Digestion and

Absorption of
Proteins
Assoc. Prof. S. Sibel Erdem
Istanbul Medipol University
International School of Medicine
 Objectives of X.
Committee
• Digestion and Absorption of Proteins
• Digestion and Absorption of Carbohydrates
• Digestion and Absorption of Lipids
• Porphyrin and Bile Chemistry
• Avitaminoses
• Liver Function Test

• LAB: Determination of Amylase in Serum

 Proteins
• Polymers of amino acids
• Contain about 16% nitrogen in addition to Carbon,
Hydrogen and Oxygen
• A 70 kg man has an average protein turnover rate of
400 g per day
• Intake of dietary protein is in the range of 50-100 g/day
• About 30-100 g/day of endogenous protein is derived
form the digestive enzymes and worn out cells of the
digestive tract
• The digestion and absorption of proteins is very
efficient in healthy humans, hence very little protein
(about 5-10 g/day) is lost through feces

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 Utilization of Amino
Acids
• Plasma protein formation.
• Formation of globin of Hb.
• Formation of protein hormones and
neurotransmitters.
• Formation of glucose
• Energy production
• NH3 and urea formation.
 Digestion
Digestion is considered as the degradation of the
nutrient molecules into components simple enough
to be subsequently absorbed in the intestine

Mechanical digestion: breaking food in small

particles so they are easily broken down by
enzymes mouth and stomach

Chemical digestion: pancreas and duodenum

Absorption is the uptake of digested components
by the intestinal cells(enterocytes).

Nutrient absorption: small intestine

Water reabsorption: large intestine

• Digestion occurs when certain enzymes are mixed
with the food.

The most important enzymatic

reaction in digestion of foodstuffs
is hydrolysis - the breaking of a
chemical bond by the addition of
a water molecule
 Enzymes Involved in Digestion
polysaccharides maltose glucose
Overview of metabolism
of amino acids
Digestion
of
Proteins
 • Endopeptidase : acts inside the core
Peptidases of protein, forms small peptide
(Proteolytic fragments
• Exopeptidase : acts from the amino
Enzymes)
terminal or carboxyl terminal ends
of protein

• Peptidases are secreted in the

Proenzymes inactive form
(zymogens) • When zymogens reach the site
of action they are activated
(intestinal lumen)
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Proteolytic enzymes of GIT are secreted by
three different organs

STOMACH

Pancreas

Intestine

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 A. Gastric Digestion of
Proteins
• Rennin: Rennin otherwise called Chymosin, is active
in infants and is involved in the curdling of milk.
• It is absent in adults.
• Rennin converts milk protein (casein) to paracasein
to be further digested by pepsin
 Digestion of Proteins Begins in Stomach

• Strong • Denatures proteins Activated to pepsin by

mineral acid • Decreases the pH HCl
HCl (pH 2 to 3) Acid Stable endopeptidase
• Activates
• Proenzyme pepsinogen
Pepsinogen
pepsinogen • Kills some bacteria
• Helps in the
Pepsinogen
absorption of
Vitamin B12
Pepsin Autocatalysis

Pepsin
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 The Stomach

Foodstuffs entering the stomach have been, crushed and

reduced in size by mastication with saliva. The muscular
walls of the stomach contract vigorously to mix food with
gastric juice, producing a mixture called chyme.

The stomach provides four basic functions that assist in

the early stages of digestion and prepare the food for
further processing in the small intestine:
 The Stomach
1. It serves as a short-term storage reservoir, allowing a
rather large meal to be consumed quickly and dealt with
over an extended period.
2. It is in the stomach that substantial chemical and
enzymatic digestion is initiated, particularly of
proteins.
3. Vigorous contractions of gastric smooth muscle mix and
grind foodstuffs with gastric secretions, resulting in
liquefaction of food.
4. As food is liquefied in the stomach, it is slowly released
into the small intestine for further processing.
Four major types of secretory epithelial cells cover the surface of
the stomach and extend down into gastric pits and glands:

1. Mucous cells: secrete an alkaline mucus

that protects the epithelium against shear
stress and acid
2. Parietal cells: secrete hydrochloric acid.
3. Chief cells: secrete pepsin, a proteolytic
enzyme
4. G cells: secrete the hormone gastrin
 Gastric secretions
1-Mucosal Protection
Mucus layer on gastric surface forms a mucosal barrier to
damage against several forms of potential injury to the
gastric mucosa.
1. A gel 0.2 mm thick; 80% carbohydrate; 20% protein
2. Can be cleaved by pepsin, so continual production is
required
3. Release is stimulated by acetylcholine from nerve endings
4. Also rich in bicarbonate
-
a. HCO3 content creates a "micro-environment" around
surface cells to prevent acid damage
-
b. HCO3 secretion is inhibited by adrenergic input
(prominent in stress)
 2-Acid Secretion
Hydrochloric acid is secreted from parietal cells into the lumen
where it establishes an extremely acidic environment.
This acid is important for activation of pepsinogen and
inactivation of ingested microorganisms such as bacteria.
Function of Gastric acid
1. To kill micro-organisms: (but H. pylori survives by making
ammonia (basic) from urea using urease).
2. To provide the optimal pH for pepsin action
3. To activate pepsinogens (cleaved to form pepsin)
4. Facilitating absorption of iron by converting colloidal iron into
ionic form.
5. Stimulating duodenum to liberate secretin
6. Breaks down connective tissue in food
 Gastric Digestion of
Proteins in Stomach
• Pepsin: It is secreted by the chief cells of stomach
as inactive pepsinogen
• The conversion of pepsinogen to pepsin is brought
about by removal of 44 amino acids from the N-
terminal end, by the HCl.
• The optimum pH for activity of pepsin is around 2.
• Pepsin is an endopeptidase.
 B. Pancreatic Digestion of
Duodenum
Proteins
• The duodenum is the first part of the small intestine.
• Chyme enters in tiny spurts. At this point, proteins and
carbohydrates are only partially digested and lipid
digestion has not begun.
 B. Pancreatic Digestion of
•
Proteins
Pancreas acts as an exocrine gland
by producing pancreatic juice which
empties into the small intestine via
duct.

• Alkaline bile and pancreatic juice are

secreted.

• The optimum pH for the activity of

pancreatic enzymes (pH 8)

• Pancreatic juice contains the

important endopeptidases, namely
Trypsin, Chymotrypsin, Elastase and
Carboxypeptidase and bicarbonate.
Digestive Enzymes of Pancreas
Proteases
Digestion of proteins is initiated by pepsin in the stomach, but
the bulk of protein digestion is due to the pancreatic proteases.
Several proteases are synthesized in the pancreas and secreted
into the lumen of the small intestine.

The two major pancreatic proteases are trypsin and

chymotrypsin both are endopeptidases, which are synthesized
and packaged into secretory vesicles as the inactive
proenzymes trypsinogen and chymotrypsinogen.
• Trypsin: Trypsinogen is
activated by
enterokinase

• Acute pancreatitis:
Premature activation of
trypsinogen inside the
pancreas itself will result in
the autodigestion of
pancreatic cells. The
result is acute
pancreatitis. It is a life-
threatening condition
 Once trypsinogen and chymotrypsinogen are released into the lumen of the
small intestine, they must be converted into their active forms in order to digest
proteins, Trypsinogen is activated by the enzyme enterokinase, which is
embedded in the intestinal mucosa.

Once trypsin is formed, it activates chymotrypsinogen, as well as additional molecules

of trypsinogen. The net result is a rather explosive appearance of active protease
once the pancreatic secretions reach the small intestine.
 Activation of Pancreatic Proteases
in the Duodenum

• Carboxypeptidases: Trypsin
and chymotrypsin degrade the
proteins into small peptides;
these are further hydrolysed
into dipeptides and tripeptides
by carboxypeptidases
• Pancreatic phase ends with some free amino acids and small peptides of
2-8 amino acid residues which account for 60% of protein digestion

Small UNCHARGED ALIPHATIC BASIC

intestine BASIC

Dietary
protein Trypsin Chymotrypsin Elastase

Enteropeptidase

Trypsinogen Chymotrypsinogen Proelastase

C. Digestion of Proteins in
Intestine
 Intestinal Digestion of
Proteins
Complete digestion of proteins to amino acids is
brought by enzymes:

• Leucine aminopeptidase,
• Proline amino peptidase,
• Dipeptidases
• Tripeptidases
 Small Intestine
The net effect of passage through
the small intestine is absorption of
most of the water and electrolytes
(sodium, chloride, potassium) and
essentially all dietary organic
molecules (including glucose,
amino acids and fatty acids).

Through these activities, the small

intestine not only provides nutrients
to the body, but plays a critical role
in water and acid-base balance.
 Absorption of Peptides
• There is virtually no absorption of peptides longer than four amino
acids.
• However, there is abundant absorption of di- and tripeptides in the
small intestine.
• These small peptides are absorbed into the small intestinal
epithelial cell by cotransport with H+ ions via a transporter

Absorption of Intact Proteins

“Normal" enterocytes do not have transporters to carry proteins
across the plasma membrane and they certainly cannot permeate
tight junctions.
 Absorption of intact
proteins and polypeptides
• Short period, immediately after birth, the small
intestine of infants can absorb intact proteins and
polypeptide by endocytosis or pinocytosis

• Intact proteins and polypeptides are not absorbed

by the adult intestine

• Macromolecular absorption in certain individuals

appears to be responsible for antibody formation
that often causes food allergy.
 ABSORPTION OF
AMINO ACIDS
• The absorption of amino acids occurs mainly in
the small intestine.

Amino acids are transported across the intestinal+

mucosa via various channels (need carrier, Na
pump, Na+ ions, ATP).

Different carrier transport systems are:

a) For neutral amino acids.
b ) For basic amino acids and cysteine.
c) For imino acids and glycine.
d) For acidic amino acids.
e) For B-amino acids (B-alanine)
 Metabolic Fates Of Amino Acids:
1- Body protein biosynthesis.
2- Small peptide biosynthesis(GSH).
3-Synthesis of non-protein nitrogenous (NPN)
compounds (creatine, urea, ammonia and uric acid)
4- Deamination & Transamination to synthesized a new
amino acid or glucose or ketone bodies or produce
energy in starvation.
 Amonia

• 1st step of catabolism of amino acids is to remove

the amino group as ammonia.
• This is the major source of ammonia. However, small
quantities of ammonia may also be formed from
catabolism of purine and pyrimidine bases.
• Ammonia is highly toxic especially to the nervous
system.
• Detoxification of ammonia is by conversion to urea
and excretion through urine.
HORMONES INVOLVED IN
DIGESTION
 1-Gastrin
The presence of food in the stomach stimulates specific
receptors which in turn stimulates endocrine cells in the
stomach to secrete the hormone gastrin into the circulatory
system.

Gastrin stimulates the stomach to secrete gastric juice.

This hormone, which is very similar to cholecystokinin, is

secreted in large amounts by the stomach in response to
gastric distention and irritation, in addition to stimulating
acid secretion by the parietal cell; gastrin stimulates
pancreatic acinar cells to secrete digestive enzymes.
 2-Secretin
Secretin is produced by cells of the duodenum.

It’s production is stimulated by acid chyme from stomach.

It stimulates the pancreas to produce sodium bicarbonate, which

neutralizes the acidic chyme.

It also stimulates the gallbladder to secrete bile.

This hormone is secreted in response to acid in the duodenum. The

predominant effect of secretin on the pancreas is to stimulate duct cells
to secrete water and bicarbonate. As soon as this occurs, the enzymes
secreted by the acinar cells are flushed out of the pancreas, through the
pancreatic duct into the duodenum. It also stimulates the liver to secrete
bile.
 3-CCK (cholecystokinin)
• CCK production is stimulated by the presence of food in
the duodenum. It stimulates the gallbladder to release
bile and the pancreas to produce pancreatic enzymes.
This hormone is synthesized and secreted by enteric
endocrine cells located in the duodenum. Its secretion is
strongly stimulated by the presence of partially digested
proteins and fats in the small intestine. As chyme floods
into the small intestine, cholecystokinin is released into
blood and binds to receptors on pancreatic acinar cells,
ordering them to secrete large quantities of digestive
enzymes. It also stimulates the gallbladder to release bile
and the pancreas to produce pancreatic enzymes.
Protein Malabsorption
Acute pancreatitis:
• Premature activation of trypsinogen inside the
pancreas itself will result in the autodigestion
of pancreatic cells

Celiac disease (celiac sprue)

Disease of malabsorption resulting from immune-
mediated damage to the small intestine in response
to ingestion of gluten (or gliadin produced from
gluten), a protein found in wheat and barley
Summary Slides