1. Arrange students into groups. Each group needs at least ONE person who has a mobile device.
2. If their phone camera doesn't automatically detect and decode QR codes, ask students to
4. Cut them out and place them around your class / school.
1. Give each group a clipboard and a piece of paper so they can write down the decoded questions and their answers to them.
2. Explain to the students that the codes are hidden around the school. Each team will get ONE point for each question they correctly decode and copy down onto their sheet, and a further TWO points if they can then provide the correct answer and write this down underneath the question.
3. Away they go! The winner is the first team to return with the most correct answers in the time available. This could be within a lesson, or during a lunchbreak, or even over several days!
4. A detailed case study in how to set up a successful QR Scavenger Hunt using this tool can be found here.
Question | Answer |
| 1. What are enzymes made up of? | Amino acids joined by peptide bonds, folded into a 3D shape. | 2. What does the enzyme protease, amylase and lipase break down? | Protease- proteins, amylase- carbohydrates and lipase- lipids. | 3. What is the area of the enzyme called that substrates bind to? | Active site. | 4. Explain the lock and key mechanism. | Where the enzyme's active site is complementary to the substrate. | 5. Define the term 'activation energy'. | The energy required for the reaction to take place. | 6. How do enzymes affect the activation energy? | Enzymes reduce the activation energy. | 7. Define the term 'denatured'. | The loss of the shape of the enzyme and its active site so the enzyme-substrate complex can no longer form. | 8. What is a buffer? | A solution used to control the pH during enzyme investigations. | 9. How is the induced fit hypothesis different to the lock and key hypothesis? | The induced fit hypothesis suggests the enzyme can change shape to fit around a substrate (a bit like a glove). | 10. What is meant by a non-competitive inhibitor? | An inhibitor which binds to an area on the enzyme other than the active site to alter the active site shape and therefore render the enzyme inactive. | 11. What is meant by a competitive inhibitor? | An inhibitor that competes to bind with the active site, reducing the speed of the reaction. | 12. Is the effects of a competitive inhibitor reversible? Why? | Yes, they can be reversed by adding more substrate. | 13. Define 'optimum temperature'. | the pH or temperature at which rate of enzyme-controlled reactions is the fastest. | 14. Explain what happens to an enzyme that is heated above its optimum temperature. | The enzyme gains even more kinetic energy that the vibrations break bonds and the enzyme's active site loses its shape. | 15. Draw the graph showing the effects of temperature on enzymatic activity. Explain the shape. | Line should go up quickly due to the enzymes and substrates having more energy as the temperature increases and so more change of successful collisions. Then peaks at its optimum, then falls as the enzyme has denatured. | 16. Draw the graph showing the effects of pH on enzymatic activity. Explain the shape. | Looks like a bell shape curve as the enzyme denatures in both too acidic or too alkaline conditions depending on the optimum pH of the enzyme. |
What are enzymes made up of?&choe=UTF-8
Question 1 (of 16)
What does the enzyme protease, amylase and lipase break down?&choe=UTF-8
Question 2 (of 16)
What is the area of the enzyme called that substrates bind to?&choe=UTF-8
Question 3 (of 16)
Explain the lock and key mechanism.&choe=UTF-8
Question 4 (of 16)
Define the term 'activation energy'.&choe=UTF-8
Question 5 (of 16)
How do enzymes affect the activation energy?&choe=UTF-8
Question 6 (of 16)
Define the term 'denatured'.&choe=UTF-8
Question 7 (of 16)
What is a buffer?&choe=UTF-8
Question 8 (of 16)
How is the induced fit hypothesis different to the lock and key hypothesis?&choe=UTF-8
Question 9 (of 16)
What is meant by a non-competitive inhibitor?&choe=UTF-8
Question 10 (of 16)
What is meant by a competitive inhibitor?&choe=UTF-8
Question 11 (of 16)
Is the effects of a competitive inhibitor reversible? Why?&choe=UTF-8
Question 12 (of 16)
Define 'optimum temperature'.&choe=UTF-8
Question 13 (of 16)
Explain what happens to an enzyme that is heated above its optimum temperature.&choe=UTF-8
Question 14 (of 16)
Draw the graph showing the effects of temperature on enzymatic activity. Explain the shape.&choe=UTF-8
Question 15 (of 16)
Draw the graph showing the effects of pH on enzymatic activity. Explain the shape.&choe=UTF-8
Question 16 (of 16)
