Enzymes: how they speed reactions, and what pH and temperature do
Grade 9 Science Worksheet

Circle the best answer.
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Model drawing, not to scale. Enzyme E has a notch, its active site, shaped to hold a round bead joined to a square bead. Molecule M1: a round bead joined to a square bead. Molecule M2: a round bead joined to a triangle bead. Molecule M3: a square bead joined to a square bead.
Enzyme E has an active site shaped for a round bead joined to a square bead. Which molecule can Ari’s enzyme E work on?
- Molecule M2, because it shares a round bead with the active site
- Molecule M1, because its beads match the active site
- Molecule M2, because a triangle bead is a better fit than a square
- Molecule M3, because enzymes work on any molecule they touch
Two digestive enzymes (real data, from OpenStax Biology)
enzyme works in substrate it breaks down pepsin stomach protein salivary amylase mouth starch Pepsin works on proteins in the stomach. Bo wonders what pepsin does if it meets a starch molecule. Use the table.
- Pepsin breaks the starch down, because enzymes work on any food molecule
- Nothing happens, because starch does not fit pepsin’s active site
- Pepsin breaks the starch down, because stomach acid supplies the energy
- Pepsin splits the starch, and then pepsin is used up
Model drawing, not to scale. Esme’s enzyme G holds three beads in a row: round, square, round. Which substrate fits it? Use the drawing.
Model drawing, not to scale. Enzyme G has an active site that holds three beads in a row: round, square, round. Molecule N1: a round bead joined to a square bead. Molecule N2: a round bead joined to a square bead joined to a round bead. Molecule N3: a square bead joined to a round bead joined to a square bead. Molecule N4: a round bead joined to a round bead joined to a square bead. Model drawing, not to scale. Enzyme G has an active site that holds three beads in a row: round, square, round. Molecule N1: a round bead joined to a square bead. Molecule N2: a round bead joined to a square bead joined to a round bead. Molecule N3: a square bead joined to a round bead joined to a square bead. Molecule N4: a round bead joined to a round bead joined to a square bead. active site Enzyme G Molecule N1 Molecule N2 Molecule N3 Molecule N4 - Molecule N4, because the enzyme reshapes to fit anything
- Molecule N3, because it has the same number of beads
- Molecule N2, because its three beads match in order
- Molecule N1, because two matching beads is close enough
Jun warms a mixture holding the model enzyme in the graph from 40 °C to 60 °C. Predict the activity and choose the reason.
Activity-versus-temperature graph for a model enzyme (model data). Temperature (°C) across, 0 to 70, a mark every 10. Enzyme activity (% of the highest rate) up, 0 to 100, a mark every 20. The line joins (0 °C, 5), (10 °C, 15), (20 °C, 35), (30 °C, 65), (40 °C, 100), (50 °C, 40), (60 °C, 5), (70 °C, 0) with straight pieces. Activity-versus-temperature graph for a model enzyme (model data). Temperature (°C) across, 0 to 70, a mark every 10. Enzyme activity (% of the highest rate) up, 0 to 100, a mark every 20. The line joins (0 °C, 5), (10 °C, 15), (20 °C, 35), (30 °C, 65), (40 °C, 100), (50 °C, 40), (60 °C, 5), (70 °C, 0) with straight pieces. Activity-versus-temperature graph for a model enzyme (model data) 0 10 20 30 40 50 60 70 0 20 40 60 80 100 Temperature (degC) Enzyme activity (% of the highest rate) - Activity stays at 100, because the enzyme is alive and adjusts
- Activity rises, because more heat makes reactions faster
- Activity falls, because the heat changes the enzyme’s shape
- Activity falls, because the heat uses the enzyme up
A mixture holds a fixed amount of enzyme. Luz raises the substrate from 5 to 7. Using the graph, predict the rate and the reason.
Rate-versus-substrate graph for a fixed amount of enzyme (model data). Substrate amount (units) across, 0 to 7, a mark every 1. Reaction rate (units per minute) up, 0 to 100, a mark every 20. The line joins (0 units, 0), (1 unit, 30), (2 units, 55), (3 units, 75), (4 units, 85), (5 units, 90), (6 units, 90), (7 units, 90) with straight pieces. Rate-versus-substrate graph for a fixed amount of enzyme (model data). Substrate amount (units) across, 0 to 7, a mark every 1. Reaction rate (units per minute) up, 0 to 100, a mark every 20. The line joins (0 units, 0), (1 unit, 30), (2 units, 55), (3 units, 75), (4 units, 85), (5 units, 90), (6 units, 90), (7 units, 90) with straight pieces. Rate-versus-substrate graph for a fixed amount of enzyme (model data) 0 1 2 3 4 5 6 7 0 20 40 60 80 100 Substrate amount (units) Reaction rate (units per minute) - It falls, because the extra substrate uses up the enzyme
- It rises, because each extra substrate adds to the rate
- It rises, because the extra substrate brings extra energy
- It stays near 90, because the active sites are full
Milo reads an energy diagram for one reaction with and without an enzyme. What is the activation energy with the enzyme?
Energy diagram (model data, not to scale). Reaction progress across. Energy (energy units) up, 0 to 120, a mark every 20. Every curve starts at 35 on the left and ends at 15 on the right. The no-enzyme curve climbs to a peak at 95. The enzyme curve climbs to a peak at 55. Energy diagram (model data, not to scale). Reaction progress across. Energy (energy units) up, 0 to 120, a mark every 20. Every curve starts at 35 on the left and ends at 15 on the right. The no-enzyme curve climbs to a peak at 95. The enzyme curve climbs to a peak at 55. Energy diagram (model data, not to scale) 0 20 40 60 80 100 120 Reaction progress Energy (energy units) no-enzyme curve enzyme curve - 55 energy units
- 20 energy units
- 60 energy units
- 95 energy units
Using Noah’s energy diagram, by how much does the enzyme lower the activation energy?
Energy diagram (model data, not to scale). Reaction progress across. Energy (energy units) up, 0 to 120, a mark every 20. Every curve starts at 30 on the left and ends at 10 on the right. Without the enzyme climbs to a peak at 80. With the enzyme climbs to a peak at 45. Energy diagram (model data, not to scale). Reaction progress across. Energy (energy units) up, 0 to 120, a mark every 20. Every curve starts at 30 on the left and ends at 10 on the right. Without the enzyme climbs to a peak at 80. With the enzyme climbs to a peak at 45. Energy diagram (model data, not to scale) 0 20 40 60 80 100 120 Reaction progress across Energy (energy units) Without the enzyme With the enzyme - 35 energy units
- 15 energy units
- 45 energy units
- 50 energy units
Which statement describes what the enzyme does to Pia’s energy diagram?
Energy diagram (model data, not to scale). Reaction progress across. Energy (energy units) up, 0 to 120, a mark every 20. Every curve starts at 50 on the left and ends at 20 on the right. Without the enzyme climbs to a peak at 110. With the enzyme climbs to a peak at 75. Energy diagram (model data, not to scale). Reaction progress across. Energy (energy units) up, 0 to 120, a mark every 20. Every curve starts at 50 on the left and ends at 20 on the right. Without the enzyme climbs to a peak at 110. With the enzyme climbs to a peak at 75. Energy diagram (model data, not to scale) 0 20 40 60 80 100 120 Reaction progress Energy (energy units) Without the enzyme With the enzyme - It raises the start from 50 to 75, so the reaction begins sooner
- It lowers the peak from 110 to 75, and then the enzyme is used up
- It lowers the peak from 110 to 75; the start and end stay at 50 and 20
- It raises the end from 20 to 50, adding energy to the products
Ren tests two model enzymes, X and Y, across temperatures. Which is more active at 60 °C, and why?
Activity-versus-temperature graph for two model enzymes (model data). Temperature (°C) across, 0 to 70, a mark every 10. Enzyme activity (% of the highest rate) up, 0 to 100, a mark every 20. Enzyme X joins (0 °C, 5), (10 °C, 15), (20 °C, 35), (30 °C, 65), (40 °C, 100), (50 °C, 40), (60 °C, 5), (70 °C, 0) with straight pieces. Enzyme Y joins (0 °C, 0), (10 °C, 5), (20 °C, 10), (30 °C, 25), (40 °C, 50), (50 °C, 80), (60 °C, 100), (70 °C, 30) with straight pieces. Activity-versus-temperature graph for two model enzymes (model data). Temperature (°C) across, 0 to 70, a mark every 10. Enzyme activity (% of the highest rate) up, 0 to 100, a mark every 20. Enzyme X joins (0 °C, 5), (10 °C, 15), (20 °C, 35), (30 °C, 65), (40 °C, 100), (50 °C, 40), (60 °C, 5), (70 °C, 0) with straight pieces. Enzyme Y joins (0 °C, 0), (10 °C, 5), (20 °C, 10), (30 °C, 25), (40 °C, 50), (50 °C, 80), (60 °C, 100), (70 °C, 30) with straight pieces. Activity-versus-temperature graph for two model enzymes (model data) 0 10 20 30 40 50 60 70 0 20 40 60 80 100 Temperature (degC) Enzyme activity (% of the highest rate) Enzyme X Enzyme Y - Enzyme Y, because 60 °C is close to its best temperature
- Enzyme X, because it is the stronger of the two enzymes
- Enzyme X, because more heat speeds up an enzyme
- Enzyme Y, because it is alive and gets used to the heat
Where two enzymes work (real data, from OpenStax Biology and OpenStax Anatomy and Physiology)
enzyme works in pH there pepsin stomach 1.5 to 2.5 salivary amylase mouth 6.35 to 6.85 Zee reads that salivary amylase has a working range of pH 6.35 to 6.85. Use the table. What happens to it in the stomach?
- It keeps working the same, because acid does not affect enzymes
- It stops working, because the stomach’s acid is far from the pH it needs
- It speeds up, because the acid adds energy
- It starts working on protein, because enzymes fit any substrate