gcse enzymes worksheet

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Enzymes teaching resources

Worksheets and lesson ideas to challenge students aged 11 to 16 to think hard about enzymes  (gcse and key stage 3).

Overview: enzymes are protein molecules that act as catalysts , speeding up chemical reactions without themselves getting used up. Each enzyme will only speed up a specific reaction, for example, catalase will speed up the decomposition of hydrogen peroxide into water and oxygen but it will not speed up the breakdown of starch into glucose. Enzymes (e.g. catalase) have active sites with specific shapes that bind to the substrate molecule (e.g. hydrogen peroxide) forming an enzyme-substrate complex. The enzyme-substrate complex then breaks down into the enzyme and product, allowing the enzyme to go on and react with another substrate molecule. Temperature and pH affect enzyme function because they can change the shape of the enzyme’s active site, preventing it from binding to the substrate, just as a broken lock will no longer fit the key. When the shape of an enzyme changes we call this denaturation. Any factor that increases the frequency of collisions between enzymes and substrates (increasing concentration, surface area or temperature) will increase the rate of reaction .

Big idea: organisms are organised on a cellular basis and have a finite life span

Key concept:  enzymes are protein molecules with specific shapes that speed up chemical reactions without being used up. Factors such as concentration, temperature and pH affect enzyme action.

Prior knowledge: rates of reaction ; bonding ; catalysts and activation energy

Teaching resources

Where to start.

The decomposition of hydrogen peroxide is a great place to begin thinking about enzymes. The decomposition of hydrogen peroxide into water and oxygen will happen spontaneously, but the addition of a catalyst e.g. catalase will speed this reaction up. Don’t believe me?! Then have a go at the decomposition of hydrogen peroxide demonstration using MnO2 (a chemical catalyst) and a piece of liver (containing catalase, a biological catalyst). Heat the liver and it no longer works. This will then begin an exploration of denaturation.

Modelling enzyme action

One of the best ways to help students understand enzyme action is to build Plasticine models of enzymes breaking down (or building up) substrate molecules. Students can modify the models to show denaturation and the effects of temperature, inhibitors and pH. Make sure you stress the different effects of temperature – denaturation versus collision theory. If possible, ask students to film their models and add annotations to help them consider the dynamic nature of enzyme action.

What do enzymes look like?

The Protein Data Bank provides some beautiful structures of enzymes.

Factors that affect enzyme action

GCSE activity for students to apply their knowledge of enzymes . Students work in pairs to apply their understanding of factors that affect enzymes. They will need to consider pH, temperature and enzyme specificity. This activity assesses and consolidates learning by asking students to apply their knowledge to novel situations. ( PDF )

Thinking deeper

• What does lemon juice, snake venom and cyanide have in common?
• Why can you make pineapple jelly from tinned pineapple but not fresh pineapple?
• When we cool an enzyme reaction the rate of reaction decreases. Do enzymes denature at low temperatures?
• How does decreasing the pH cause denaturation?
• Why do you die of heat stroke?

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Required Practical: Enzymes ( AQA GCSE Biology )

Revision note.

Biology Lead

Enzyme required practical

• Aim: To investigate the effect of pH on the rate of reaction of amylase
• Use the enzyme amylase to breakdown starch at a range of pH values, using iodine solution as an indicator for the reaction occurring
• Use a continuous sampling technique to monitor the progress of the reaction
• Amylase is an enzyme that digests starch (a polysaccharide of glucose) into maltose (a disaccharide of glucose)
• Starch can be tested for easily using iodine solution

Iodine can be used qualitatively to indicate the presence or absence of starch from a sample

• Place single drops of iodine solution in rows on the tile
• Label a test tube with the pH to be tested
• Use the syringe to place 2cm 3 of amylase in the test tube
• Add 1cm 3 of pH buffer solution to the test tube using a syringe
• Use another test tube to add 2cm 3 of starch solution to the amylase and buffer solution, start the stopwatch whilst mixing using a pipette
• After 10 seconds, use a pipette to place one drop of the mixture on the first drop of iodine, which should turn blue-black
• Wait another 10 seconds and place another drop of the mixture on the second drop of iodine
• Repeat every 10 seconds until iodine solution remains orange-brown
• Repeat experiment at different pH values – the less time the iodine solution takes to remain orange-brown, the quicker all the starch has been digested and so the better the enzyme works at that pH

Investigating the effect of pH on enzyme activity

Adjustments to the method

• The above method can be adapted to control temperature by using a water bath at 35°C
• All solutions that need to be used (starch, amylase, pH buffers) 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; with a solution containing starch being darker and glucose light (as a result of the colour-change of iodine) – this will affect the absorbance or transmission of light in a colorimeter

Describing and explaining experimental results for enzyme experiments is a common type of exam question so make sure you understand what is happening and, for a 7, 8 or 9, can relate this to changes in the active site of the enzyme when it has denatured.

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Author: Lára

Lára graduated from Oxford University in Biological Sciences and has now been a science tutor working in the UK for several years. Lára has a particular interest in the area of infectious disease and epidemiology, and enjoys creating original educational materials that develop confidence and facilitate learning.

Enzymes are biological catalysts – protein molecules that speed up chemical reactions. They catalyse chemical reactions in living cells such. Examples of these chemical reactions are:

• Respiration
• Photosynthesis
• Protein synthesis

Active Sites

The shape of an enzyme determines how it works. Enzymes have active sites that substrate molecules (the substances involved in the chemical reaction) fit into when a reaction happens.

The active site has to be the right shape for the substrate molecules to fit into. This means that enzymes have a high specificity for their substrate – a particular type of enzyme will only work with one or a smaller number of substrates. The animation shows how this works:

The mechanism involved is called the ' lock and key ' mechanism. Just as a lock will only accept one key, an enzyme will only accept one substrate.

Enzyme-catalysed reactions

Enzymes work best at particular temperatures and pH values.

Enzymes and Temperature

At low temperatures, enzyme reactions are slow. They speed up as the temperature rises until an optimum temperature is reached. After this point the reaction will slow down and eventually stop. The graph shows what happens to enzyme activity when the temperature changes.

In the example above, enzyme activity increases steadily. It peaks (the enzyme's optimum temperature) then decreases rapidly.

Enzymes and pH

Different enzymes work best at different pH values, their optimum pH . Many enzymes work fastest in neutral conditions. Making the solution more acidic or alkaline will slow the reaction down. At extremes of pH the reaction will stop altogether.

Some enzymes, such as those used in digestion, are adapted to work faster in unusual pH conditions. For example, stomach enzymes have an optimum pH of 2, which is very acidic.

The graph shows what happens to enzyme activity when the pH changes.

In the example above, enzyme activity increases, it peaks then decreases.

• Unlock Enzyme Action!

Understand Lock and Key Theory to Explain Enzyme Action

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EdPlace's GCSE Home Learning Biology Lesson: Enzymes

Looking for short lessons to keep your child engaged and learning? Our experienced team of teachers have created English, maths and science lessons for the home, so your child can learn no matter where they are.  And, as all activities are self-marked, you really can encourage your child to be an independent learner.  

Get them started on the lesson below and then jump into our teacher-created activities to practice what they've learnt. We've recommended five to ensure they feel secure in their knowledge - 5-a-day helps keeps the learning loss at bay (or so we think!).

Are they keen to start practising straight away? Head to the bottom of the page to find the activities. 

Now...onto the lesson!

Enzymes: Controlling all Reactions in Living Organisms

Biology is often seen as the easier of the sciences by many students, but this is a mistake that leads some students to not learn content in enough detail. During assessments, this can result in students not being able to fully apply and explain their understanding when presented with new examples. Enzymes are vital in Biology and students should ensure they learn them in detail as they're likely to appear in any terminal Biology GCSE examination.

Whilst initially enzymes may appear to be a small and straight forward topic, they're one of the most commonly assessed application and practical questions for GCSE Biology courses. This means that students must know how an enzyme works, and be able to link this to data on the effects of temperature or pH on the rate of reactions. 

As a parent, this may seem daunting but all temperature practical questions for enzymes will be looking for students to apply the same basic understanding of enzymes. This is also important information that needs to be taken forward by those planning on studying A-Level Biology.

At EdPlace we’re surrounded by a team of experts who communicate these concepts with children on a day-to-day basis, and we’re ready to share their teaching gems with you. We're confident if you follow this step by step approach your child will:

1) Understand  how enzymes work via Lock and Key Theory

2) Apply  Lock and Key Theory to explain how temperature affects the rate of enzyme-controlled reactions 

3) Analyse and  Explain   the temperature-rate of a reaction graph

Step 1: Breaking Down the Terminology

Before we look at how temperature affects the rate of enzyme-controlled reactions, we must first understand some key scientific terminology. These terms will be reinforced during this step-by-step approach, so that your child is able to recall their meanings.

An enzyme is a biological catalyst. This means that they speed up the rate of chemical reactions in cells.

The active site is where the reaction happens in an enzyme. It has a specific shape.

The substrate is the molecule involved in the reaction which fits into the active site of the enzyme. 

Enzymes can become denatured which is effectively when the enzyme changes shape permanently and no longer works.

The rate of reaction is how fast a reaction happens.

Step 2: Prior Knowledge Needed

For all living things to stay alive they must continually complete chemical reactions in their cells. All reactions happen in the cytoplasm of the cell and are controlled by enzymes .

Enzymes are biological catalysts . This means they speed up  the rate of reaction and do so by lowering the activation energy of a reaction (the energy needed to start a reaction).

Students should already know that enzymes are an important part of digestion breaking large insoluble molecules down to smaller soluble molecules. They should be able to recall the three following digestive enzymes:

Step 3: Introducing the New Skill

Enzymes are specific to the substrate they work with. So, for example in the table above, only the enzyme protease will digest proteins into amino acids. Protease cannot digest starch or lipids.

This can be explained by looking a little closer at how an enzyme works:

Enzymes have a specific shaped area called the active site . 

This is where the substrate (B) attaches to the enzyme allowing the reaction to happen.

As you will see in the diagram the substrate fits into the active site as they have a complementary shape. A differently shaped substrate will not fit into the active site and reaction will not continue.

This is called the Lock and Key Theory which states that enzymes are specific to one type of substrate as they have an active site that has a complementary shape to one substrate type only.

Once the substrate has fitted perfectly into the active site it forms an enzyme-substrate complex (C). Here, the enzyme causes the reaction to happen, in this example pulling the large substrate molecule into two smaller molecules by breaking the bonds holding it together.

The new products formed will now have a new shape and are released from the active site as a result (D). The enzyme is then ready to accept another substrate and can be constantly reused.

The effect of temperature on the rate of enzyme-controlled reactions :

Students need to understand how temperature affects the rate of enzyme-controlled reactions. All enzymes have an optimum temperature , which is the temperature at which the most enzyme-substrate complexes form. As you move away from this temperature the rate of reaction falls.

Students need to be able to explain what they can see on a graph, plotting the temperature against the rate of reaction for any practical. This may sound daunting, but the graph is always identical.

This graph is used to assess a student’s understanding of enzyme structure and the effect of temperature on it. Most students understand it, but often only half answer a question based upon this.

Imagine the student is given the following exam question:

Use the graph to describe and explain the effect of temperature on the rate of enzyme activity (6 marks).

To gain the full six marks students must talk about the graph both before and after the optimum temperature. Often students only remember to explain the effect of higher temperatures and while they may do this in detail, it'll only give them 3 of the possible 6 marks.

Effect of increasing temperature from 0 ° C to 40 ° C :

As the temperature increases so does the rate of enzyme activity.

This is because the enzymes and the substrates gain more kinetic energy and move at a faster rate.

Therefore, they collide more frequently and form more enzyme-substrate complexes. 

The optimum temperature for this enzyme is 40°C which is where the rate of making new enzyme-substrate complexes is highest.

Effect of increasing temperature above 40°C (optimum temperature):

Above the optimum temperature, the rate of enzyme activity rapidly decreases.

This is because the particles make the enzyme vibrate which breaks bonds, changing the shape of the active site.

The active site is no longer a complementary shape to the substrate and the substrate no longer fits into the enzyme, so the reaction stops. The enzyme is denatured , and this is permanent .

Step 4: Give it a Go!

Why not apply what you've learnt from this step-by-step lesson to attempt to the following questions?

a) Explain what Lock and Key Theory is (3 marks)

b) Why does the rate of an enzyme-controlled reaction increase up to the optimum temperature? (3 marks)

c) Why does the rate of reaction drop above the optimum temperature of an enzyme? (3 marks)

Stretch and challenge:

d) Why is human body temperature important to maintain at about 37°C? (4 marks)

e) Enzymes also have a specific pH. What may happen to the structure of an enzyme in the wrong pH which will decrease the rate of enzyme activity? (3 marks)

Step 5 - Putting it into Practice

Now, you’ve covered this together why not put this to the test and assign your child the following 5 activities in this order.

All activities are created by teachers and automatically marked. Plus, with an EdPlace subscription, we can automatically progress your child at a level that's right for them. Sending you progress reports along the way so you can track and measure progress, together - brilliant!

Activity 1 - Identify and Describe Key Features of Eukaryotes and Prokaryotes

Activity 2 - Describe Enzyme Function

Activity 3 - Understand Enzyme Function

Activity 4 - Describe the Enzymes in the Digestive System

Activity 5 - Understand Hormones and Homeostasis

a) The Lock and Key Theory explains why enzymes increase the rate of reaction for one substrate only (specific). The active site of the enzyme has a complementary shape in which the substrate fits perfectly. This forms an enzyme-substrate complex and then the reaction can proceed.

b) The rate of an enzyme-controlled reaction increases up to the optimum temperature because as the temperature increases, the enzymes and the substrates gain more kinetic energy. As a result, they collide more frequently and form more enzyme-substrate complexes. 

c) The rate of reaction decreases above the optimum temperature of an enzyme because the energy gains too much energy and its particles vibrate to the point where they break bonds in the enzyme. This causes the active site to change shape, so it's no longer a complementary shape to the substrate. The substrate can no longer fit into the active site and no more enzyme-substrate complexes can form. Therefore, the reaction stops.

Stretch and challenge :

d) Human body temperature needs to be maintained at about 37°C because this is the optimum temperature for the enzymes in our cells. If the temperature drops too much below this the enzymes and substrates will have less kinetic energy and collide less frequently reacting slower. If the temperature increases too high above this, the enzymes will become denatured and the active site changes shape. This means they can no longer form enzyme-substrate complexes and the reactions stop.

e) Enzymes have a specific pH which is where they form the most enzyme-substrate complexes and have the highest rate of reaction. At the wrong pH, enzymes are denatured and their active site changes shape. This means the active site is no longer a complementary shape to the substrate which can no longer fit into it. Therefore, no more enzyme-substrate complexes can form and the rate of reaction decreases.

Keep going! Looking for more activities, different subjects or year groups?

Click the button below to view the EdPlace English, maths, science and 11+ activity library

All English, maths and science from Year 1 - GCSE

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WRITTEN BY: Mr Philips – SCIENCE TEACHER

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Enzymes Worksheets

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GCSE Biology (9-1) - Digestive Enzymes - Worksheet

Subject: Biology

Age range: 14-16

Resource type: Worksheet/Activity

Last updated

16 November 2018

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This worksheet explores where digestive enzymes are made, what they breakdown, and what they produce.

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Thanks for these - I recently discovered your wonderful videos on YouTube and have been using them for a boy that I teach (he is being home-schooled). I've been getting him to watch a video for homework, and complete a worksheet that I make (to make sure he has watched it!). Then we go over it at the start of the lesson then reinforce what he's learned with other activities. Currently doing Chemistry & Physics, but I'll let his Biology tutor know about these.

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