Unit 2 – Enzymes and the

Digestive System
2.1 – Enzymes and Digestion

Digestive system is made up of a long muscular tube and its

associated glands. These glands produce enzymes that break down
large insoluble molecules, into small soluble ones ready for
absorption.

Ingestion  Digestion  Absorption  Assimilation  Egestion

What is Digestion?
Digestion is the process in which large molecules are
hydrolysed by enzymes into small molecules which can be
absorbed and assimilated.

In humans, digestion takes place in two stages:

1. Physical breakdown
2. Chemical digestion

Physical Breakdown
Food is taken into the body via ingestion. The teeth break down
food. This makes it possible to ingest food and also provides a larger
surface area for chemical digestion.
Food is then churned by the muscles in the stomach wall, which also
physically breaks it down.

Chemical Breakdown
Enzymes (hydrolases) break down large insoluble molecules into
smaller soluble ones, via hydrolysis. Different enzymes break down
different molecules and so often more than one enzyme is needed
to break down a large molecule. Usually one enzyme splits the
molecule into sections, and these sections are then hydrolysed by
additional enzymes.

Carbohydrases – carbohydrates  monosaccharides

Lipases – lipids (fats and oils)  fatty acids and glycerol
Proteases – proteins  amino acids

Once large molecules have been broken down, they are absorbed
from the small intestine into the blood via diffusion or active
transport. They are carried to different parts of the body, and often
built up again into large molecules. These molecules are then
incorporated into body tissues and/or used in processes within the
body (assimilation).
Any undigested food (cellulose) is then egested in faeces via the
anus.
2.2 – Carbohydrates – monosaccharides

Carbohydrates = organic molecules (they contain carbon and

hydrogen)
Some molecules are large and some are small
Sugars – small molecules (fructose, glucose, sucrose, lactose,
maltose)
Starch – large molecules (polymers)

Many organic molecules, such as carbohydrates, are made up of a

chain of individual molecules, called monomers. The carbon atoms
of the monomers join up to make longer chains, called polymers.

Monomers ( simple units )  Polymers

Most polymers are made up of four elements: carbon, hydrogen,

nitrogen and oxygen.

In carbohydrates, the monomer unit is a sugar (aka. saccharide). A

single monomer is therefore called a monosaccharide (eg. Glucose
and fructose). Pair of monosaccharides makes a disaccharide (eg.
Sucrose, maltose and lactose). Many monomers can be combined to
make polysaccharides (eg. Starch, glycogen and cellulose).

Starch = polymer of α -glucose

Glycogen = polymer of α -glucose
Cellulose = polymer of β -glucose

Monosaccharides
Sweet-tasting, soluble substances that have the general formula
(CH2o)n where n can be any number from 3 to 7.

Glucose is a monosaccharide. It is a hexose (6-carbon) sugar with

the formula C6H12O6 .

α -glucose β -
glucose
OH = Hydroxyl group

α -glucose and β -glucose are isomers (same molecular formula but

different arrangement of atoms / groups)
2.3 – Carbohydrates – disaccharides and
polysaccharides

Disaccharides
Maltose – glucose + glucose
Sucrose – glucose + fructose
Lactose – glucose + galactose

Monosaccharides join in a condensation reaction – a molecule of

water is removed. This forms a glycosidic bond.

Disaccharides are broken in hydrolysis – a molecule of water is

added. This breaks the glycosidic bond.

Polysaccharides
Polysaccharides are polymers, formed by combining together many
monosaccharides molecules by condensation reactions.
Polysaccharides are very large molecules, and are insoluble. This
makes them suitable for storage e.g. starch in plants.

Polysaccharides break down into disaccharides and

monosaccharides.
2.4 – Carbohydrate Digestion

Starch Digestion
More than one enzyme is usually needed to break down the large
polymer into its monomers. These enzymes are produced at
different parts of the digestive system – due to differing pHs in the
body.

Amylase – produced in the mouth and pancreas. Amylase

hydrolyses the alternate glycosidic bonds of the starch molecule to
produce the disaccharide maltose.
Maltase – produced by the lining of the intestine. Maltase
hydrolyses maltose into the monosaccharide α -glucose.

Ingestion  physical breakdown  saliva enters mouth  salivary

amylase hydrolyses starch into maltose  food enters stomach 
acid pH denatures amylase, prevent further hydrolysis of starch 
food passes into small intestine and mixes with pancreatic fluid 
pancreatic amylase in the juice hydrolyses remaining starch into
maltose  food is pushed along the small intestine  epithelial
lining of small intestine produces maltase  maltase hydrolyses the
maltose into α -glucose  absorption  assimilation  egestion

Disaccharide Digestion
Sucrose
Sucrose is contained within cells and these must be physically
broken down by teeth in order to release it. Sucrose is broken down
by sucrase, which is produced by the epithelial lining in the small
intestine.
Sucrose  glucose and fructose

Lactose
A sugar found in milk and milk products. Digested by lactase, which
is produced by the epithelial lining in the small intestine.
Lactose  glucose and galactose
2.5 - Proteins

Very large molecules made up by different combinations of 20

amino acids.
They have a tertiary structure, and a complex 3D globular shape.

Protein Structure
Amino acids are the basic monomer units, which make up a polymer
called polypeptide. Polypeptides can be combined to form proteins.
About 100 amino acids have been identified, of which 20 occur
naturally in proteins.

Every amino acid has a central carbon atom attached four different
chemical groups:
1. Amino group (NH2) -
2. Carboxyl group (COOH)
3. Hydrogen atom (H)
4. R group – a variety of different
chemical groups. This changes the
amino acid.

Formation of a Peptide Bond

Amino acid monomers can combine to form dipeptides by a
condensation reaction. The –OH group from the carboxyl group in
the amino acid combines with an –H from the amino group of
another amino acid. A peptide bond is produced between the carbon
atom of one amino acid and the nitrogen of the other.
Peptide bonds can also be broken by hydrolysis.

The Primary Structure of Proteins – Polypeptides

Polymerisation – many amino acid monomers joined together by a
series of condensation reactions.
The resulting chain of many hundreds of amino acids is called a
polypeptide. The sequence of amino acids in this chain forms the
primary structure of any protein.
It is the primary structure that determines its ultimate shape and
hence its function – a change of a single amino acid can lead to a
change of shape of the protein and may stop it functioning.

The Secondary Structure of Proteins

The linked amino acids that make up the polypeptide, both have –
NH and –C=O groups on either side of every peptide bond. The
hydrogen of the –NH group has an overall positive charge, while the
O of the –C=O group has an overall negative charge. These two
groups attract slightly, forming a weak hydrogen bond. This causes
the ling polypeptide chain to twist into a 3D shape, such as an α -
helix.

Tertiary Structure
The α -helices of the secondary structure can be twisted and folded
more to give the complex, and often unique 3D structure of each
protein. This is the tertiary structure, which is maintained by
different bonds:
• Disulfide bonds – formed between two sulphur-containing
cysteine side chains. Fairly strong and not easily broken down.
• Ionic bonds – formed between the carboxyl and amino
groups that are not involved in peptide bonds. They are
weaker than disulfide bonds and are easily broken by changes
in pH.
• Hydrogen bonds – numerous between R-groups, but easily
broken

The 3D structure is important when it comes to how the protein

functions.

Quaternary Structure
Large proteins often form complex molecules containing a number
of individual polypeptide chains, linked in various ways. There may
also be non-protein (prosthetic) groups associated with the
molecules, such as the iron-containing haem group in haemoglobin.

Protein Shape and Function

Protein roles in living organisms depends on their molecular shape,
which can be of two types:
1. Fibrous proteins – have structural functions (e.g. collagen)
2. Globular proteins – carry out metabolic functions (e.g.
enzymes and haemoglobin)

The proteins structure and shape enables them to carry out their
functions.

Fibrous Proteins:
Form long chains, which run parallel to each other. These chains are
linked by cross-bridges - so form very stable molecules. One
example is collagen:
• Primary structure – un-branched polypeptide chain
• Secondary structure – polypeptide chain is very tightly wound
• Tertiary structure – the chain is twisted into a second helix
• Quaternary structure – 3 polypeptide chains wound together
 like a rope

Collagen is found in tendons, joining muscles to bones. When a

muscle contracts, the bone is pulled in the direction of the
contraction. The points where one collagen molecule ends and the
next begin are spread throughout the fibre to increase strength.

2.6 – Enzyme Action

Enzymes are globular proteins that act as catalysts. Catalysts alter

the rate of a chemical reaction without undergoing permanent
changes themselves. This means they can be reused repeatedly and
are effective in small amounts. Enzymes simply alter the speed of
reactions.

Enzymes Lowering Activation Energy

Sucrose + water  glucose + fructose

For this reaction to take place:

• The substrate molecules must collide with enough energy to
alter the arrangement of their atoms to form the products
• The energy of the product must be less than that of the
substrates
• There is enough activation energy – the initial energy needed
to start the reation

Enzymes work by lowering the activation energy level. This allows

reactions to happen at a lower temperature.

Enzyme Structure
Enzymes are globular proteins with a specific 3D shape that is a
result of their primary protein structure). Enzymes contain an active
site, made up of relatively small number of amino acids.
The molecule on which the enzyme acts is the substrate. When this
substrate fits into the enzyme, an enzyme-substrate complex is
formed. This complex is held together by temporary bonds, which
form between the certain amino acids of the active site and groups
on the substrate molecule.

Lock and Key Model

A substrate will only fit the active site of one particular enzyme. This
model is supported in the observation that enzymes are specific in
the reactions that they catalyse. The shape of the substrate exactly
fits the active site of the enzyme because they have complementary
shapes.
Limitation – the enzyme is considered to be a rigid structure.
However, scientists had observed that other molecules could bind to
enzymes at sites other than the active site and in doing so, altered
the activity of the enzyme. This suggested that binding molecules
could alter the shape of the enzyme, showing that its structure was
infact flexible.

Induced Fit Model

The enzyme changes its shape slightly to fit the profile of the
substrate. The enzyme has a certain general shape, which changes
shape slightly in the presence of a substrate. As it changes its
shape, the enzyme puts strain on the substrate molecule which
distorts a particular bond, consequently lowering the activation
energy needed to break the bond.

It is better than the lock and key because it explains:

• How other molecules can affect enzyme activity
• How the activation energy is lowered
2.7 – Factors Affecting Enzyme Action

For an enzyme to work, it must:

• Come into physical contact with its substrate
• Have an active site with fits the substrate

Effect of Temperature
A rise in temperature increases the kinetic energy of the molecules.
This makes the molecules move around more rapidly and collide
more often. This means the enzymes and substrates come into
contact more often in a given time and so the rate of reaction
increases.
After its optimum temperature, the bonds on the enzyme molecule
start to break, causing the enzyme to change shape. At some point
the enzyme is denatured, causing it to be so disrupted that it stops
working all together.

Effect of pH
The pH of a solution is a measure of its hydrogen ion concentration.
A change in pH alters the charges on the amino acids that make up
the active site of the enzyme. As a result, the substrate can no
longer become attached to the active site and so an enzyme-
substrate complex cannot be formed.
A change in pH can cause the bonds in the enzyme’s tertiary
structure to break, therefore changing its shape. This can alter the
shape of the active site and denature the enzyme.

The arrangement of the active site is partially determined by the

hydrogen and ionic bonds between –NH2 and –COOH groups of the
polypeptides that make up the enzyme. The change in H+ ions
affect this bonding causing the active site to change shape.