MEDICAL NUTRITION PROTEIN METABOLISM

Astari Ridhanya - 1206289243

PROTEIN METABOLISM
Body protein is made up of 20 different amino acids, each with
different metabolic fates in the body, with different activities in
different metabolic pathways in different organs, and with differing
compositions in different proteins. When amino acids are liberated
after absorption of dietary protein, the body makes a complex series
of decisions concerning the fate of those amino acids: to oxidize
them for energy, to incorporate them into proteins in the body, or to
use them in the formation of a number of other N-containing
compounds. The purpose of this chapter is to elucidate the complex
pathways and roles amino acids play in the body, with a focus on
nutrition.
Protein digestion occurs in the stomach and the small intestine.
Reaction arrows are in red. The enzymes involved are in italics
and label the relevant reaction arrows. The activation of enzymes
are indicated by black arrows.
Protein Digestion in the Stomach

Pepsinogen, the inactive form of pepsin, is secreted (solid-headed

dashed arrow) by chief cells (labeled circle) that line the gastric
glands. This enzyme is activated (black reaction arrow) by
hydrogen ions, H+. These ions are from the hydrochloric acid
secreted (solid-headed dashed arrow) by parietal cells that also
line the gastric glands.
Proteins are long chains of amino acids. The enzyme pepsin
hydrolyzes

proteins

into

fragments

of

various

sizes

called

peptides; some amino acids are also produced in this manner.

This indicated by the red reaction arrow.
The factors listed below determine the period of time required by
the enzymes to breakdown the proteins:
Concentration of the enzyme
Quantity of protein to be disintegrated
Acidity of the stomach and food
Temperature of the food
Time of the day when the food is ingested
Antacids or other substances that may inhibit digestion
Protein Digestion in the Small Intestine

Hydrolysis of peptides from the stomach continues by the action of

three 'proteases' secreted (solid-headed arrows) in pancreatic
juice. These 'proteases' are inactive until they reach the lumen of
the

small

intestine;

chymotrypsinogen,

and

they

are

trypsinogen.

procarboxypeptidase,
Their

activations

are

indicated by the black reaction arrows.

The enzyme enterokinase is membrane-bound along the lining of
this region of the small intestine. It converts trypsinogen into its
active form trypsin. Trypsin catalyzes the conversion of both
procarboxypeptidase and chymotrypsinogen into their active
forms, carboxypeptidase and chymotrypsin, respectively. These
are represented by the black reaction arrows with 'trypsin' written
atop them.
The enzyme chymotrypsin, like pepsin, hydrolyzes peptides in
various size smaller amino acid chains finally producing dipeptides
& tripeptides. Carboxypeptidase specifically hydrolyzes the
amino acid from the carboxyl end of peptide chains to yield
individual amino acids. These reactions are indicated by red

reaction arrows.
Amino acids are transported through the cells lining the small
intestine and into the blood. The small peptides are transported into
the cells lining the small intestine where intracellular peptidases
(labeled outside symbolic GI tract) convert them into amino acids
that then enter the blood.
Absorption of amino acids
One thing that needs to be taken into consideration is that the
protein source greatly influences the amount of time required by
individual amino acids to be absorbed. For instance, amino acids
from soy and milk proteins are digested differently. In addition, there
are differences between individual types of milk protein. The
absorption of milk proteins is:
50 percent of the digested protein between the stomach and
the jejunum (middle section of the small intestine)
90 percent when the digested food gets in the ileum (final
segment of the small intestine)