BIOLOGICAL AS

MOLECULES
Monomers and
ATP Inorganic Ions
Polymers

Biological
Carbohydrates Water Tests

Lipids DNA and RNA

Proteins Enzymes
MONOMERS AND POLYMERS
• Monomer – single molecule, e.g. monosaccharide (glucose), amino acids and
nucleotides.
• Polymer – long, complex chain of repeating monomers chemically joined together
by covalent bonds, e.g. polysaccharides (carbohydrate polymers).

•Condensation reactions join monomers together to make polymers. A water

molecule is released for every chemical bond made.
•Hydrolysis reactions use water to break down polymers and release individual
monomers.
 Carbohydrates - general
formula: Cx(H20)y

CARBOHYDRATES Monosaccharide - general

formula: C(H20)n
{n= no. carbon atoms}

•Carbohydrates are made from monosaccharide and are substances used as energy and
structural materials.
•All carbohydrates contain: carbon, hydrogen and oxygen.

There are three main groups of carbohydrates:

Monosaccharide – simple sugars, e.g. glucose, fructose and galactose
Disaccharides – “double sugars” formed from two monosaccharides, e.g. maltose,
sucrose and lactose
Polysaccharides – large molecules formed from many monosaccharides, e.g. cellulose,
starch and glycogen
FUNCTIONS OF CARBOHYDRATES

Substrate for respiration (glucose is essential for cardiac

tissues).
Energy stores (e.g. starch, glycogen).
Structural (e.g. cellulose, chitin in arthropod exoskeletons
and fungal walls).
Transport (e.g. sucrose is transported in the phloem of a
plant).
Recognition of molecules outside a cell (e.g. attached to
proteins or lipids on cell surface membrane).
MONOSACCHARIDE: • Hexose sugar (has six carbon atoms)
• Major energy source for most cells

GLUCOSE (C 6H12O6)…
• Highly soluble
• Transported around the body

Two common isomers of glucose are alpha glucose and beta glucose.
They have the same chemical formula, however the atoms are arranged differently. On C1
the OH and the H group have swapped over in the beta glucose molecule.
 Join together by a glycosidic

DISACCHARIDE (MALTOSE)
bond – a glycosidic bond is a
bond between two sugars that
involves oxygen.

Formation of disaccharides:
Maltose: Two Alpha-Glucose
Maltose
C6H12O6 molecules
+ C6H12O6
- H2O Sucrose Glucose and Fructose
__________
= C6H22O11
Lactose Glucose and Galactose
POLYSACCHARIDES: • Storage molecule
• A mixture of two polysaccharides of

STARCH
alpha glucose: amylose and amylopectin

Amylose
•1-4 glycosidic bonds
•Unbranched chains
•Coiled/helical structure
•It is compact – more stored (fit more in)
Amylopectin
•1-4 + 1-6 glycosidic bonds
•Highly branched chains – so they can be
broken down more easily by the
enzymes and glucose can be released
quickly.

Plants store excess glucose as starch. When a plant needs more glucose for
energy, it breaks down starch to release the glucose.
GLYCOGEN
•In animal cells –excess glucose is not stored as starch but as glycogen.
•Glycogen has a similar structure to amylopectin, containing many alpha 1-6
glycosidic bonds that produce even more branched structures; so glucose can be
released quickly and it is very compact (good for storage).
•This is due to the fact that there is a higher metabolic rate in animals than in plants
– so animals have a greater energy demand. So, being more highly branched means
that it can be hydrolysed even more rapidly.
•It is stored as granules, particularly in the muscles and liver.
CELLULOSE
• Cellulose is the main part of plant cell walls.
•It is very strong and prevents cells from bursting (due to osmotic pressure).
•Contains long, unbranched chains of beta glucose.
•Every other glucose molecule rotates 180so that the hydroxyl (OH) groups on each
molecule are adjacent to each other.
•Hydrogen bonding between chains give cellulose molecules great tensile strength
and structural support for cells (cell walls).
•Microfibrils are formed when many cellulose molecules are linked together by
hydrogen bonds.
 NOTE: You don’t need to know much about chitin – except that
it makes up the cell walls for fungi

CHITIN
•A polymer of nitrogen-containing polysaccharide rendering a tough, protective
covering or structural support in certain organisms and makes up the cell walls of
fungi and exoskeleton of insects.
•It is made up of chains of the monosaccharide N-acetylglucosamine, which is
derived from glucose. The polysaccharide chains are long, unbranched and linked
together by weak hydrogen bonds.
•Chitin can be broken down by the enzyme called chitinase, which catalyse
hydrolysis reactions. Some organisms are able to make their own chitinases.
 LIPIDS
Structure of a Triglyceride

Triglycerides are a kind of lipid and are made up of:

•One glycerol molecule
•Three fatty acids

•Fatty acid molecules have long ‘tails’ made out of hydrocarbons.

The tails are hydrophobic (they repel water molecules). These
tails make lipids insoluble in water. All fatty acids have the same
basic structure, but the hydrocarbon tail varies.

Structure of a Fatty Acid

TRIGLYCERIDES
The diagram shows a fatty acid joining to a glycerol molecule. When the ester bond is
formed a molecule of water is released per bond made – it’s a condensation reaction.

The triglyceride
is insoluble in
water, as it no
longer has an
OH group.
FATTY ACIDS
There are two kinds of fatty acids – saturated and
unsaturated.
The difference is in their hydrocarbon tails (R group).

•Saturated fatty acids don’t have any double bonds

between their carbon atoms. The fatty acid is ‘saturated’
with hydrogen.
•Unsaturated fatty acids have at least one double bond
between carbon atoms, which cause the chain to kink.
PHOSPHOLIPIDS
•The lipids found in cell membranes aren’t triglycerides –
they’re phospholipids.
•Phospholipids are pretty similar to triglycerides except
one of the fatty acid molecules is replaced by a
phosphate group.
•The phosphate group is hydrophilic (attracts water). The
fatty acid tails are hydrophobic (repel water). This is an
important feature in cell membranes.
FUNCTIONS OF LIPIDS
Triglycerides – are mainly used as energy storage Phospholipids – make up the bilayer of cell
molecules. They’re good for this because: membranes. Cell membranes control what
•The long hydrocarbon tails of the fatty acids contain enters and leaves a cell.
lots of chemical energy – a load of energy is released •Their heads are hydrophilic and their tails
when they’re broken down. Because of these tails, are hydrophobic, so they form a double
lipids contain about twice as much energy per gram layer with their heads facing out towards
as carbohydrates. the water on either side.
•They’re insoluble, so they don’t affect the water
•The centre of the bilayer is hydrophobic, so
potential of the cell and cause water to enter the
water–soluble substances can’t easily pass
cells by osmosis (which would make them swell). The
triglycerides clump together as insoluble droplets in through it – the membrane acts as a barrier
cells, because the fatty acid tails are hydrophobic to those substances.
(water repelling) – the tails face inwards, shielding
themselves from water with their glycerol heads.
 PROTEINS
•Made from long chains of amino acids (monomers).
•A dipeptide is formed when two amino acids join together.
•A polypeptide is formed when more than two amino acids join together.
•Proteins are made up of one or more polypeptides.

•Amino acids have the same general structure – a carboxyl group, an amino group,
and a carbon-containing variable group.
•They contain the elements: carbon, hydrogen, oxygen and nitrogen.
•All living things share a bank of only 20 amino acids.
•The only difference between them is their variable group.
POLYPEPTIDES
•Amino acids are linked together by
condensation reactions to form
polypeptides. A molecule of water is
released during the reaction. The bonds
formed between amino acids are called
peptide bonds.
•The reverse reaction happens during
digestion (hydrolysis).
STRUCTURE OF PROTEINS
•Primary Structure – this is the sequence of amino acids in the polypeptide
chain.
•Secondary Structure – hydrogen bonds form between the amino acids in the
chain. This makes it coil into an alpha helix or fold into a beta pleated sheet.
•Tertiary Structure – the coiled or folded chain of the amino acids is often
coiled and folded further. More bonds form between different parts of the
polypeptide chain, including hydrogen bonds and ionic bonds (due to the
attraction between negative and positive charges on different parts of the
molecule). Disulphide bridges also form whenever two molecules of the
amino acid cysteine come close together – the sulphur atom in one cysteine
bonds to the sulphur atom in the other.
•Quaternary Structure – some proteins are made of several different
polypeptide chains held together by bonds (e.g. haemoglobin, insulin,
collagen). The 4th structure is the way these polypeptide chains are
assembled together. This is the protein’s final 3D structure.
FUNCTIONS OF PROTEINS
Usually roughly spherical in shape due to the tight folding of the polypeptide chains.
They are soluble and often have roles in metabolism. Example, some enzymes break
Enzymes down large molecules and other enzymes help to synthesise (make) large molecules
(digestive enzymes)
Involved in the immune response. They’re made up of two short polypeptide chains
Antibodies and two long polypeptide chains bonded together. Antibodies have variable regions,
the amino acid sequences in these regions vary greatly.
Example, channel proteins are present in cell membranes. Channel proteins contain
Transport hydrophobic (water-hating) and hydrophilic (water-loving) amino acids, which cause
proteins the protein to fold up and form a channel. These proteins transport molecules and
ions across membranes.
Are physically strong. They consist of long polypeptide chains lying parallel to each
Structural other with cross-links between them. Structural proteins include keratin (found in
proteins hairs and nails) and collagen (found in connective tissue).
 ENZYMES
Biological catalysts – speed up a reaction (by providing an alternative path which is
easier and requires less energy), and without being used up.
•Enzymes catalyse metabolic reactions – both at a cellular level (e.g. respiration) and
for the organism as a whole (e.g. digestion in mammals).
•Enzymes can affect structures in an organism (e.g. enzymes are involved in the
production of collagen, an important protein in the connective tissues of animals) as
well as functions (like respiration).
•Enzyme action can be intracellular (within cells), or extracellular (outside cells).
•Enzymes are proteins.
 Activation energy – the energy
needed to start a reaction

ACTIVATION ENERGY
•In a chemical reaction, a certain amount of energy needs to be
supplied to the chemicals before the reaction will start. This is
called the activation energy – it’s often provided as heat.
Enzymes lower the amount of activation energy that’s needed,
often making reactions happen at a lower temperature than they
could without an enzyme. This speeds up the rate of reaction.
•When a substrate fits into the enzyme’s active site, it forms an
enzyme-substrate complex it’s this that lowers the activation
energy. Here are two reasons why:

If two substrate molecules need to be joined, If the enzyme is catalysing a breakdown

being attached to the enzyme holds them close reaction, fitting into the active site puts a
together, reducing any repulsion between the strain on the bonds in the substrate, so the
molecules so they can bond more easily. substrate molecule breaks up more easily.
‘LOCK AND KEY’ MODEL ‘Lock and Key’

The ‘lock and key’ model proposed

that a substrate fits an enzyme the
same way a key fits a lock.
However, scientists found new
evidence which shows that the
enzyme-substrate complex changes
shape slightly to complete the fit. ‘Induced Fit’
This locks the substrate even more
tightly to the enzyme.
Scientists modified the old lock and
key model and came up with the
‘induced fit’ model.
‘INDUCED FIT’ MODEL
•The ‘induced fit’ model helps to explain why enzymes are so specific and only bonds to
one particular substrate. The substrate doesn’t only have to be the right shape to fit the
active site, it has to make the active site change shape in the right way as well.
 ENZYME PROPERTIES
•Very specific – usually only catalyse one reaction, e.g. maltase only breaks down maltose. This
is because only one complementary substrate will fit into the active site.
•The active site’s shape is determined by the enzyme’s tertiary structure (which is determined
by the enzyme’s primary structure). Each different enzyme has a different tertiary structure
and so a different shaped active site. If the substrate shape doesn’t match the active site, an
enzyme-substrate complex won’t be formed and the reaction won’t be catalysed.
•If the tertiary structure of the enzyme is altered in any way, the shape of the active site will
change. This means the substrate won’t fit into the active site, an enzyme-substrate complex
won’t be formed and the enzyme will no longer be able to carry out its function.
•The tertiary structure of an enzyme may be altered by changes in pH or temperature.
•The primary structure (amino acid sequence of a protein) is determined by a gene. If
mutation occurs in that gene, it could change the tertiary structure of the enzyme produced.
 FACTORS AFFECTING ENZYME ACTIVITY

As the temperature As pH increases, the

increases up to the rate of reaction
‘optimum’ the enzyme increases up to the
activity increases, then optimum pH and then
decreases. decreases.

• As the temperature rises, reacting molecules have more
kinetic energy. This increases the chances of a successful
collision and so the rate increases (more enzyme-substrate
complexes formed).
• Above the optimum temperature the enzyme structure
begins to break down hydrogen bonds at higher temperatures
(denature), causing the active site to change shape (few/no
enzyme-substrate complexes formed).
• As the pH moves away from the optimum, H+ (in
acids) or OH- (in alkalis) break the hydrogen bonds and
ionic bonds that maintain the tertiary structure of the
enzyme. As a result, the enzyme denatures so the
active site’s shape changes – fewer/no enzyme-
substrate complexes form.
FACTORS AFFECTING ENZYME ACTIVITY

Enzyme As substrate
concentration is the concentration increases,
limiting factor. the rate of reaction
increases up to a point
and then levels off.

Increasing enzyme concentration will increase the rate of
reaction, as more enzymes will be colliding with substrate
molecules.
However, this will only have an effect up to a certain
concentration, where the enzyme concentration is no longer
the limiting factor. Substrate is limited so there's no further
effect.
• An increase in substrate concentration means more
substrate molecules will be colliding with enzyme
molecules, so more product will be formed.
• After a certain point, all the enzyme active site’s are
occupied. This is the ‘saturation point’ (enzyme
concentration is the limiting factor).
NON/COMPETITIVE
INHIBITION
•Competitive Inhibitor: These molecules have a similar structure to
the actual substrate and will compete with the substrate molecules
to bind to the active site, but no reaction takes place.
•How much enzyme is inhibited depends on the relative
concentrations of the inhibitor and the substrate.

•Non-competitive inhibitors: these molecules bind with the enzyme

away from the active site. This binding changes the shape of the
enzyme, so the substrate molecules can no longer bind to the active
site.
•Increasing the concentration of the substrate won’t make a difference
to the reaction rate – enzyme activity will still be inhibited.
 Nucleotides:

DNA AND RNA

are monomers that
make up DNA and RNA.

DNA and RNA are both types of nucleic acid. They’re found in
all living cells and they both carry information. • Chromosomes are made
from DNA
• DNA and RNA are
•DNA (deoxyribonucleic acid) is used to store genetic macromolecules (very
information – that’s all the instructions an organism needs to large molecule)
• They are also polymer,
grow and develop from a fertilised egg to a fully grown adult.
made up of many similar,
•RNA (ribonucleic acid) is similar in structure to DNA. One of its smaller molecules joined
main functions is to transfer genetic information from the together in a chain
• The smaller molecules are
DNA to the ribosomes. Ribosomes are the body’s ‘protein nucleotides
factories’ – they read the RNA to make polypeptides (proteins) • DNA and RNA are
in a process called translation. Ribosomes themselves are therefore a
made from RNA and proteins. polynucleotides

DEOXYRIBOSE AND RIBOSE
DNA Nucleotide
•The pentose sugar in a DNA nucleotide is called
deoxyribose.
•Each DNA nucleotide has the same sugar and a
phosphate group. The base on each nucleotide
can vary though.
•There are four possible bases – adenine,
thymine, cytosine and guanine.
Two condensation reactions are involved
in the formation of a nucleotide:
1. Deoxyribose + Base
2. Deoxyribose + Phosphate
RNA Nucleotide:
•RNA contains nucleotides with a ribose
sugar.
•Like DNA, RNA nucleotide has a phosphate
group and one of four different bases.
•In RNA though, uracil replaces thymine as
a base.
POLYNUCLEOTIDES
P
Thymine

Sugar-phosphate backbone
•Nucleotides join, by condensation reactions, to Sugar
form polynucleotide strands. Both DNA and RNA
nucleotides form polynucleotides (polymer of
nucleotides). P
Cytosine

•The nucleotides join up between the phosphate

Sugar
group of one nucleotide and the pentose sugar of
another, forming a sugar-phosphate backbone.
•The bond between the phosphate group and the P
Adenine
sugar is called a phosphodiester bond.
Sugar

Phosphodiester bond
DOUBLE-HELIX RNA is made from a single
polynucleotide chain (not a double one.

STRUCTURE
It’s much shorter than most DNA
polynucleotides.

Two polynucleotide chains of DNA are held together by hydrogen bonds between
complementary base pairs:
•Adenine pairs with thymine (A=T) via two hydrogen bonds
•Guanine pairs with cytosine (G=C) via three hydrogen bonds
This means that there are always equal amounts of both pairs in a DNA molecule.

In order for bases to be facing each other and thus able to pair, the two strands must
run in opposite directions (i.e. they are anti-parallel). These twist to form a double
helix.
FUNCTION OF DNA
Each gene in a molecule of DNA contains:
A different sequence of bases •DNA molecules are very
long and coiled so a lot of
Codes for a particular protein genetic information can be
stored in a small space.
Proteins are made in the cytoplasm of a cell, not in •The double helix is a very
the nucleus. Genes cannot leave the nucleus, so a stable structure.
copy of the gene is needed. This copy is able to •Base-pairing allows
leave the nucleus to go into the cytoplasm so that accurate replication.
proteins can be made by the cell.
DNA REPLICATION
The enzyme helicase ‘unzip’ (break) hydrogen bonds between bases on the two
polynucleotide DNA strands. This makes the helix unwind, to form single strands. This
leaves the bases exposed.
•Each original strand acts as a template. In the nucleus there are many free nucleotides
which can pair up with the exposed bases (complementary base pairing).
•Condensation reactions join the nucleotides of the new strands together – catalysed by
the enzyme DNA polymerase. Hydrogen bonds form between the bases of the original
and new strands.

•This is semi-conservative replication – Each new DNA molecule contains one strand
from the original DNA molecule and one new strand.
ANTIPARALLEL DNA STRANDS
A single DNA strand is different at its two ends. One end is called  5' (5 prime), the other is
called 3' (3 prime). In a DNA helix, the strands run in opposite directions – they’re
antiparallel.
•The active site of DNA polymerase is only complementary to the 3’ end of the newly forming
DNA strand – so the enzyme can only add nucleotides to the new strand at the 3’ end.

•This means that the new strand is made in a 5’ to

3’ direction and that DNA polymerase moves down
the template strand in a 3’ to 5’ direction. Because
the strands in a double-helix are antiparallel, the
DNA polymerase working on one of the template
strands moves in the opposite direction to the DNA
polymerase working on the other template strand.
 DNA of heavy, light, and intermediate densities can be
separated by centrifugation.

MESELSON AND STAHL

Meselson and Stahl (1957) gave experimental
evidence that each DNA strand served as a
template for new synthesis, a process called semi-
conservative replication.
•E. coli was grown in 15N nitrogen (more dense
isotope).
•This was then transferred to 14N nitrogen (less
dense isotope) and after one, two, or three
generations take samples of DNA.
•They were then mixed with caesium chloride and
separate DNA by centrifugation.
WATER
•Water is a metabolite in loads of important
metabolic reactions, including condensation and
hydrolysis reactions.
• A Water molecule consists of two hydrogen
•Water is a solvent which means some substances atoms covalently bonded to an oxygen atom.
dissolve in it. Most metabolic reactions take place in • Because oxygen is more electronegative than
solution (e.g. cytoplasm of eukaryotic and hydrogen, it has a greater pull on the shared
prokaryotic cells).
electrons.
•Water helps with temperature control because it has • This that the oxygen atom is slightly negative (δ-) and
a high latent heat of vaporisation and a high specific can pull the electrons towards itself. The unshared
heat capacity. distribution of electrons, means hydrogen
•Water molecules are very cohesive (they stick becomes slightly positive (δ+).
• Water is therefore called a polar molecule.
together), which helps water transport in plants as
well as transport in other organisms.
 PROPERTIES OF WATER

It’s an important metabolite •This means the ions will get totally surrounded by water
molecules – in other words, they’ll dissolve.
• Many metabolic reactions involve a condensation or a
hydrolysis reaction.
•A hydrolysis reaction requires a molecule of water to break a Buffer (resist) changes in temperature
bond. A condensation reaction releases a molecule of water as
a new bond is formed. •Hydrogen bonds absorb a lot of energy, which means that a
large amount of energy is required to raise the temperature of
water. This property means that oceans and lakes provide
a stable environment in which organisms can live.
Excellent polar solvent
•This also means that a large amount of heat is required
•A lot of important substances in metabolic reactions are ionic to evaporate water, so it is very useful in cooling, for example,
(e.g. salt). sweating to cool down.
• Because water is polar, the positive end of a water molecule
will be attracted to the negative ion, and the negative end of a
water molecule will be attracted to a positive ion.
 PROPERTIES OF WATER
High latent heat of evaporation
• It takes a lot of energy (heat) to break the hydrogen bonds
between water molecules.
•So water has a high latent heat of vaporisation – a lot of
energy is used up when water evaporates (vaporises).
•This is useful for living organisms because it means they can
use water loss through evaporation to cool down without
losing too much water.
High cohesive force between molecules (surface tension)
•Cohesion is the attraction of molecules within a substance
ao they 'stick together'. Water molecules are very
cohesive because they’re polar.
•Strong cohesion helps water flow, e.g. transport of water in
the Xylem in plants.
•Cohesion also gives the water a high surface tension when
it comes into contact with air, allowing small
organisms, such as Pond Skaters, to walk along it. This is also
why sweat forms droplets, which evaporate from the skin to
cool and organism down.
Ice is less dense than water and therefore floats
•Water is unusual because it's solid form is less dense than
it's liquid form. Below 4°c the density of water starts to
decrease and so ice floats on water and insulates the water
below it.
•This reduces the chances of large bodies of water
completely freezing and increases the chances of life in
water surviving. These changes in density of water with
temperature are important in the oceans because they set
up currents, which circulate nutrients.
 ATP ATP is the immediate source of energy in a cell.

Uses of ATP:
•Plants and animal cells release energy from glucose – this process is called • muscle contraction
respiration. • active transport
•A cell can’t get its energy directly from glucose. • synthesis of
macromolecules
•So, in respiration the energy released from glucose is used to make ATP • stimulates the breakdown
(adenosine triphosphate).
of substrates to make even
•ATP is made from the nucleotide base adenine, combined with a ribose sugar more ATP for other uses.
and three phosphate groups. It’s what's known as a nucleotide derivative.
Because it’s a modified form of a nucleotide:

•Once made, ATP diffuses to the part of the cell that needs energy.
•The energy in ATP is stored in high energy bonds between the phosphate
groups. Its release via hydrolysis reactions.
 IMPORTANT FEATURES OF ATP
•ATP releases energy in small amounts
•It is broken down in one step (single bond broken
between phosphate groups)
•It provides immediate energy (makes energy available
rapidly)
•Can phosphorylate other molecules (add phosphate to
other molecules) – this makes substances more
reactive/lowers the activation energy.
•It can be reformed and made again – i.e. ADP + Pi  ATP
INORGANIC IONS
•An inorganic ion is on which doesn’t contain carbon (although there are a few
exceptions to this rule).
•Inorganic ions occur in solution, in the cytoplasm of cells and body fluids of
organisms, some in high concentrations and others in very low concentrations
(inferred by the ion’s role).
•Each type of ion has a specific role, depending on its properties.

• An ion is an atom (or group of atoms) that has an electric charge.

• An ion with a positive charge is called a cation.
• An ion with a negative charge is called a anion.
ROLES OF IONS
Hydrogen ions determine pH
•pH is calculated based on the concentration of
hydrogen ions (H+) in the environment. The more
H+ present, the lower the pH (and the more acidic
the environment).
•Enzyme-controlled reactions are all affected by the
pH.
Iron ions as a component of haemoglobin
• Haemoglobin is a large protein that carries oxygen
around the body, in the red blood cells.
• It’s made up of four different polypeptide chains,
each with an iron ion (Fe2+) in the centre. The iron
ion binds to the oxygen in haemoglobin – so it’s a
key component.
Sodium ions help transport glucose and amino acids
across membranes
•A molecule of glucose or an amino acid can be
transported into a cell (across the cell-surface
membrane) alongside sodium ions (Na+). This is
known as co-transport.
Phosphate ions are essential components of DNA
and ATP.
•When a phosphate ion is attached to another
molecule, it’s known as a phosphate group.
•DNA, RNA and ATP all contain phosphate groups.
• The phosphate groups in DNA and RNA allow
nucleotides to join up to form the polynucleotides.
Biological
Tests
 Reducing sugar: Benedict’s test:
1. Add Benedict’s reagent to a
sample
2. Heat the sample in a water bath

BENEDICT'S TEST
3. Observe colour change

Non-reducing sugar:
•Add dilute hydrochloric acid to sample and boil for
one minute.
•Allow the tube to cool and then neutralize the acid
with sodium hydrogen carbonate.
•Carry out Benedict’s test.
•Observe colour change.
Solution Glucose Maltose Fructose Sucros Starch
e
Colour Brick- Brick- Brick-red Blue Blue
(non-
change red/Orange red/Orange /Orange reducing
sugar)
IODINE TEST FOR STARCH
Iodine dissolved in potassium iodide solution is added to a sample. A positive
result (starch is present), changes the solution from an brown-orange to a
blue-black colour.
BIURET TEST FOR PROTEINS

•Add biuret reagent to a sample.

If protein is present then the solution turns purple.

If there’s no protein, the solution will stay blue.
EMULSION TEST FOR LIPIDS
1. Add a suitable volume of ethanol to
the test substance. Then shake the
mixture.
2. Next add a equal volume of distilled
water. Shake the mixture again.
3. A milky-white emulsion forms if
the test substance contains lipids

The more lipid there is the more

noticeable the colour will be.