The Big Picture: Enzymes
The Big Picture: Enzymes
The Big Picture: Enzymes
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Enzymes
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5.1.1 () Contents
5.1.2 () 5.1.0 The big picture ()
5.1.1 Enzymes as catalysts ()
5.1.3 ()
5.1.2 Enzyme specificity (E) ()
5.1.4 () 5.1.3 Enzyme activity and temperature (E) ()
5.1.4 Practical: Effect of temperature on enzyme activity ()
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5.1.5 Practical: Effect of pH on enzyme activity ()
Section 5.1.0
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Credit: Skarie20, Getty Images
Enzymes control chemical and biological reactions. The ones in biological powders break down fat, oil and protein
molecules into smaller molecules which will dissolve in water. This makes it much easier to remove stains such as egg
from clothes. Enzymes stop working if they get too hot, which is one reason why you are encouraged to wash clothes at
low temperatures. This also has the benefit of saving energy and reducing the chance of shrinking your clothes in the
wash (Figure 2).
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Before you move on to the next section, read through the learning outcomes below and answer the section questions to
check that you have the prior knowledge required to understand this subtopic.
Learning intentions
By the end of this subtopic, you will be able to:
5.1 () explain how enzymes function as biological catalysts that are essential for life
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Section questions
- Hide 3 questions
Question 1
Multiple choice
What is the building block of proteins (what are they made of)?
Choices
Correct choice #1
Amino acids
Answer explanation
Amino acids are the smallest unit, building block, of a protein. Glucose is a building block for carbohydrates.
Glycerol and fatty acids are components of fats and oils.
#2
Glucose
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Glycerol
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Fatty acids
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Question 2
5.1.5 () Short text
True or false?
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Proteins are composed of the elements C, N and O only.
Correct answers
False
F
Answer explanation
Question 3
Short text
True or false?
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Correct answers
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True
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5.1.5 () Answer explanation
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This is the generalised structure of an amino acid.
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Section 5.1.1
Enzymes as catalysts
A catalyst is a substance that increases the rate of a reaction, but is not changed by the reaction. For example,
manganese dioxide powder catalyses the breakdown of hydrogen peroxide to form water and oxygen. Watch this video
to see what can happen.
Using Manganese Dioxide As a Catalyst to Decompose Hydrogen Per…
Per…
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If you add 1 g of manganese dioxide to some hydrogen peroxide, you will still have 1 g of manganese dioxide after the
reaction. Its mass stays the same and it is not changed chemically.
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5.1.4 () Figure 1. Going from a starting molecule to a product in three reactions, each controlled by an enzyme.
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5.1.6 () If one of the enzymes was missing, the product may be made very slowly or not at all:
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one of the reactions may happen very slowly, increasing the time needed to make the product
one of the reactions may happen in a different way, producing an unwanted substance that cannot take part in the
other reactions.
Without enzymes, the rate of reactions in living organisms would be too slow to sustain life. For example, digestive
enzymes are needed to break down the substances in food so they can be absorbed by the body:
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Exercise questions
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+ Show 1 question
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Enzyme action
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Each type of enzyme has a specific and unique shape. The shape of an enzyme fits the reactants in the reaction
catalysed by the enzyme. A reactant in an enzyme-catalysed reaction is called the substrate. The substrate attaches to a
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particular enzyme in a specific way – rather like a key fitting a particular lock. Figure 2 shows an example of how this
works.
Figure 2. The enzyme and the substrate fit together like the pieces of a jigsaw. Their shapes are complementary.
This is often called the ‘lock and key model’ of enzyme action. The shape of an enzyme’s active site and its substrate
are described as being complementary. In an enzyme-catalysed reaction:
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1. The substrate fits into the part of the enzyme with a complementary shape, the active site.
5.1.1 () 2. The reaction happens.
5.1.2 () 3. The product or products of the reaction leave the enzyme’s active site.
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Once the products have left an enzyme molecule, the enzyme is ready for another substrate molecule to attach to it. This
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can happen extremely quickly. For example, catalase is an enzyme that breaks down hydrogen peroxide. It can break
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The activity of enzymes is affected by changes in temperature and pH. If the temperature gets too high, some of the
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bonds holding the enzyme together will break and its shape will change. This means the substrate will no longer fit and
the reaction cannot take place. If the pH gets too low or too high, it also disrupts the bonds of the enzyme and changes
its shape. This change to the enzyme is called denaturation.
Section questions
- Hide 3 questions
Question 1
Multiple choice
Choices
Correct choice
#1
To catalyse a reaction, so it takes place more quickly.
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Answer explanation
5.1.0 () Enzymes act as biological catalysts. They increase the rate of reactions.
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#2
5.1.2 () To make a reaction slower, so it can be controlled more easily.
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#3
5.1.4 () To alter the taste of a food.
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#4
5.1.6 () To provide energy during a reaction.
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Question 2
Multiple choice
Choices
Correct choice #1
-ase
Answer explanation
Enzymes end in the suffix ‘-ase’. For example, protease is an enzyme that breaks down protein.
#2
-ese
#3
-ate
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-ose
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Question 3
5.1.3 () Multiple choice
5.1.5 () Choices
Correct choice #1
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The way that a particular enzyme fits with a specific substrate.
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Answer explanation
The lock and key model explains why particular enzymes only affect specific substrates. The lock represents the
shape of the enzyme and the key represents the shape of the substrate.
#2
The action of the substrate on the enzyme.
#3
The rate at which a product is created in a catalysed reaction.
#4
The way an enzyme works is secret.
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Section 5.1.2
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Enzyme specificity (E)
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Extended
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Enzymes show specificity – each type only works for one reaction, or a very small number of reactions. This is
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because of a part of the enzyme molecule called the active site.
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The active site has a particular shape that only the correct substrate (or a very similarly shaped molecule) can
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fit into. The shapes of the active site and substrate are described as being complementary. The enzyme and
substrate fit together to make an enzyme–substrate complex, allowing the reaction to happen. The products are
then produced and will detach from the enzyme making it available to catalyse another reaction.
Activity
Use the following drag and drop activity to check your understanding of the interactions involved in
enzyme-controlled reactions.
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/
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G
Active site Enzyme
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G
Enzyme–substrate Substrate
complex
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Check
As the substrate enters the active site, the shape of the active site may alter slightly to allow a better fit. It also
increases the attractive forces between the substrate and active site in the enzyme.
Denaturation
The shape of an enzyme molecule depends on factors such as:
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its sequence of amino acids
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attractive forces between different parts of the molecule.
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The sequence of amino acids cannot change (unless the protein molecule is digested using very hot acid or
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protease enzymes) but the attractive forces can be changed. They can be weakened or broken. When this
5.1.3 () happens, the shape of the enzyme and its active site change. The enzyme can no longer function and is
5.1.4 () described as being denatured.
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5.1.7 () Remember, enzymes are not living things, so do not refer to denatured enzymes as dead enzymes. They
were never alive.
This process of denaturation happens if the pH of the enzyme’s surroundings change, or if its temperature gets
too high.
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This is important for their correct function. Pepsin is a protease that works in the stomach, which is acidic.
Salivary amylase works in the mouth, which is very slightly alkaline.
Section questions
- Hide 3 questions
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Question 1
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Multiple choice
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Extended
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What is the active site of an enzyme?
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5.1.4 () Choices
Correct choice #1
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It is the site on an enzyme at which substrates bind.
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Answer explanation
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The active site is the region of an enzyme at which the substrate(s) bind. This leads to the reaction being catalysed
and the product(s) being formed.
#2
It is a group of amino acids lined up in a unique sequence.
#3
It is the site at which an enzyme attaches to another enzyme.
#4
It is the site at which the enzyme increases its catalytic activity.
Question 2
Multiple choice
Extended
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What is denaturation of an enzyme?
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Choices
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Correct choice #1
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A permanent change in the shape of the enzyme that alters its properties.
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Answer explanation
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When an enzyme is denatured, its shape is permanently changed by high temperatures or extremes of pH. These
5.1.5 () changes alter the shape of the active site so that the substrate(s) no longer fits and the enzyme can no longer
5.1.6 () catalyse a reaction.
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#2
A change in the substrate with which the enzyme works.
#3
A lower rate of reaction at a lower temperature.
#4
An increase in the activation energy needed by an enzyme.
Question 3
Multiple choice
Extended
Amylase is an enzyme that breaks down starch into simpler sugars. An experiment was carried out to
determine its optimum conditions. At which pH would you predict amylase to have the highest activity?
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Choices
7
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Amylase breaks down starch into simpler sugars in the mouth, with an optimum activity at pH 7.
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#2
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2
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#3
5
#4
10
Section 5.1.3
There will be no reaction if the particles do not collide, or if they do not have enough kinetic energy. A
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collision that results in a chemical reaction is described as an effective collision .
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5.1.5 () The greater the frequency of effective collisions, the greater the rate of reaction.
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Figure 1 shows a reaction profile diagram for a reaction. It shows how the energy of the reacting substances
changes during the reaction. Notice how the activation energy is lower with the enzyme (dashed line) than it is
without the enzyme (solid line).
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A lower activation energy means that a greater proportion of collisions will be effective. As a result of this, the
frequency of effective collisions will be higher with a catalyst present. This increases the rate of reaction.
Study skills
Take care to discuss the frequency or rate of collisions, not the number of collisions. This is because, given
enough time, even a very slow reaction will have a lot of collisions.
Exercise questions
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- Hide 1 question
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Question 1
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Multiple choice
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5.1.3 () Extended
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How do enzymes affect the activation energy of a reaction?
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Choices
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Answer explanation
Enzymes increase the rate of reactions by lowering the activation energy required for the reaction to take place.
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Figure 2. Effect of increasing temperature on the rate of an enzyme-catalysed reaction.
You should see from Figure 2 that the rate of reaction increases as the temperature increases from 0 °C.
However, it reaches a peak at about 37 °C, then decreases until it becomes zero just under 60 °C. This happens
because of denaturation.
As the temperature increases, attractive forces between different parts of the enzyme molecule weaken or
break. The shape of the active site changes and no longer fits the substrate, the enzyme becomes denatured and
so no longer functions. This is why the rate of reaction decreases when the temperature becomes too high. The
temperature at which the enzyme activity is highest is called the optimum temperature .
Exercise questions
- Hide 1 question
5.1 () Question 1
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Multiple choice
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5.1.2 () Extended
5.1.3 () Why does an increase in temperature increase the rate of reaction up to a maximum?
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Choices
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Correct choice
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5.1.7 () The increase in temperature increases the kinetic energy of the molecules. This increases the chances of collisions
between the substrate and the enzyme’s active site.
Answer explanation
The increase in temperature increases the kinetic energy of the molecules. As a result, the molecules move more
and faster. This means they are more likely to collide with the active site of the enzyme, so the rate of reaction
increases.
The increase in temperature causes the molecules to vibrate more, so they can be broken down more easily.
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5.1.2 () Extended
5.1.3 () Different enzymes have different optimum temperatures. Enzymes in our bodies work best at around 37 °C, but
5.1.4 () this is not true of the enzymes in all living organisms (Figure 3).
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Figure 3. These tube worms live in extremely hot water far below the surface of the sea. Their enzymes denature at
high temperatures and have high optimum temperatures.
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Section questions
- Hide 3 questions
Question 1
Multiple choice
Extended
What are two factors that alter the rate of an enzyme-catalysed reaction?
Choices
Correct choice #1
pH and temperature
Answer explanation
Every enzyme has an optimum pH and an optimum temperature. Changes away from the optimum decrease the
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rate of reaction.
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High temperature and fewer collisions with the active site.
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Acidic pH and room temperature.
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Only low temperatures and high pH levels.
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5.1.7 () Question 2
Multiple choice
Extended
What would you expect to happen when an enzyme is placed in a solution with pH 2 at a temperature close to
40 °C?
Choices
Correct choice #1
If those are the optimum conditions for the enzyme, the rate of reaction will reach a maximum.
Answer explanation
#3
5.1.0 () The enzyme will not work until the temperature increases to its optimum.
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#4
5.1.2 () The enzyme will work but the rate of reaction will be slower than it would be at a neutral pH.
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5.1.4 () Question 3
Multiple choice
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Extended
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The graph below shows the effects of increasing the temperature on the rate of an enzyme-controlled reaction.
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Which process occurs to cause the rate of reaction to suddenly decrease?
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Choices
5.1.0 () #1
Correct choice
5.1.1 () denaturation
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Answer explanation
5.1.3 () As the temperature increases, there is more energy available for the enzymes, which increases the rate of reaction.
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The sudden decrease in the rate of reaction is caused by the enzymes changing shape as the temperature has risen
too much. This change in shape, known as denaturation, prevents the enzymes from being able to catalyse the
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reaction.
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5.1.7 () #2
homeostasis
#3
saturation
#4
oxidation
Section 5.1.4
Practical: Effect of temperature on enzyme activity
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5.1.1 () Aim
5.1.2 () To investigate the effect of temperature on the rate of an enzyme-controlled reaction.
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5.1.4 () Safety
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A full risk assessment must be carried out before starting this practical activity (see section 0.0.1
5.1.6 () (/schoolstaff/app/cambridge-igcse-biology-fe2023/book/introduction/introduction/introduction-and-key-features/) for
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more information).
five water baths set at 20 oC, 30 °C, 40 °C, 50 °C and 60 °C with test tube racks in each
ten test tubes
5 cm3 of 5% lipase solution
35 cm3 of 0.05 M sodium carbonate solution
thermometer
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glass stirring rod
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25 cm3 milk (full fat preferred or semi-skimmed)
5.1.1 () two 10 cm3 measuring cylinders
5.1.2 () 2 cm3 syringe
stopwatch
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phenolphthalein in a dropper bottle.
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5.1.5 () Phenolphthalein indicator is not part of the syllabus. It is used in this practical as it can detect the specific point at which
5.1.6 () an alkaline solution is neutralised as it changes from pink to colourless. Universal indicator is used to determine the
approximate pH of a solution. If used in this practical, it would be much harder to identify the end point.
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Table 1. Time taken for lipase to break down fats in milk at different temperatures.
20 300 3.3
Temperature / °C Time taken / s Rate of reaction
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30 190 5.3
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50 240 4.2
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Worked example 1
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Convert the 300 seconds taken for a reaction to occur into the rate of that reaction.
1
Rate of reaction = ( ) × 1000
300
Figure 1 shows these results plotted on a graph of time against temperature. The greater the rate of reaction, the sooner
the colour will change from pink to clear, and the lower the time recorded.
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5.1.7 () Figure 1. Line graph showing the effect of temperature on the time taken for lipase to break down fats in milk.
Figure 2 shows the results of the calculated rate of reaction against temperature. Note that the reaction is fastest and the
graph peaks at 40 °C which is closest to the enzyme’s optimum temperature.
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Figure 2. Line graph showing the effect of temperature on the rate of reaction for lipase breaking down fats in milk.
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Exercise questions
- Hide 1 question
Question 1
Multiple choice
How would you expect the optimum temperature of enzymes in a fish living in the Arctic to differ from enzymes in
humans?
Choices
Correct choice
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The optimum temperature of the fish’s enzymes would be lower.
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Answer explanation
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5.1.2 () As the fish live in a very cold environment and their body is the same temperature as the water, their enzymes need
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to work best at these lower temperatures.
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The optimum temperature of the fish’s enzymes would be higher.
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The optimum temperature of the fish’s enzymes would be the same as for a human’s enzymes.
Conclusion
This investigation should show you how temperature affects the breakdown of fats in milk by the enzyme lipase. At low
temperatures the kinetic energy of the molecules is too low for effective collisions to occur, making the breakdown rate
very low. As the temperature increases, so does the kinetic energy of the molecules, causing more effective collisions.
Once the temperature exceeds the optimum temperature of the enzyme, it begins to denature, slowing the reaction.
Watch the following video to see another way to investigate the effect of temperature on an enzyme-controlled reaction.
Effect of temperature on digestion of starch by amylase
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Section questions
- Hide 3 questions
Question 1
Multiple choice
An investigation showed that the rate of an enzyme-catalysed reaction was fastest at 20 °C. Based on this information,
which of the following statements is true?
Choices
Correct choice #1
The rate of reaction will be slower when the temperature is less than its optimum value.
Answer explanation
Different enzymes have different optimum temperatures. The optimum temperature is the temperature at which the
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enzyme works best. Although many enzymes have an optimum temperature of 37 °C, we know from the
investigation that the optimum temperature for this enzyme is 20 °C.
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#2
This is a human enzyme.
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#3
The rate of reaction will be faster when the temperature is close to 37 °C.
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#4
The enzyme is not working properly.
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Question 2
Multiple choice
Choices
Correct choice #1
It is a pH indicator.
Answer explanation
#2
It will cause the fats in the milk to break down more rapidly.
#3
It will prevent the pH of the milk from changing.
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#4
5.1.0 () It will keep the lipase enzyme from denaturing.
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5.1.2 () Question 3
Multiple choice
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How would you increase the reliability of this investigation?
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Choices
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Correct choice #1
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Carry out repeats.
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Answer explanation
#2
Have two people record the time and take an average of the two.
#3
Record the colour change with a camera to find the exact time the colour disappeared.
#4
Use a pH probe to measure the change in pH instead of the phenolphthalein.
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Section 5.1.5
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Practical: Effect of pH on enzyme activity
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Aim
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To investigate the effect of pH on the rate of an enzyme-controlled reaction.
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Safety
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A full risk assessment must be carried out before starting this practical activity (see section 0.0.1
(/schoolstaff/app/cambridge-igcse-biology-fe2023/book/introduction/introduction/introduction-and-key-features/) for
more information).
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Running your experiment
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1. Place the beakers containing buffer solutions in the water bath set at 25 °C.
2. Place containers of starch solution and amylase solution in the water bath.
3. While you are waiting for the solutions to reach 25 °C, use a dropping pipette to add one drop of iodine solution to
each depression on a spotting tile.
4. Transfer 2 cm3 of one of the buffer solutions to a clean test tube in the water bath.
5. Add 2 cm3 of amylase solution to the test tube.
6. Add 2 cm3 of starch solution to the test tube. This gives you 6 cm3 of a buffer/amylase/starch mixture in the water
bath at 25 °C.
7. Start a stopwatch.
8. Mix the contents of the test tube using a glass rod.
9. Immediately remove a drop of the mixture with the glass rod and place it into the first depression on the spotting
tile. The iodine solution should turn blue-black, indicating the presence of starch in the mixture (see Figure 1).
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11. Use the glass rod to transfer a drop of mixture from the test tube to the next
12. Continue steps 10 and 11 at 30 second intervals until the iodine solution
13. Stop the stopwatch. Record this time and the pH of the buffer solution in a table.
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pH of solution Time taken / s Rate of reaction
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5.0 more than 360 0
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6.0 90 11.1
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Worked example 1
Convert the time of 120 seconds taken for a reaction to occur into the rate of that reaction.
1
Rate of reaction = ( ) × 1000
120
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Rate of reaction = 8.3
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Question 1
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Multiple choice
5.1.7 ()
Salivary amylase is produced by the salivary glands around the mouth. What will happen to this enzyme when it
reaches the acidic conditions of the stomach?
Choices
Correct choice
Answer explanation
The salivary amylase will be denatured by the stomach acid and will no longer break down starch.
It will be modified by the acid and will begin to digest protein.
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Figure 2 shows these results plotted on a graph of time against pH. The greater the rate of reaction, the sooner the
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reaction will be completed and the lower the time recorded.
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Figure 2. Line graph showing the effect of pH on the time taken for amylase to completely break down starch.
Figure 3 shows the results of the calculated rate of reaction against pH. Note that the reaction is fastest and the graph
peaks at a pH of 6.0, which is closest to the enzyme’s optimum pH.
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Figure 3. Line graph showing the effect of pH on the rate of reaction for amylase breaking down starch.
Conclusion
This investigation should show you how pH affects the breakdown of starch by the enzyme amylase. When the pH is
too high or too low, the bonds holding the enzyme molecule in its shape will be disrupted by the extreme pH values and
the enzyme denatures. The enzyme will function at its highest rate at its optimum pH.
Watch the following video to see another way to investigate the effect of pH on an enzyme-controlled reaction.
Effect of Changing pH on Enzyme Activity Lab
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Section questions
- Hide 3 questions
Question 1
Multiple choice
Why should the glass rod be rinsed between each sampling point?
Choices
Correct choice #1
Answer explanation
All of the mixture needs to be removed between each sampling point, so that the previous sample does not
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interfere with the next sampling point.
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#2
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To stop the workbench getting dirty.
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#3
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To save time at the end of the experiment.
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#4
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As enzymes do not react in water.
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Question 2
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Multiple choice
Choices
Correct choice #1
Answer explanation
Repeated experiments allow anomalies to be identified and excluded when calculating a mean. This can help to
reduce the effects of random errors on the results.
#2
It lets you use up the whole lesson.
#3
It lets you get lots of results to use when calculating a mean.
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#4
5.1.0 () It saves time.
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5.1.2 () Question 3
Multiple choice
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In this investigation, what indicates that the starch has all been digested?
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Choices
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Correct choice #1
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Answer explanation
When the iodine remains orange/brown this indicates that there is no longer any starch in the sample to change the
colour of the iodine.
#2
The iodine turns blue-black.
#3
There is no amylase left.
#4
The iodine turns colourless.
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Summary and key terms
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All the chemical reactions in cells are controlled by enzymes. Enzymes are biological catalysts which increase the
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rate of reactions without being destroyed.
5.1.5 () Enzymes have a conformational shape which compliments the shape of the substrate which attaches at the active
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Enzyme activity is affected by environmental conditions, such as pH and temperature.
Enzymes have an ideal temperature and/or pH value where its activity is at its highest point, this is known as the
optimum.
Investigations can be carried out to observe the effects of temperature and pH on enzyme-controlled reactions.
Extended
The enzyme and substrate have a complementary or matching shape, forming enzyme–substrate
complexes.
Enzymes increase the rate of reactions. This is a result of lowering the activation energy of a reaction. The
activation energy is the energy needed to start or initiate a chemical reaction.
Temperature affects the speed of molecular movement and rate of collisions between the substrate and
enzyme. Raising the temperature will result in more collisions, increasing the reaction rate.
Key terms
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5.1.0 () Review these key terms. Do you know them all? Fill in as many gaps as you can using the terms in
this list.
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1. are and they are biological ,
5.1.3 () meaning they speed up chemical reactions in biological systems.
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3. Enzymes function best at an temperature and pH.
5.1.5 () 4. If enzymes get too hot or their pH gets too high or too low, they will .
proteins complementary
Check
Reuse
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Section 5.1.7
Checklist
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What you should know
After studying this subtopic, you should be able to:
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5.1.6 () Core
5.1.7 () Describe a catalyst as a substance that increases the rate of a chemical reaction and is not changed by the
reaction.
Describe enzymes as proteins that are involved in all metabolic reactions, where they function as biological
catalysts.
Describe why enzymes are important in all living organisms in terms of a reaction rate necessary to sustain
life.
Describe enzyme action with reference to the shape of the active site of an enzyme being complementary to
its substrate and the formation of products.
Investigate and describe the effect of changes in temperature and pH on enzyme activity with reference to
optimum temperature and denaturation.
Extended
Explain enzyme action with reference to: active site, enzyme-substrate complex, substrate and product.
Explain the specificity of enzymes in terms of the complementary shape and fit of the active site with the
substrate.
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Explain the effect of changes in temperature on enzyme activity in terms of kinetic energy, shape and fit,
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5.1.1 () Explain the effect of changes in pH on enzyme activity in terms of shape and fit and denaturation.
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