Proteins their Digestion & Absorptions,

Catabolism of protein, Protein turnover,.

Nitrogen balance, Transamination,
Protein Degradation

ADIL JAMAL (M.Phil, PhD)

Assistant Professor
College of Nursing, Umm Al Qura University
Email: adiljamalcemb@gmail.com
Introduction

Proteins subjected to digestion & absorption obtained from 2

sources i.e Dietary & Endogenous

The intake of dietary protein is 50-100 g/day.

About 30-100 g/day of endogenous protein is derived from digestive

enzymes & worn out cells of digestive tract.

Digestion & absorption of proteins is very efficient in healthy

humans, hence very little protein (5-10 g/day) is lost through feces.
Introduction Cont’d

Dietary proteins are denatured on cooking & therefore easily

digested.
Proteins are degraded by class of enzymes namely hydrolases
which especially cleave the peptide bonds, hence known as
peptidases.

1. Endopeptidases. Which attack the internal peptide bonds &

release peptide fragments e.g Pepsin, Trypsin.

2. Exopeptidases. Which act on peptide bonds of terminal

amino acids. Exopeptidases are subdivided into
carboxypeptidases (act on c-terminal) & aminopeptidases
(act on N terminal)
 I. Digestion of proteins by gastric secretion
Protein digestion begins in the stomach, not in mouth due to absence of
proteases. Gastric juice produced by stomach contains HCl & protease
proenzyme namely pepsinogen.

HCl: The pH of stomach is <2 due to presence of HCl secreted by

parietal cells of gastric glands. HCl performs 2 imp functions –
denaturation of protein & killing of certain microorganisms.

Pepsin: Pepsin is produced by serous cells of stomach as pepsinogen

or proenzyme. Pepsinogen is converted to active pepsin either by
a. Autocatalysis brought about by other pepsin molecules
b. By gastric HCl
Pepsin digestion of proteins results in peptides & few amino acids.

Renin (Chymosin): This enzyme is found in the stomach of infants &

children. It is involved in curdling of milk. It converts milk protein casein
to Calcium paracaseinate which can be effectively digested by pepsin.
 II. Digestion of proteins by Pancreatic Proteases
The proteases of pancreatic juice are secreted as zymogens & then
converted to active forms. These processes are initiated by release of
2 polypeptide hormones, namely cholecystokinin & secretin.

Release & activation of zymogens: The key enzyme for activation of

zymogens is enteropeptidase produced by intestinal mucosal
epithelial cells. Trypsin in turn activates trypsinogen molecules.
Further trypsin is the common activator of all other pancreatic
zymogens to produce the active proteases.

Action of pancreatic proteases. Trypsin, chymotrypsin are

endopetidases & elastase are active at neutral pH. Gastric HCl is
neutralized by pancreatic NaHCO3 in the intestine & this creates
favorable pH for the action of proteases.

The Amino acid Serine is essential at the active centre to bring about
the catalysis of all 3 pancreatic proteases, hence these enzymes are
referred as Serine Proteases.
III. Digestion of proteins by Small Intestinal Enzymes

• The luminal surface of intestinal epithelial cells contains

aminopeptidases & dipeptidases.

• Aminopeptidase is a non specific exopeptidase which repeatedly

cleaves N terminal amino acids one by one to produce free amino
acids & smaller peptides.

• Dipeptidases act on different dipeptides to liberate amino acids.

 Absorption of Amino acids

The free amino acids, dipeptides & to some extent tripeptides are
absorbed by intestinal epithelial cells.

The di- & tripeptides after being absorbed are hydrolysed into free
amino acids in the cytosol of epithelial cells. The activities of
dipeptidases are high in these cells. Therefore, after a protein
meal, only the free amino acids are found in the portal vein.

The small intestine possesses an efficient system to absorb free

amino acids. L- amino acids are more rapidly absorbed than D-
amino acids.

The transport of L- amino acids occurs by an active process in

contrast to D- amino acids which takes place by simple diffusion.
 Essential & Non Essential Amino acids

Essential amino acids

Can’t be synthesized by body
It should be obtained from the diet therefore called essential amino
acids
Essential amino acids are Arginine, Histidine, Isoleucine, Leucine,
Lysine, Methionine, Phenylalanine, Threonine, Tryptophan & Valine.

Non Essential amino acids.

Can be synthesized in the body
Non essential amino acids are Alanine, Asparagine, Aspartate,
Cysteine. Gultamate, Glutamine, Glycine, Proline, Serine, Tyrosine.

Gultamate & Glutamine together constitute about 50% & essential

amino acids about 10% of the body pool.
 Sources of Amino acid pool –
Protein Turnover & Nitrogen Balance

Turnover of body protein, intake of dietary protein & the synthesis of

non essential amino acids contribute to amino acid pool.

Protein Turnover: The protein present in the body is in dynamic state.

About 300-400 g of protein/ day is constantly degraded & synthesized
which represents body protein turnover.
There is wide variation in the turnover of individual proteins. For
instance the plasma proteins & digestive enzymes are rapidly
degraded, their half lives being in hours or days. The structural
protein (e.g collagen) have long half lives , often in months & years.

Control of protein turnover: The turnover of the protein is influenced

by many factors. Certain proteins with amino acids sequence proline,
glutamine, serine & threonine are rapidly degraded.
Overview of amino acid pool- sources & utilization
 Nitrogen Balance (Positive & Negative Nitrogen Balance )

There is regular loss of Nitrogen from the body due to degradation of

amino acids. In healthy adults it is estimated that about 30-50 g of
protein is lost everyday from body. This amount of protein (30-50 g)
must be supplied daily in the diet to maintain Nitrogen balance.
Nitrogen is a fundamental component of amino acids, which are the
molecular building blocks of protein. Therefore, measuring nitrogen
inputs and losses can be used to study protein metabolism.
Positive nitrogen balance
• is associated with periods of growth, hypothyroidism, tissue repair,
and pregnancy. This means that the intake of nitrogen into the body is
greater than the loss of nitrogen from the body, so there is an increase in the
total body pool of protein.
• Negative nitrogen balance is associated with burns, serious tissue
injuries, fevers, hyperthyroidism, wasting diseases, and during periods
of fasting. This means that the amount of nitrogen excreted from the body is
greater than the amount of nitrogen ingested. A negative nitrogen
balance can be used as part of a clinical evaluation of malnutrition
 Metabolism of Amino acids
• The amino acids undergo certain common reactions like
transamination followed by deamination for the liberation of
ammonia.

• The amino group for the amino acids is utilized for the formation of
urea which is an excretory end product of protein metabolism.

• The carbon skeleton of the amino acids is first converted to keto

acids (by transamination) which meets one or more of the following
fates.
• A . utilized to generate energy
• B. Used for the synthesis of glucose
• C. Involved in production of non-essential amino acids
• D. Diverted for the formation of fat or ketone bodies
An Overview of amino acid metabolism
 TRANSAMINATION
• The transfer of amino (-NH2) group from an amino acid to a keto
acid is known as Transamination.

• This process involves the interconversion of a pair of amino acids

and a pair of keto acids catalyzed by a group of enzymes called
Transaminases.
 Mechanism of Transamination
Transamination occurs in following 2 stages .
1. Transfer of the amino group to the coenzyme pyridoxal
phosphate (PLP) (bound to the coenzyme) to form
pyridoxamine phosphate.
2. The amino group of pyridoxamine phosphate is then transferred
to a keto acid to produce a new amino acid and the enzyme
with PLP is generated.

All the transaminases require pyridoxal phosphate, a derivative of

vitamin B6.
 B. Formation of enzyme PLP-
A. Mechanism of transamination
Schiff base and amino acids
Involvement of pyridoxial
PLP-Schiff base.
phosphate (PLP) in the transfer of
Note that when amino acid
amino group
binds, the enzyme separates
 DEAMINATION
• The removal of amino group from the amino acids as NH3 is
deamination.
• Transamination involves only the shuffling of amino groups among
the amino acids. On the other hand, deamination results in liberation
of ammonia for urea synthesis.
• Simultaneously, the carbon skeleton of amino acids is converted to
keto acids. Deamination may be either oxidative or non-oxidative.

Oxidative deamination: it is the liberation of free ammonia from the

amino group of amino acids coupled with oxidation in presence of
amino acid oxidase enzyme. This takes place mostly in liver & kidney.
The purpose of oxidative deamination is to provide NH3 for urea
synthesis & keto acids for a variety of reactions, including energy
generation.

Non-oxidative deamination: some of the amino acids can be

deaminated to liberate NH3 without undergoing oxidation in presence
of dehydratase enzyme.
Protein degradation
• Protein degradation may take place intracellularly or extracellularly. In
digestion of food, digestive enzymes may be released into the
environment for extracellular digestion whereby proteolytic cleavage
breaks down proteins into smaller peptides and amino acids so that
they may be absorbed and used by an organism.

• In animals the food may be processed extracellularly in specialized

digestive organs or guts, but in many bacteria the food may be
internalized into the cell via phagocytosis. Microbial degradation of
protein in the environment can be regulated by nutrient availability.

• Proteins in cells are also constantly being broken down into amino
acids. This intracellular degradation of protein serves a number of
functions: It removes damaged and abnormal protein and prevent
their accumulation, and it also serves to regulate cellular processes
by removing enzymes and regulatory proteins that are no longer
needed. The amino acids may then be reused for protein synthesis.