DIGESTION AND ABSORPTION OF

PROTEINS
SELECTED TOPICS IN GIT PHYSIOLOGY
HPHY 306

Prof. M.I.A. SALEH

Group 7

Saturday, January 29, 2022

SYNOPSIS

 Introduction
 Digestion
 Absorption
 Functions
 Disorders
 INTRODUCTION TO PROTEINS

• Proteins are formed from multiple amino acids that are

bound together by peptide linkages.
• They constitute part of the major foods on which the body
lives on.
• Generally they cannot be absorbed in their natural forms
through the gastrointestinal mucosa and, for this reason,
are useless as nutrients without preliminary digestion.
• Digestion of proteins occurs by hydrolysis.
Digestion Of Proteins

• The digestion of proteins begins in the stomach with the

action of pepsin and is completed in the small intestine
with pancreatic and brush-border proteases.
• Proteases are enzymes that break down the peptide
bonds of proteins.
• The two classes of proteases are endopeptides and
exopeptides.
• Endopeptidases hydrolyze the interior peptide bonds of
proteins.
• The endopeptidases of the gastrointestinal tract are
pepsin, trypsin, chymotrypsin and elastase.
• Exopeptidases hydrolyze one amino acid at a time from
the carboxyl-terminal ends of proteins and peptides.
• The exopeptidases of the gastrointestinal tracts are
carboxypeptides A and carboxypeptides B.
Digestion Of Proteins In The Stomach
• Protein digestion in the stomach begins with the action of
pepsin.
• Pepsinogen, the inactive precursor of pepsin is secreted
by the gastric parietal cells.
• At low (acidic) pH, pepsinogen is activated to pepsin.
• Pepsin is most active a a pH of 2.0 to 3.0
• Pepsin cleaves some of the peptide linkages of proteins,
so the products of peptic digestion are polypeptides of
various sizes
• Peptic digestion only accounts for 10-20% of protein
digestion.
• Pepsin action is terminated in the duodenum, where
pancreatic HCO-3 secretions neutralize gastric acidity and
increase the pH.
Digestion In The Small Intestine
• In the small intestine, the polypeptides formed by digestion
in the stomach are further digested by the proteolytic
enzymes of the pancreas and intestinal mucosa.
• Five major pancreatic proteases are secreted as inactive
precursors: trypsinogen, chymotrypsinogen, proelastase,
procarboxypeptidase A and procarboxypeptidase B.
• Trypsinogen is activated to its active form, trypsin by the
brush border enzyme; Enterokinase.
• Trypsin then converts chymotrypsinogen, proelastase, and
procarboxypeptidase A and B to their active forms.
• Trypsinogen is also auto-catalyzed by trypsin to form more
trypsin.
• Trypsin, chymotrypsin, elastase split the interior peptide bond
in the peptide molecules into smaller polypeptides.
• Carboxypeptidase A and carboxypeptidase B hydrolyze
peptide bonds adjacent to the carboxy terminus, thereby
resulting in the release of individual amino acids.
• Only a small percentage of the proteins are digested all the
way to their constituent amino acids by the pancreatic juices.
• Most remain as dipeptides and tripeptides.
Absorption Of Proteins

• Stomach plays a negligible role in the absorption of

protein digestion products.
• The small intestine is the principal site of protein
absorption.
• The products of protein digestion are amino acids,
dipeptides, and tripeptides.
• Each form can be absorbed by intestinal epithelial cells.
• The amino acids are transported from the lumen into the
cell by Na+amino acid cotransporters in the apical
membrane.
• The dipeptides and tripeptides are transported from the
intestinal lumen into the cell by separate H+ dependent co
transporters in the apical membrane.
• Once inside the cell, most of the dipeptides and tripeptides
are hydrolyzed to amino acids by cytosolic peptidases,
producing amino acids that exit the cell by facilitated
diffusion.
• The remaining dipeptides and tripeptides are absorbed
unchanged.
Functions of proteins

• The following are some of the biomedical importance of

proteins;
• Proteins are the main structural components of the
cytoskeleton. They are the sole source to replace
Nitrogen of the body.
• Biochemical catalysts known as enzymes are proteins.
• Proteins known as immunoglobulins serve as the first line
of defence against infection.
• Several hormones are protein in nature
Disorders of Protein Digestion and Absorption

• Disorders of protein digestion or absorption occur when

there is a deficiency of pancreatic enzymes or when there
is a defect in the transporters of the intestinal epithelial
cells. They include;
• Cystinuria: is a genetic disorder in which the transporter
for the dibasic amino acids cystine, lysine, arginine, and
ornithine is absent in both the small intestine and the
kidney.The intestinal defect results in failure to absorb the
amino acids, which are excreted in feces.
• Chronic pancreatitis: This is the inflammation of the
pancreas.There is a deficiency of all pancreatic enzymes
including the proteases. Dietary protein cannot be
absorbed if it is not digested by proteases to amino acids,
dipeptides, and tripeptides.
 References
• V.Ganapathy, Y.D.Bhutia, Digestion and absorbtion of
proteins (2018) page;1063-1065
• Guyton and Hall, 2014. page 808-810
• Costanzo. Physiology, sixth edition. page 377-380
• Ganong’s Review. 26th Edition, page 1101-1105
• WF.Boron, E.L.Boulpaep. Medical Physiology, A Cellullar
and Molecular Approach. page 956-957.
 ARIGATO
GOZAIMASU