Biochemistry Aspects of Gastrointestinal Tract

Digestion and Absorption of Proteins

Proteins are broken down by peptidases. Peptidase is divided into:

Endopeptidases (proteases), which attack internal bonds and liberate large peptide fragments.
Exopeptidases, which cleave off one amino acid at a time from either the COOH (carboxypeptidases) or
the

NH 2 terminus (aminopeptidases).

Endopeptidases are important for an initial breakdown of long polypeptides into smaller products, which
can then be attacked more efficiently by exopeptidases. The final products are free amino acids and di and
tripeptides.
As we know most enzymes cant work optimally or it can be destroyed in an extreme pH. Pepsins are
unique in that they are acid stable. Active pepsin is generated from the proenzyme pepsinogen by the
removal of 44 amino acids from the

NH 2

terminus.

Cleavage between residues 44 and 45 of pepsinogen occurs as either an intramolecular reaction

(autoactivation) below pH 5 or by active pepsin (autocatalysis). The liberated peptide from the

NH 2

terminus remains bound to pepsin and acts as "pepsin. The major products of pepsin action are large peptide
fragments and some free amino acids.
Pancreatic juice is rich in proenzymes of endopeptidases and carboxypeptidases, which are activated after
they reach the lumen of the small intestine. Enteropeptidase, a protease produced by duodenal epithelial
cells, activates pancreatic trypsinogen to trypsin by scission of a hexapeptide from the

NH 2

terminus.

Trypsin in turn autocatalytically activates more trypsinogen to trypsin and also acts on the other
proenzymes.
Polypeptides generated from ingested proteins are degraded within the small intestinal lumen by
carboxypeptidases A and B. The pancreatic carboxypeptidases are

2+

Zn

metalloenzymes and possess a

different type of catalytic mechanism than the carboxyl or serine peptidases. The combined action of
pancreatic peptidases results in the formation of free amino acids and small peptides.
Digestion and Absorption of Carbohydrates
Starch, a major nutrient, is a plant polysaccharide with a molecular mass of more than 100 kDa. It consists
of a mixture of linear chains of glucose molecules linked by -1,4 glucosidic bonds (amylose) and of
branched chains with branch points made up by -1,6 linkages (amylopectin).

Hydrated starch and glycogen are attacked by the endosaccharidase, -amylase present in saliva and
pancreatic juice. Amylase is specific for internal -1,4 glucosidic bonds -1,6 bonds are not attacked, nor
are -1,4 bonds of glucose units that serve as branch points. The products of the digestion by a amylase are
mainly the disaccharide maltose, the trisaccharide maltotriose, and so called a limit dextrins containing on
average eight glucose units with one or more -1,6 glucosidic bonds.
Most of the surface oligosaccharidases are exoenzymes that cleave off one monosaccharide at a time. The
capacity of the -glucosidases is normally much greater than that needed for completion of the digestion of
starch.
Digestion and Absorption of Lipid
Triacylglycerols constitute more than 90% of the dietary fat. The rest is made up of phospholipids,
cholesterol, cholesterol esters, and free fatty acids. Digestion of lipids is initiated in the stomach by an acidstable lipase, most of which is thought to originate from glands at the back of the tongue. However, the rate
of hydrolysis is slow because the ingested triacylglycerols form a separate lipid phase with a limited water
lipid interface. The lipase adsorbs to that interface and converts triacylglycerols into fatty acids and
diacylglycerols.
The major enzyme for triacylglycerol hydrolysis is the pancreatic lipase. This enzyme is specific for esters
in the -position of glycerol and prefers long chain fatty acids with more than ten carbon atoms. Hydrolysis
by the pancreatic enzyme also occurs at the waterlipid interface of emulsion droplets. The products are
free fatty acids and -monoacylglycerols.

Devlins Textbook of Biochemistry with Clinical Correlations, 4th edition