Pepsin
• Secreted by chief cells as pepsinogen
– inactive precursor
• Converted to active pepsin by high
hydrogen ion concentration
• Works at acidic pH
• Cleaves peptide bonds of aromatic &
acidic aa
 Rennin
• Chymosin
• Important in infants digestive process
• Clotting of milk

casein paracasein ca++paracaseinate

The purpose of this reaction is to convert milk into more

solid form to prevent the rapid passage of milk from
stomach of infants
2.Digestion in intestine by pancreatic enzymes

Acidic contents (chyme) passing into small

intestine triggers the secretion of
1. Secretin
2. Cholecystokinin
 Secretin

• Stimulates pancreas to secrete bicarbonate &

release of pancreatic juice into the small
intestine.
• Neutralises gastric Hcl changing pH from 1.5
– 7.0
 Cholecystokinin

• Stimulates secretion of pancreatic endopeptidase &

exopeptidase
• Endopeptidase includes chymotrypsin & elastase,
cleaving internal peptide bonds
• Exopeptidase cleaves aa from either ‘C’ or ‘N’
terminal end. Includes carboxypeptidase &
aminopeptidase
Activation Of Pancreatic Pro-enzymes

TRYPSINOGEN
ENTEROPEPTIDASE

TRYPSIN
CHYMOTRYPSINOGEN CHYMOTRYPSIN

PRO-ELASTASE ELASTASE

PROCARBOXYPEPTIDASE CARBOXYPEPTIDASE
• Trypsin – hydrolyses peptide bonds whose
carboxyl groups are contributed by lys & arg
residues

• Chymotrypsin-cleaves peptide bonds involving

carboxyl group of aromatic aa

• Elastase – hydrolyses those peptide bonds formed

by small non-polar aa residues such as ala, ser &
gly
 Degradation of short peptides in the small intestine
is continued by an exopepetidase-
carboxypeptidase which removes the successive
carboxy terminal aa residues from peptide

1. Carboxypeptidase A – releases hydrophobic aa

2. Carboxypeptidase B – releases basic aa
 3.Digestion in intestine by intestinal
proteoses
• The digestion is completed by the peptidases
of the mucosa of the small intestine namely:

1. Aminopeptidases
2. Group of dipeptidases
Amino-peptidase
- Exopeptidase
- Require Mg/Mn
- Hydrolyse peptide bonds next to N-terminal aa of
short peptides

Dipeptidases
- Complete the digestion of dipeptides to free amino acids
 Absorption of amino-acids

• Mostly through active transport

• 5 separate systems – transport amino-acids from intestinal

lumen into intestinal epithelial cells

• Thus aa released by digestion pass from gut through hepatic

portal vein to the liver

• Transport system also present in renal system

Transport System Aminoacid Disorder
Transported
Small neutral Ala Ser & Thr
aminoacids
Large neutral Isoleu, Leu, HARTNUP
aminoacids Val,Tyr,Trp,Phe Disease
Basic aa & Cystine Arg, Lys, CYSTINURIA
Ornithine, Cys
Acidic aminoacids Glutamic acid
Aspartic acid
Iminoacid, Glycine Pro, Hydroxy pro, GLYCINURIA
Gly
Thank You