Food Test 3

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YOUR NOTES
IGCSE Biology Edexcel 
Biological Molecules
CONTENTS
2.7 Chemical Elements in Biological Molecules
2.8 Structure of Carbohydrates, Proteins & Lipids
2.9 Practical: Food Tests
2.10 Role of Enzymes
2.11 Temperature & Enzyme Function
2.12 Practical: Investigating Temperature & Enzyme Activity
2.13 pH & Enzyme Function
2.14B Practical: Investigating pH & Enzyme Activity
Page 1 of 32
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2.7 Chemical Elements in Biological Molecules YOUR NOTES


Chemical Elements
Most of the molecules in living organisms fall into three categories: carbohydrates,
proteins and lipids
These all contain carbon and so are described as organic molecules
Page 2 of 32
2.8 Structure of Carbohydrates, Proteins & Lipids YOUR NOTES


Large Molecules are Made from Smaller Molecules
Carbohydrates
Carbohydrates contain the elements carbon, hydrogen and oxygen
A monosaccharide is a simple sugar e.g. glucose (C6H12O6) or fructose
Glucose molecules contain lots of energy which can be released in respiration by
breaking the bonds between the carbon atoms
A disaccharide is made when two monosaccharides join together
Maltose is formed from two glucose molecules
Sucrose is formed from one glucose and one fructose molecule
A polysaccharide is formed when lots of monosaccharides join together
Starch, glycogen or cellulose are all formed when lots of glucose molecules join
together
Polysaccharides are insoluble and therefore useful as storage molecules
Glycogen, cellulose and starch are all made from glucose molecules
Fats
Most fats (lipids) in the body are made up of triglycerides
Their basic unit is one glycerol molecule chemically bonded to three fatty acid chains
The fatty acids vary in size and structure
Lipids are divided into fats (solids at room temperature) and oils (liquids at room
temperature)
Page 3 of 32
YOUR NOTES

The structure of a triglyceride

Proteins
Proteins are formed from long chains of amino acids
There are 20 different amino acids
When amino acids are joined together a protein is formed
Amino acids can be arranged in any order, resulting in hundreds of thousands of different
proteins
Examples of proteins include enzymes, haemoglobin, ligaments and keratin
Page 4 of 32
YOUR NOTES

Amino acids join together to form proteins

Protein shape
Different proteins have different amino acid sequences resulting in them being different
shapes
Even a small difference in the amino acid sequence will result in a completely different
protein being formed
The different sequences of amino acids cause the polypeptide chains to fold in different
ways and this gives rise to the different shapes of proteins
In this way, every protein has a unique 3-D shape that enables it to carry out its function
The shape of a protein determines its function
For example:
Enzymes have a specifically shaped active site - this is where a specific substrate
molecule fits in order for a reaction to take place
If the shape of the active site does not match the shape of the molecule that fits into it,
the reaction will not take place
Antibodies are proteins produced by certain types of white blood cells that attach to
antigens on the surface of pathogens
The shape of the antibody must match the shape of the antigen so that it can attach
to it and signal it for destruction
Page 5 of 32
YOUR NOTES

Every enzyme has a different shaped active site-specific to one substrate
 Exam Tip
You should be able to explain the importance of sugars, amino acids, fatty acids and
glycerol in the synthesis and breakdown of carbohydrates, proteins and lipids. There
will be many examples of each of these molecules throughout the course.
Page 6 of 32
2.9 Practical: Food Tests YOUR NOTES


Practical: Food Tests
Preparing a sample
Before you can carry out any of the food tests described below, you may need to prepare a
food sample first (especially for solid foods to be tested)
To do this:
Break up the food using a pestle and mortar
Transfer to a test tube and add distilled water
Mix the food with the water by stirring with a glass rod
Filter the mixture using a funnel and filter paper, collecting the solution
Proceed with the food tests
Test for glucose (a reducing sugar)
Add Benedict's solution to the sample solution in a test tube
Heat in a boiling water bath for 5 minutes
Take the test tube out of the water bath and observe the colour
A positive test will show a colour change from blue to orange / brick red
The Benedict's test for glucose

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Test for starch using iodine YOUR NOTES

We can use iodine to test for the presence or absence of starch in a food sample 
Add drops of iodine solution to the food sample
A positive test will show a colour change from orange-brown to blue-black
In the presence of starch, iodine will turn from brown to blue-black

Test for protein
Add drops of Biuret solution to the food sample
A positive test will show a colour change from blue to violet / purple
Page 8 of 32
YOUR NOTES

The Biuret test for protein

Test for lipids
Mix the food sample with 4cm3 of ethanol and shake
Allow time for the sample to dissolve in the ethanol
Strain the ethanol solution into another test tube
Add the ethanol solution to an equal volume of cold distilled water (4cm3)
A positive test will show a cloudy emulsion forming
Page 9 of 32
YOUR NOTES

The ethanol test for lipids

Food Test Results Table
Important hazards
Whilst carrying out this practical you should try to identify the main hazards and be thinking
of ways to reduce harm
Page 10 of 32
Biuret solution contains copper (II) sulfate which is dangerous particularly if it gets in the YOUR NOTES
eyes, so always wear goggles 
Iodine is also an irritant to the eyes
Sodium hydroxide in biuret solution is corrosive, if any chemicals get onto your skin wash
your hands immediately
Ethanol is highly flammable; keep it away from any Bunsen burner
The Bunsen burner itself is a hazard due to the open flame
 Worked Example
Food tests: analysis
Write a conclusion to state which food groups are present one of the food samples
you tested and an explanation of how you know this.
Conclusion:
The apple contained both starch and sugar as it tested positive for both the iodine test
(orange → blue - black) and the benedict's test (blue → orange).
The apple did not contain protein or lipid (fat) as the biuret and emulsion tests were both
negative.
Applying CORMS to practical work
When working with practical investigations, remember to consider your CORMS
evaluation.
Page 11 of 32
YOUR NOTES

CORMS evaluation
In this investigation, your evaluation should look something like this:
C - We are changing the type of food in the sample
O - This is not relevant to this investigation as we aren't using an organism
R - We will repeat the investigation several times for each food sample to ensure a
reliable result
M1 - The presence of the specific biological molecule in each food type by noting the
colour change
M2 - ....after testing with each specific testing agent
S - We will control the volume of each testing agent used, the quantity of the food
sample, the concentration of the testing agents, the temperature of the water bath for
the Benedicts test. There may be other examples that you can think of
 Exam Tip
When describing food tests in exam answers, make sure you give the starting
colour of the solution and the colour it changes to for a positive result.
Page 12 of 32
2.10 Role of Enzymes YOUR NOTES


Page 13 of 32
Enzymes as Biological Catalysts YOUR NOTES

Enzymes 
Enzymes are proteins that act as biological catalysts to speed up the rate of a chemical
reaction without being changed or used up in the reaction
They are biological because they are made in living cells
Enzymes are necessary to all living organisms as they maintain reaction speeds of all
metabolic reactions at a rate that can sustain life
For example, if we did not produce digestive enzymes, it would take around 2 - 3 weeks
to digest one meal; with enzymes, it takes around 4 hours
Often the products of one reaction are the reactants for another (and so on)
The mechanism of enzyme action
Enzymes are specific to one particular substrate(s) as the active site of the enzyme, where
the substrate attaches, is a complementary shape to the substrate
When the substrate moves into the enzyme’s active site they become known as the
enzyme-substrate complex
After the reaction has occurred, the products leave the enzyme’s active site as they no
longer fit it and it is free to take up another substrate
Step One: Enzymes and substrates randomly move about in solution
Step Two: When an enzyme and its complementary substrate randomly collide an
enzyme-substrate complex forms, and the reaction occurs
Step Three: A product (or products) forms from the substrate(s) which are then
released from the active site. The enzyme is unchanged and will go on to catalyse
further reactions
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YOUR NOTES

How enzymes work
Page 15 of 32
2.11 Temperature & Enzyme Function YOUR NOTES


Page 16 of 32
Factors Affecting Enzyme Action: Temperature YOUR NOTES

Enzymes are proteins and have a specific shape, determined by the amino acids that 
make the enzyme and held in place by bonds
This is extremely important around the active site as the specific shape is what ensures the
substrate will fit into the active site and enable the reaction to proceed
Enzymes work fastest at their ‘optimum temperature’
In the human body, the optimum temperature is 37⁰C
Heating to high temperatures (beyond the optimum) will break the bonds that hold the
enzyme together and it will lose its shape
This is known as denaturation
Substrates cannot fit into denatured enzymes as the shape of their active site has been lost
Denaturation is irreversible - once enzymes are denatured they cannot regain their proper
shape and activity will stop
Page 17 of 32
YOUR NOTES

Effect of temperature on enzyme activity

Increasing the temperature towards the optimum increases the activity of enzymes as the
more kinetic energy the molecules have the faster they move and the number of
collisions with the substrate molecules increases, leading to a faster rate of reaction
This means that low temperatures do not denature enzymes, they just make them work
more slowly due to a lack of kinetic energy
Page 18 of 32
YOUR NOTES

Graph showing the effect of temperature on the rate of enzyme activity
Page 19 of 32
2.12 Practical: Investigating Temperature & Enzyme Activity YOUR NOTES


Page 20 of 32
Practical: Enzymes & Temperature YOUR NOTES

Amylase is an enzyme that digests starch (a polysaccharide of glucose) into maltose (a 
disaccharide of glucose)
The effect of temperature on the activity of amylase can be investigated
Apparatus
Spotting tile
Measuring cylinder
Test tube
Syringe
Pipette
Stopwatch
Water
Thermometer
Water bath
Iodine
Starch solution
Amylase solution
Method
Add 5cm3 starch solution to a test tube and heat to a set temperature using beaker of
water with a Bunsen burner
Add a drop of Iodine to each of the wells of a spotting tile
Use a syringe to add 2cm3 amylase to the starch solution and mix well
Every minute, transfer a droplet of solution to a new well of iodine solution (which should
turn blue-black)
Repeat this transfer process until the iodine solution stops turning blue-black (this means
the amylase has broken down all the starch)
Record the time taken for the reaction to be completed
Repeat the investigation for a range of temperatures (from 20°C to 60°C)
Page 21 of 32
YOUR NOTES

Investigating the effect of temperature on enzyme activity

Results and Analysis
Page 22 of 32
Amylase is an enzyme which breaks down starch YOUR NOTES

The quicker the reaction is completed, the faster the enzyme is working 
This investigation shows:
At the optimum temperature, the iodine stopped turning blue-black the fastest
This is because the enzyme is working at its fastest rate and has digested all the
starch
At colder temperatures (below optimum), the iodine took a longer time to stop turning
blue-black
This is because the amylase enzyme is working slowly due to low kinetic energy
and few collisions between the amylase and the starch
At hotter temperatures (above optimum) the iodine turned blue-black throughout the
whole investigation
This is because the amylase enzyme has become denatured and so can no longer
bind with the starch or break it down
Limitations
Note that there are several different ways in which the temperature could be controlled. The
method described above is not very precise, an improvement would be to use water baths
kept at each temperature
The starch and amylase solutions that need to be used should be placed in a water bath
and allowed to reach the temperature (using a thermometer to check) before being used
A colorimeter can be used to measure the progress of the reaction more accurately
A solution containing starch will be darker than a solution containing glucose (as a
result of the colour change of iodine)
The absorbance or transmission of light through the coloured solution can be
measured using a colorimeter
When working with practical investigations, remember to consider your CORMS evaluation
Page 23 of 32
YOUR NOTES

CORMS evaluation
C - We are changing the temperature in each repeat
R - We will repeat the investigation several times to make sure our results are reliable
M1 - We will measure the time taken
M2 - for the iodine to stop turning black
S - We will control the concentration and volume of starch solution, iodine and amylase
used in the investigation
 Exam Tip
Describing and explaining experimental results for enzyme experiments is a common
type of exam question so make sure you understand what is happening and can
relate this to changes in the active site of the enzyme when it has denatured, or if it is
a low temperature, relate it to the amount of kinetic energy the molecules have.
Page 24 of 32
2.13 pH & Enzyme Function YOUR NOTES


Page 25 of 32
Factors Affecting Enzyme Action: pH YOUR NOTES

The optimum pH for most enzymes is 7 
Some enzymes that are produced in acidic conditions, such as the stomach, have a
lower optimum pH (pH 2)
Some that are produced in alkaline conditions, such as the duodenum, have a higher
optimum pH (pH 8 or 9)
If the pH is too high or too low, the bonds that hold the amino acid chain together to make
up the protein can be disrupted/destroyed
This will change the shape of the active site, so the substrate can no longer fit into it,
reducing the rate of activity
Moving too far away from the optimum pH will cause the enzyme to denature and activity
will stop
Effect of pH on enzyme activity
Page 26 of 32
YOUR NOTES

Graph showing the effect of pH on the rate of activity for an enzyme from the duodenum
 Exam Tip
Remember the terminology when writing about enzymes is very important. Make
sure you refer to an enzyme becoming 'denatured' not 'dying'.Being able to describe
AND explain the effect of each environmental condition on enzyme action is
key.Practise describing and explaining using the graphs and then check your
descriptions against your notes.
Page 27 of 32
2.14B Practical: Investigating pH & Enzyme Activity YOUR NOTES


Page 28 of 32
Practical: Enzymes & pH YOUR NOTES

Amylase is an enzyme that digests starch (a polysaccharide of glucose) into maltose (a 
disaccharide of glucose)
The effect of different pH levels on the activity of amylase can be investigated
Apparatus
Spotting tile
Measuring cylinder
Test Tube
Syringe
Pipette
Stopwatch
Buffer solutions
Iodine
Starch solution
Amylase solution
Method
Add a drop of iodine to each of the wells of a spotting tile
Use a syringe to place 2 cm3 of amylase into a test tube
Add 1cm3 of buffer solution (at pH 2) to the test tube using a syringe
Use another test tube to add 2 cm3 of starch solution to the amylase and buffer solution, start
the stopwatch whilst mixing using a pipette
Every 10 seconds, transfer a droplet of the solution to a new well of iodine solution (which
should turn blue-black)
Repeat this transfer process every 10 seconds until the iodine solution stops turning blue-
black (this means the amylase has broken down all the starch)
Record the time taken for the reaction to be completed
Repeat the investigation with buffers at different pH values (ranging from pH 3.0 to pH 7.0)
Page 29 of 32
YOUR NOTES

Page 30 of 32
Investigating the effect of pH on enzyme activity YOUR NOTES

Results and Analysis 
Amylase is an enzyme which breaks down starch
When the iodine solution remains orange-brown, all the starch has been digested
This investigation shows:
At the optimum pH, the iodine stopped turning blue-black and remained orange-
brown within the shortest amount of time
This is because the enzyme is working at its fastest rate and has digested all the
starch
At higher or lower pH's (above or below the optimum) the iodine took a longer time to stop
turning blue-black or continued to turn blue-black for the entire investigation
This is because on either side of the optimum pH, the enzymes are starting to become
denatured and as a result are unable to bind with the starch or break it down
Limitations
The starch and amylase solutions that need to be used should be placed in a water bath at
optimum temperature before being used
A colorimeter can be used to measure the progress of the reaction more accurately by
measuring the absorbance/transmission of light through the coloured solution
A control of iodine solution would be used for comparison
A graph showing the optimum pH for an enzyme from a region of the small intestine
Page 31 of 32
When working with practical investigations, remember to consider your CORMS evaluation YOUR NOTES

CORMS Evaluation
C - We are changing the pH of the environment
R - We will repeat the investigation several times to ensure reliability
M1 - We will measure the time taken for
M2 - the iodine to stop turning black
S - We will control the concentration and volume of the amylase, iodine and starch
solution used in the investigation
 Exam Tip
When describing the effect of pH on enzyme activity, it is important to remember
that any pH outside of the optimum can lead to the enzyme becoming permanently
denatured.
Page 32 of 32

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2.7 Chemical Elements in Biological Molecules YOUR NOTES

2.8 Structure of Carbohydrates, Proteins & Lipids YOUR NOTES

The structure of a triglyceride

Amino acids join together to form proteins

Every enzyme has a different shaped active site-specific to one substrate

2.9 Practical: Food Tests YOUR NOTES

The Benedict's test for glucose

Test for starch using iodine YOUR NOTES

In the presence of starch, iodine will turn from brown to blue-black

The Biuret test for protein

The ethanol test for lipids

2.10 Role of Enzymes YOUR NOTES

Enzymes as Biological Catalysts YOUR NOTES

How enzymes work

2.11 Temperature & Enzyme Function YOUR NOTES

Factors Affecting Enzyme Action: Temperature YOUR NOTES

Effect of temperature on enzyme activity

Graph showing the effect of temperature on the rate of enzyme activity

2.12 Practical: Investigating Temperature & Enzyme Activity YOUR NOTES

Practical: Enzymes & Temperature YOUR NOTES

Investigating the effect of temperature on enzyme activity

Amylase is an enzyme which breaks down starch YOUR NOTES

2.13 pH & Enzyme Function YOUR NOTES

Factors Affecting Enzyme Action: pH YOUR NOTES

Effect of pH on enzyme activity

2.14B Practical: Investigating pH & Enzyme Activity YOUR NOTES

Practical: Enzymes & pH YOUR NOTES

Investigating the effect of pH on enzyme activity YOUR NOTES

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