| Lesson Plan |
| Grade: |
Date: 25/02/2026 |
| Subject: Biology |
| Lesson Topic: investigate and explain the effects of the following factors on the rate of enzyme-catalysed reactions: temperature, pH (using buffer solutions), enzyme concentration, substrate concentration, inhibitor concentration |
Learning Objective/s:
- Describe how temperature, pH, enzyme concentration, substrate concentration, and inhibitor concentration each affect the rate of an enzyme‑catalysed reaction.
- Explain the kinetic basis for the observed effects, including concepts of optimum conditions, saturation, and inhibition types.
- Analyse experimental data to determine the optimum condition for a given enzyme and to distinguish between competitive and non‑competitive inhibition.
- Design a simple investigation that isolates one factor while controlling the others.
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Materials Needed:
- Spectrophotometer or colourimeter
- Cuvettes and pipettes
- Enzyme solution (e.g., catalase)
- Substrate solution (e.g., hydrogen peroxide)
- Buffer solutions covering a range of pH values
- Water bath or temperature‑controlled block
- Lab notebook and data table handout
- Projector for diagram presentation
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Introduction:
Begin with a quick demonstration of a colour change in a reaction tube as temperature is increased, prompting students to predict what will happen.
Recall prior learning about enzyme active sites and factors that influence reaction rates.
Explain that today’s success criteria are to predict, explain and evaluate how each factor alters enzyme activity.
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Lesson Structure:
- Do‑now (5’) – Students answer a short question on enzyme kinetics on the board.
- Mini‑lecture (10’) – Review of the five factors with illustrative graphs projected.
- Practical investigation (30’) – In groups, students vary one factor (e.g., temperature) while keeping others constant, record initial rates using the spectrophotometer.
- Data analysis (10’) – Groups plot their results, identify optimum points and discuss trends.
- Whole‑class debrief (10’) – Compare findings across groups, link observations to kinetic theory and discuss inhibition types.
- Check for understanding (5’) – Quick exit quiz via Kahoot or paper.
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Conclusion:
Summarise that each factor has a characteristic optimum or linear relationship with rate, and that inhibitors modify kinetic parameters differently.
Students complete an exit ticket stating one real‑world example of enzyme regulation.
For homework, assign a short report designing an experiment to test the effect of a new inhibitor on the same enzyme.
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