DIGESTION

Definition: Many of the inorganic components of food are in the form of large insoluble
molecules which have to be broken down into simpler compounds before they can pass
through the mucous membrane of the alimentary canal into the blood and lymph.

The breaking- down process is termed ‘digestion’, the passage of the digested nutrients through
the mucous membrane ‘absorption’.

The Alimentary Canal:

AC can be considered as a tube extending from mouth to anus, lined with mucous membrane,
whose function is the ingestion, comminution, digestion and absorption of food, and elimination
of solid waste material. The various parts are mouth, pharynx, oesophagus, stomach, small and
large intestine.

The movement of the intestinal contents along the tract is produced by peristaltic waves, which
are contractions of the circular muscle of the intestinal wall.

The small intestine is the main absorption site and contains a series of microscopic finger-like
projections, the villi, which greatly increase the surface area available for absorption of nutrients.
Each villus contains an arteriole and venule, together with a drainage tube of the lymphatic
system, a lacteal. The venules ultimately drain into the portal system, and the lacteals into the
thoracic lymphatic duct.

Digestion in the Mouth

--mainly mechanical: mastication and to mix with saliva which acts as a lubricant. The saliva is
secreted into the mouth by three pairs of salivary glands: the parotids, which are sited in front of
each ear, the sub-maxillary glands, which lie on each side of the lower jaw; and the sublingual
glands, which are underneath the tongue.

Saliva is about 99% water, the remaining 1% consisting of mucin, inorganic salts and other
enzymes – α-amylase and the complex lysozyme

Ptyalin hydrolyse starch /glycogen to maltose and dextrins at the α-1,4-glycosidic bonds to form
maltose

Starch and glycogen require another enzyme to hydrolyse the α-1,6-glycosidic bonds to ensure
full hydrolysis.

Some anions acts as activation of ptyalin e.g: Cl-, Br-, I-, NO- PO43-.

Ptyalin seems to have a stronger action on cooked starch than on raw carbohydrates but this only
occurs in vitro. In the mouth there is usually no difference in its action.. This is because of the
presence of ions which affects its activity. Two major anions that aid its activity are Cl- and
HCO3-. Other anions include Br, NO- I- etc. Its activity is decreased by low pH

Salivary lipase

In the salivary secretion, there is a fat digesting enzyme, salivary (lingual) lipase. This
hydrolyses about 30% of total oil (fat0 ingested-----

----hydrolyses dietary triacylglycerols (triglycerides) (TAG) to glycerol and fatty acids or

2’monoacyglycerol.

Digestion in the Stomach

Gastric juices: presence of

--enzyme precursor :- pepsinogen and in small quantities pro-rennin and lipase

--- free HCl

---Inorganic chloride, lactic acid

--phosphates

HCl

 Produced by the oxyntic cells

 Activates pepsinogen to active enzyme, pepsin and the pro-rennin to yield rennin

 Lowers pH to 1.5-2.0

 Hydrolysis of sucrose to glucose and fructose

 Splits the nucleoproteins of the food into nucleic acid and protein.

Pepsin

 An endopeptidase

 Hydrolysis of proteins to peptones and some few amino acids

 Pepsin attacks the peptide bonds at the phenyl group (NH3 of tyrosine and
phenylalanine) of amino acids to yield phenolic acids

 It activates other peptidases such as trypsinogen to trypsin, chemotrypsinogen to

chymotrypsin to their active states

Rennin
 Found in suckling mammals

 Clots milk

 Precursor pro-rennin activated by intestinal enterokinsase

 Conversion of milk protein (soluble caseinogen) by H+ to the insoluble Ca salt of casein in

the presence of Ca2+ ions so forming curd.

Digestion in the Duodenum

-Pancreatic juice secreted by the pancrease; produced by the acini cells of the pancrease

Contains trypsin as trypsinogen (zymogen)

Zymogen: Secreted in its inactive form trypsinogen to prevent auto-digestion since it acts
on protein molecules – to avoid autocatalysis- attacking the pancrease.

Trypsinogen is activated to the enzyme trypsin by enterokinase

Trypsin:

 An endopeptidase and a serine protease. It has the amino acid aspartate at its active site,

 Hence attacks all proteins, preferentially action on those peptide linkages involving the
carboxyl group of either basic amino acids- lysine (and/or arginine) and phenylalanine or
tyrosin) residues.

 Involved in the activation of many digestive enzymes from their inactive to their active state.
These include proelastase to elastase, chymotrypsinogen to chymotrypsin, procarboxylase to
carboxylase. Its pH is about 7.5 – 8.8 due to the presence of NaHCO3.

Chymotrypsin:

 -also an endopeptidase, preferentially acting on the carboxyl linkages of phenylalanine or

tyrosine, specific for peptide bonds containing uncharged amino acid residues such as
aromatic amino acids

 Activated by active trypsin

Elastase:

 Has broad specificity in attacking bonds next to small amino acid residues such as
glycine, alanine and serine.

 Hydrolyses fibrous proteins

Collagenase

 hydrolyzes collagen

Pancreatic Amylase – amylopsin

 - hydrolyzes branching polysaccs to form maltose and higher oligosaccs containing α-

1,4- linkages, isomaltose (α -1,6-linkages) and small amounts of glucose.

The amylase finishes the work begun by ptyalin and thus all starch and glycogen are converted to
maltose.

 α -1,6 branches requires further hydrolysis by α-dextrinase or isomaltase

Pancreatic Lipase

 ---glyceride hydrolyzing enzyme otherwise called carboxyesterase

 --hydrolyzes fats to fatty acids and glycerol

Its hydrolyzing activity increases with:

i. Mol.wt. of the component fatty acid

ii. Extent of unsaturation

iii. The number of fatty acids in the molecule of the glyceride

The conditions in the intestine are never optimal for digestion of ingested fat so that the resulting
mixture usually consists of undigested fat (TAGs), diglycerides, monoglycerides and some
depending on a number of circumstances:- quantity of the ingested fat, its nature, pH and
motility of the bowel.

Bile

secreted by the liver, stored in the gall bladder; contains a number of bile acids:- Sodium
glycocholate, sodium taurocholate, also: bile pigments, bilirubin and biliverdin, some mucin,
cholesterol.

Bile acids are end products of cholesterol breakdown and thus a major rout of elimination of
cholesterol from the body, via the feces.

The bile salts have the property of considerably reducing the surface tension at fat-water
interfaces, and therefore make emulsification of fats a much simpler process- enabling lipase to
work more rapidly.

If fat droplets are small enough, they can be absorbed directly.

Clinical Significance of Bile Acids

1. Their synthesis and subsequent excretion in the faeces represent the only significant
mechanism for the elimination of excess cholesterol.

2. Bile acids and phospholipids solubilize cholesterol in the bile, thereby preventing the
precipitation of cholesterol in the gall bladder.

3. They facilitate the digestion of dietary TAG by acting as emulsifying agents that render
fats accessible to pancreatic lipase.

4. They facilitate the intestinal absorption of fat soluble vitamins

Digestion in the Small Intestine

The intestinal juice secreted by the glands of Brunner and Lieberkūhn also contain digestive
enzymes. The major site of CHO digestion is in the Small intestine, where another α-amylase –
like enzyme called amylopsin contains the cleave the remainder of the α-1,4- glucosidic
linkages: Any residual α-1,6-glucosidic linkages are split by an α-1,6-glucosidase, which also is
active in the small intestine.

1. Aminopeptidase: attack peptide bonds next to N- terminal amino acids of polypeptides

and oligopeptides.

---dipeptidases of various specificity: completes digestion of dipeptides to free amino

acids.

2. Disaccharidases and oligosaccharidases: α-glucosidase (maltase) which removes single

glucose residues from α - (1-4) linked oligosaccharides and disaccharides, starting from
non- reducing ends.

 Lactase – lactose to glucose + galactose

 Sucrase - hydrolyse sucrose to glucose + fructose

 Maltase – maltose to glucose

3. Phosphotase - removes phosphate from certain organic phosphates from certain organic
phosphates such as hexose-phosphates, glycerophosphate, and the nucleotides derived
from the diet and the digestion of nucleic acids by nucleases.

4. Polynucleotidases which split nucleic acids into nucleotides

 5. Nucleosidases – catalyze the phosphorolysis of nucleosides to give the free nitrogen base
plus a pentose phosphate.

6. Phospholipase that attacks phospholipids to produce glycerol, fatty acids, phosphoric

acid, and bases such as choline.

-Lecithin: oleic, palmitic, choline & P

- Cephalin: oleic, palmitic, aminoethanol

- Cephalin: oleic, palmitic, serine

7. Cholesterol Esterase; in the pancreatic juice hydrolyses cholesterol esters, bile acids as
co-factors

Digestion in the Large Intestine

In man no digestion takes place, except intestinal putrefaction and fermentation

--absorption of water takes place, and the semiliquid intestinal contents gradually become
more solid. During this period considerable bacterial activity occurs.

 By ferment/putrefaction, the bacteria release various gases:- CO2, methane, hydrogen,

nitrogen, and H2S as well as acetic, lactic and butyric acids

 Some nutritional benefits is derived from bacterial activity in the synthesis of certain
vitamins, particularly vits K, B12 and possibly other members of the B- complex,
which are made available to the body.

Digestion of Nucleo-protein

Like polysaccharides and proteins, nucleic acids are high- mol wt. polymers made up of
monomeric units, nucleotides. Nucleic acids may be therefore be referred to also as
polynucleotides. These nucleotides may be ultimately hydrolyzed into simpler subunits.

1. A nitrogen-containing ring compound with basic properties,

2. A pentose sugar

3. Phosphoric acid.

An intermediate product of hydrolysis is nucleoside which is a combination of the N-base with

the pentose sugar.
The nucleic acids DNA and RNA are hydrolysed by the polynucleotidases – deoxyribonuclease
(DNase) and ribonuclease (RNase) respectively.

The enzymes catalyze the cleavage of the ester bonds between the sugar and phosphoric acid in
the nucleic acids.

The end products are the component nucleotides

Nucleosidases attack the linkage between the sugar and nitrogenous bases, liberating the free
purines and pyrimidines.

Phosphotases complete the hydrolysis by separating the orthophosphoric acid from the ribose or
deoxyribose