Chemical

Compounds in Cells

Elements

An element is any substance that cannot be

broken down into simpler substances.
The smallest unit of an element is an atom.
Example of an element is carbon.

Compounds

A compound is two or more elements that

are chemically combined.
The smallest unit of a compound is a
molecule.
An example of a compound is water.

ESSENTIAL ELEMENTS
MAJOR ELEMENTS
( 96% of the mass of
the human body

Carbon, C
Oxygen, O
Hydrogen, H
Nitrogen, N

OTHER ELEMENTS
(Remaining 4%)

Sulphur, S
Phosphorus, P
Calcium, Ca
Potassium, K
Magnesium, Mg
Chlorine, Cl
Sodium, Na
Iron, Fe

Organic and Inorganic Compounds

Organic compounds contain carbon and

hydrogen and usually are associated with
living things.
Inorganic compounds do not contain
carbon. Eg. water

Four groups of Organic Compounds

Carbohydrates
Proteins
Lipids
Nucleic Acids

Carbohydrates

Main source of energy in the cell

Made of the elements carbon, hydrogen, and
oxygen
As energy storage in animal cells in the form of
glycogen and starch in plant cells
Cellulose form the main constituent of cell walls
and dietary fibre

Proteins

Made of the elements carbon, oxygen, hydrogen,

nitrogen,and sulfur
Regulate cell processes, build new cells for growth
and renew damaged tissues.
Form structural components such as keratin,
myosin and collagen
Requires for synthesis of enzymes, hormones and
antibodies.
As an important component of the plasma
membrane.

Lipids

Made of the elements carbon, hydrogen, and

oxygen
Store large amounts of energy long term; form
boundaries around cells
Fats and oils are the main sources
Adipose tissues underneath the skin insulate the
bodies of animals against low temperature and
provide physical protection to major organs.

Lipids
Pospholipids are the major constituent of
plasma membrane
Lipids act as a solvent for fat-soluble
vitamins ((A,D,E,K)
Wax reduces water loss in plants and
infection by pathogen

Nucleic Acids

Made of the elements carbon, oxygen, hydrogen,

nitrogen, and phosphorus
Carry genetic information; in the form of code
2 types ; DNA and RNA
DNA is the genetic material that organisms inherit
from their parent
RNA is found in cytoplasm, ribosomes and nucleus
and are involved in proteins synthesis

Water
a) Makes up 70% of human body
Is a polar molecule and universal solvent of
many biological molecules
b) Water helps in maintaining the osmotic balance
( between the blood and interstitial fluid in
animals) and turgidity ( provides support in plants)

Water
c) Water helps to maintain body
temperature by eliminating excess heat
through urination, defecation and
evaporation of sweat.
Transpiration in plants helps to keep
plant tissues cool.

Water
d) Water is a medium for biochemical reactions
Acts as a medium for biochemical reactions
biochem reaction need water to take place(ex:
break down of protein,lipids & sugar
e) The transport medium in blood, lymphatic,
excretory and digestive system, and in the vascular
tissues of plants.

Water
f) Water provides moisture to alveoli which
enables respiratory gases to dissolve and
diffuse across the respiratory surfaces.
g) Helps in lubrication
mucus assists the movement of food in
intestinal tract
Synovial fluid lubricates the joints to ease
movement

Water
h) Has very high cohesion
Enables movement through xilem tissue
in plant to maintain a continuous flow of
water up the stem to the leaves
water molecules tend to stick to each
other and move in long unbroken columns
through the vascular tissues in plants

4.2 CARBOHYDRATE

4.2 CARBOHYDRATE
Source of energy
Contains carbon, hydrogen and oxygen
Ratio of hydrogen atoms to oxygen atoms is 2:1
There are THREE types of carbohydrate:
1) Monosaccharides
2) Disaccharides
3) Polysaccharides

1. MONOSACCHARIDES

Are monomers of carbohydrates which are

the simplest types of carbohydrates (also
known as simple sugar)
General formula ; C6H12O6
Long chain monosaccharides can combine
with protein glycoprotein, with lipid
glycolipid

1. MONOSACCHARIDES

Are REDUCING SUGARS and can act as a

REDUCING AGENT
Examples of monosaccharides:
Glucose found in plants & fruits
Fructose found in sweet fruits & honey
Galactose present in milk

2. DISACCHARIDES

Consist of two monosaccharides joined

together through condensation with the
elimination of water molecule ( a process
which involves the removal of a water
molecule when a bond is formed between
two molecules of monosaccharides)
Also known as complex sugars

2. DISACCHARIDES

General formula : C12H22O11

Maltose and lactose are reducing sugars,

sucrose is a non-reducing sugar
Disaccharides can be broken down into their
constituent monosaccharide by hydrolysis
Hydrolysis is a reaction that involves the
addition of water

2. DISACCHARIDES
Example of disaccharides:
(a) Maltose(malt sugar) formed from the
condensation of TWO glucose molecules
(b) Sucrose(cane sugar) formed from the
condensation of glucose and fructose
(c) Lactose(milk sugar) formed from the
condensation of glucose and galactose

2. DISACCHARIDES

Glucose + glucose

condensation

maltose + water

hydrolysis

Glucose + fructose

Glucose + galactose

condensation
hydrolysis

condensation
hydrolysis

sucrose + water

lactose + water

3. Polysaccharides

a polymer formed by the condensation of hundreds

or thousand of glucose monomers
Insoluble in water due to their large molecular size
Do not taste sweet & do not crystallize
Examples: Starch, glycogen & cellulose
General formula ; ( C6H10O5) n
Can be hydrolyses into smaller molecules by adding
dilute acids, by boiling or through enzymatic
reactions

3. Polysaccharides
Starch is found in plants (wheat,rice..)
main carb reserve in plants
Glycogen is the main reserve in animals &
yeast store in liver& muscle cells
Cellulose makes up cell walls

4.3 Protein
Made

up of elements carbon,
hydrogen, oxygen and nitrogen, also
contain phosphorus & sulphur
Made up of monomers called amino
acid

A dipeptide consists of two molecules of

*amino acids that are linked together b a
peptide bond through condensation
A dipeptide can be broken by hydrolysis
condensation

Amino acid + amino acid

hydrolysis

dipeptide + water

Further condensation can link more amino a.

to form polypeptide chain
There are 20 types of *a.a
Protein/polypeptides that are broken down
through hydrolysis by digestive enzymes are
absorbed into the bloodstream
These a.a used to synthesis protein
molecules that are needed by the body
polypeptide + water

hydrolysis

dipeptides or a.a

Types of amino acid

Can be divided into TWO groups:
1) Essential a.acid a.a that cannot be
synthesised by the body,
2) There are nine essential amino acids
- can be obtained from the diet, eg leucine
- Animal protein contain all the essential a.a
(first class protein) EX: meat,fish, dairy &
eggs

Types of amino acid

2) Non-essential a.acid a.a that can be
synthesised by the body
- There are 11 non essential a.a
- Derived from other amino acids eg; alanine
- Do not contain all the a.a (plant proteins)
- Are called second class proteins EX:
vegetable,peas,beans,nuts and seeds

Protein structure

Can be grouped into 4 level

Primary structure linear sequence of a.a
Sequence are determined by the genetic code
carried in the DNA
Secondary structure - refers to the polypeptide
chain that is coiled to form an alpha-helix(ex: hair)
or folded into beta-pleated sheets. The structure
are held together by hydrogen bonds ex: keratin
(hair protein) , silk

Protein structure
Tertiary structure helix chains & betapleated sheets are folded into a 3D shape
to form a globular protein
The structures are maintained by hydrogen
bonds and disulphate bonds
(ex: hormone, enzymes, antibody&plasma
protein)

Protein structure

Quaternary structure combination of two

or more tertiary structure of polypeptide
chain to form one large & complex protein
molecule
(ex: haemoglobin)

4.4 LIPIDS
Made of carbon, hydrogen & oxygen
The percentage of O2 in lipids is lower than in
carbohydrates
(Ratio of H : O is higher than 2:1 ratio in
carbohydrates)
May contain phosphorus & nitrogen
Are insoluble in water but soluble in other lipids
and organic solvents such as alcohol & ether

Types of lipids
Main

types are: fats, oils, waxes,

phospholipids and steroids

Types of lipids : Fats and oils

Fats and oils are triglycerides(an ester that is

formed through condensation of one molecule
of glycerol and 3 molecules of fatty acid)
Can be broken down into fatty acids & glycerol
by hydrolysis
Each molecules of fatty acids consists of a long
hydrocarbon chain with a different number of
carbon atom

Types of lipids : Fats and oils

Fats containing saturated fatty acids are

saturated fats while those containing
unsaturated fatty acids are unsaturated fats
Saturated fats are solids at room
temperature
Unsaturated fats are liquid at room
temperature

Types of lipids : Waxes

Waxes are found in the cuticle of the epidermis

of leaves water proof, preventing the entry &
evaporation of water
Long chain molecules which are water proof
In plant: on the epidermis cuticle of leaves, fruits
and seeds
In animal; sebum is secreted from the oil glands
in the skin to soften the skin.

Types of lipids : Phospholipids

Main components of plasma membranes

Control the permeability of plasma
membranes

Types of lipids : Steroids

Steroids are complex organic compounds

which include cholesterol and sex
hormones such as testosterone, oestrogen
& progesterone
Cholesterol : major component in plasma
membrane, needed for the synthesis of
steroids and vitamins

Types of lipids : Steroids

Unsaturated fats contain less
cholesterol when compare to saturated
fats
The liver controls the level of
cholesterol in the blood. Unsaturated
fats inhibit the synthesis of cholesterol
in the liver

Similarities saturated fats and

unsaturated fats

Basic components are glycerol and fatty

acids
Formed through the condensation of one
molecule of glycerol and three molecules of
fatty acids
Can be broken down into glycerol and fatty
acids by hydrolysis reactions

Differences : Saturated fats

Saturated fats contain fatty acids which do not

have any double bonds between carbon atoms
All bonds between the carbon atoms have the
maximum number of hydrogen atom
cannot form any chemical bond with other
atoms
Solids at room temperature
(EX: butter,solid in room.temp)

Differences : Unsaturated fats

Unsaturated fats contain fatty acid that have at

least one double bond between the carbon atoms
hydrocarbon chain are not bonded to the
maximum number of hydrogen atoms
Unsaturated fats with one double
bondmonounsaturated, 2 or more double
bonds polyunsaturated fats
Eg; vegetable oils such as corn oil

Fatty Acids
Saturated fats

Cannot form any

chemical bond with other
atoms.
All the bonds between the
carbon atoms have
maximum number of H
atoms.
Eg: butter (solid at RT)

Unsaturated fats

Carbon atoms in
hydrocarbon chain are
not bonded to the
maximum number of H
atoms.
One double bond
monounsaturated fats
Two/ more double bond
polyunsaturated fats.
Eg: corn oil (liquid at RT)

Fatty Acids

Saturated FATS

Fats containing saturated

fatty acids saturated
fats

Unsaturated fats

Fats containing
unsaturated fatty acids
unsaturated fats

4.5 ENZYMES

Enzymes are biological catalyst that regulate

almost all the cellular reactions and speed up
a biochemical reaction in the cell.
It is needed in life processes to regulate
biochemical reaction in the cells
metabolism.
The reactant in biochemical reaction is called
a substrate while the substance formed at
the end of the reaction is called a product.

Characteristics of Enzymes
1.
2.

Enzymes are proteins: synthesized by

living organisms.
Enzymes are highly specific
Each enzyme can only catalyze a single
reaction or one kind of substrate
In enzymatic reactions:

Cont.
Not

destroyed by the reactions

they catalyze.
Have specific sites called active
sites to bind to specific
substrates.
Eg: maltase acts only on maltose.

Cont.
3. Activity of enzymes can be slowed down or
completely stopped by inhibitors.
Eg: Lead, mercury
4. Enzymes speed up biochemical reactions
Enzymes remain unchanged or not destroyed
at the end of the reactions.
5. Most reactions catalysed by enzymes are
reversible reaction

Cont.
6. Enzymes are needed in small amounts
The same enzyme molecule can process a large
number of substrate molecule
7. To function well, enzymes require helper molecules
called cofactor.

Eg:

organic cofactor are derivatives of water-soluble vitamins such

as Vit.B.
Inorganic cofactors: iron and copper
Coenzyme : vit B complex

Naming of Enzymes

Named according to the name of the substrate

it catalyses.
Adding ase at the end of the name of their
substrate.
Eg:
Other enzymes were named before a
systematic way of naming enzymes. Eg:
pepsin, trypsin and rennin.

The Sites of Enzyme Synthesis

Enzymes are proteins, therefore ribosomes

are also the sites of enzyme synthesis.
Information for enzyme synthesis is carried by
DNA.

Different sequences of bases in the DNA are coded

to make different proteins.
During the process, messenger RNA is formed to
translate the codes into a sequence of a.acids.
These a.a are bonded together to form specific
enzymes according to DNAs codes.

Intracellular Enzymes

Intracellular enzymes: enzymes which are

synthesized and retained in the cell for the
use of the cell itself.
Found in cytoplasm, nucleus, mitochondria,
chloroplast

Eg: oxidoreductase catalyses biological oxidation

and reduction in mitochondria.

Extracellular enzymes

Extracellular enzymes: enzymes which are

synthesized in the cell but secreted from
the cell to work externally.

Eg: digestive enzymes produced by the pancreas

but are transported to the duodenum (the site for
enzyme action).

The production of extracellular

enzymes

The production of extracellular

enzymes
1.
2.

3.

The nucleus contains DNA which carries

the information for enzyme synthesis.
Protein are synthesised at the ribosomes.
The proteins are transported through the
spaces within the rough endoplasmic
reticulum (RER).
Proteins wrapped in vesicles bud off from
the membranes of RER as transport
vesicles.

The production of extracellular

enzymes cont
4. The transport vesicles then fuse with
the membranes of the Golgi apparatus.
The proteins are further modified in the
Golgi apparatus.
5. Secretory vesicles containing
modified proteins bud off from Golgi
apparatus

The production of extracellular

enzymes cont
6. The secretory vesicles travel to the
plasma membrane.
7. The vesicles then fuse with the
plasma membrane before releasing the
proteins outside the cell as
extracellular enzymes.

The mechanism of enzyme action

The

way an enzyme binds to it

substrate can be explained by the
lock and key hypothesis.
The substrate molecule is
represented by the key while enzyme
molecule is represented by the lock

The mechanism of enzyme action

a)

Each

enzyme molecule has an active site

The active site of an enzyme has distinctive
shape that complements the substrate
molecule.
Enzymes are highly specific

The mechanism of enzyme action

b)

The

substrate molecule binds to the active

site of the enzyme to form an enzymesubstrate complex

The mechanism of enzyme action

c)
The

enzyme catalyses the substrate to form

a product
The product then leaves the active site of
the enzyme
The enzyme molecule is now ready to bind
to another substrate molecule

Factors affecting enzyme activity:

pH
2. Temperature
3. Enzyme concentration
4. Substrate concentration
1.

Factors affecting enzyme activity:

pH
A slight change in pH can decrease the rate

of enzyme catalysed reactions as each

enzyme function optimally at a particular pH
The optimum pH is the pH at which the rate
of reaction is maximum.
In a cell, most enzymes function optimally
at pH 6 to 8

Factors affecting enzyme activity:

pH

A change in the pH value can alter the

charges on active site of an enzyme and the
surface of the substrate.
This can reduce the ability of both molecules
to bind.
When the pH returns to the optimum level,
the ionic charges on the enzyme are restored
and the enzyme resume its function.

Factors affecting enzyme activity:

Temperature

At low temperature, an enzyme-catalysed

reaction takes place slowly.
For every 10oC rise in temperature, the rate of
reaction is doubled until the optimum
temperature is reached.
The optimum temperature is the temperature
at which an enzyme catalyses a reaction at
the maximum rate (about 37oC in humans)

Factors affecting enzyme activity:

Temperature

Beyond the optimum temperature, any

increase in temperature causes the rate of
reaction to decrease sharply due to the
denaturation of the enzyme, at about 60oC.

Factors affecting enzyme activity:

Enzyme concentration

The rate of an enzyme-catalysed reaction

increases when the enzyme concentration
increases, as long as:
no

other factors are limiting the

reaction
the substrate molecules available
are in excess

Factors affecting enzyme activity:

Enzyme concentration

The rate of reaction is directly proportional

to the concentration of the enzyme until a
maximum rate is achieved.
Beyond the maximum rate, the
concentration of substrate becomes a
limiting factors.

Factors affecting enzyme activity:

Substrate concentration

The rate of an enzyme-catalysed reaction

increases in direct proportion to the
substrate concentration until the reaction
reaches a maximum rate.
It will only lead to an increase in the rate of
reaction if there are enough enzyme
molecules to catalyse the additional
substrate molecules.

Factors affecting enzyme activity:

Substrate concentration

After the maximum rate, any increase in

substrate concentration has no effect on
the rate of reaction.
The rate of reaction becomes constant and
the enzyme concentration becomes a
limiting factors.

The uses of enzymes in daily life

and industry.
Enzyme

Uses

Protease

Tenderies meat in the food industry

Removes the skin of fish in the fish industry
As a detergent to dissolve protein and starch
stains in clothes

Amylase

Changes starch to sugar in the making of syrup

Removes starch that is used as a stiffener from
fabrics

Lipase

Ripening of cheese in dairy products

Cellulase

Breaks down cellulose and removes seed coats

from cereal grains
Extracts agar from seaweed

The importance of chemical

substances in cells

Enables cells to function optimally

Consequences of deficiency :
Carbohydrates

Lack of energy
Lack of food storage

Consequences of deficiency : lipids

Lack of energy

Consequences of deficiency :
Proteins

New cells and tissues cannot be produced

to replace damaged cells.
Inhibit body growth

Discussion:Experiment 4.3
1.The test tubes are immersed
in their respective water
baths for 5 minutes at the
beginning of the experiment
to allow both solutions to
reach the temperature set.
2.Starch is hydrolysed by
salivary amylase to a
reducing sugar (maltose)

3. The iodine solution is used to

test for the presence of starch.
If the iodine solution changes
from brownish-yellow to blueblack, this indicates that starch
is still present in the test tube.
If the colour of the iodine
remains unchanged, this
indicates that all starch has
been hydrolysed by the salivary

4.The graph shows that the rate

of enzyme activity against
temperature is bell-shaped
curve. At low temperatures, for
o
every 10 C increase in
temperature, the rate of
enzymatic reaction is doubled.
The maximum rate of reaction
o
occurs at 37 C, which is the
optimum temperature for

5.At 0oC, the enzyme is not active.

Therefore, the salivary amylase
cannot hydrolysed the starch. The
optimum temperature for the
o
activity of salivary amylase is 37 C.
This is because the hydrolysis of
starch is completed in the shortest
period. Beyond the optimum
temperature, the rate of enzymatic
reaction decreases and cease
o
altogether at 60 C. There is no
activity at 60oC. This is because the
enzyme has denatured due to the

Conclusion
Changes in temperature affect the activity
of salivary amylase on starch. Salivary
amylase is inactive at 0oC and denatures
at 60oC. The rate of reaction catalysed by
salivary amylase is the highest at 37oC,
which is the optimum temperature. The
hypothesis is accepted.

Discussion:Experiment 4.4
1.

2.

The test tubes are immersed in the water

bath maintained at 37oC because this is
the optimum temperature for the action of
pepsin.
Pepsin hydrolyses albumen (protein) into
polypeptides in an acidic medium. The
solution turns clear because polypeptides
are soluble in water.

3.
The pH condition in test tube P (pH3) is optimum
for the function of pepsin
This is because the contents of test tube P
become clear at the end of the experiment.
This shows that albumen has been completely
digested or hydrolysed by pepsin.
The content of test tubes Q and R are still cloudy
at the end of the experiment. This shows that a
neutral (test tubes Q) and an alkaline pH (test
tube R) are not suitable for the activity of pepsin.

Conclusion

The activity of pepsin is affected by the pH

of its medium. An acidic medium (pH3) is
the most suitable medium for pepsin to
function efficiently. The hypothesis is
accepted.