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NotesBiologyTopic 3.1Temperature, pH and substrate concentration
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3.1.43 min read

Temperature, pH and substrate concentration

IB Biology • Unit 3

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Contents

  • What changes the rate of an enzyme
  • Working out each graph
  • Exam-style question
The big idea: An enzyme is a biological catalyst — it speeds up a reaction without being used up.

How fast an enzyme works (its rate) depends on three things you must be able to explain and read from a graph:

1. Temperature, 2. pH, and 3. substrate concentration.

Each one has its own shaped graph, and each shape has a story about what is happening to the enzyme.

The three classic enzyme-rate graphs: rate rises to an optimum temperature then falls as the enzyme denatures; rate peaks at an optimum pH; and rate rises with substrate concentration then plateaus once every active site is saturated.

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Enzyme
A protein that acts as a biological catalyst, speeding up a specific reaction without being used up.
Active site
The part of the enzyme with a specific shape that the substrate fits into. Its shape is what gives the enzyme its job.
Substrate
The molecule an enzyme acts on. It binds to the active site, where it is changed into product.
Optimum
The temperature or pH at which an enzyme works fastest — the peak of the graph.
Denaturation
A permanent change to the SHAPE of an enzyme's active site (caused by high temperature or extreme pH) so the substrate no longer fits and the enzyme stops working.
Saturation
The point where every active site is occupied by substrate, so adding more substrate cannot increase the rate.
Why shape is everything: An enzyme only works because its active site has a shape that the substrate fits into.

Anything that changes that shape — like too much heat or the wrong pH — stops the enzyme working. This single idea explains almost every enzyme graph.

Each factor changes the rate for a different reason. Work through them one at a time, always asking: what is happening to the active site or to the collisions?

Temperature — up to a point: As temperature rises, molecules move faster, so the substrate collides with the active site more often — the rate increases.

This continues only up to the optimum temperature, where the rate is highest (about 37 degrees C for many human enzymes).

Above the optimum the rate falls sharply: the heat denatures the enzyme — the active site changes shape, so the substrate no longer fits and the reaction stops.

Read the temperature graph (left): the rate climbs to a peak at the optimum, then drops sharply because high heat denatures the enzyme — the active site changes shape and the substrate no longer fits.

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pH — a peak either side of which it falls: Every enzyme has an optimum pH where its active site is the right shape and the rate is highest.

Move the pH too far either way (too acidic or too alkaline) and the active site is distorted — the enzyme is denatured and the rate drops.

Different enzymes have different optimum pHs: for example, a stomach enzyme works best in very acidic conditions, while many others prefer a near-neutral pH.
Substrate concentration — until the sites are full: Adding more substrate gives more molecules to collide with active sites, so at first the rate increases.

Eventually the rate levels off — a plateau. At this point every active site is occupied (the enzymes are saturated), so the substrate has to wait for a site to become free.

Adding even more substrate cannot speed things up — the number of enzymes is now the limiting factor, not the substrate.

Read the substrate-concentration graph (right): the rate rises then levels off (plateau). At the plateau every active site is occupied — the enzymes are saturated, so adding more substrate cannot speed the reaction up.

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Denaturation (temperature & pH graphs)

  • Caused by high temperature or extreme pH
  • The active-site shape is changed
  • Substrate no longer fits → rate falls
  • Usually permanent (cannot recover)

Saturation (substrate graph)

  • Caused by high substrate concentration
  • All active sites are occupied
  • Rate plateaus (stays constant)
  • Enzyme is unharmed — just fully busy
A memory hook: Denatured = shape destroyed (heat or pH wrecks the active site → rate falls).

Saturated = sites all seated (every active site is taken → rate plateaus, but the enzyme is fine).
FactorBelow the optimumAt the optimumPast / above the optimum
TemperatureRate is slow — molecules move slowly, so fewer collisions with the active siteRate is highest — fastest successful collisionsRate falls sharply — heat DENATURES the enzyme (active site changes shape)
pHRate is low — the wrong pH distorts the active siteRate is highest at the enzyme's optimum pHRate falls — too acidic or too alkaline DENATURES the enzyme
Substrate concentrationRate rises as more substrate is added (more collisions)—Rate PLATEAUS — all active sites are full (enzyme is saturated); rate is now limited by enzyme number

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How this is tested: This is the most-examined part of enzymes, and it is a data-question favourite. On Paper 2 you may be given a rate-versus-temperature graph and asked to label the point of highest rate (the optimum), then outline why the rate falls above it — the answer is denaturation.

On Paper 1B / Paper 2 you may be handed a graph (for example, enzyme activity at different storage temperatures) and asked to explain the relationship shown — read the trend off the graph, then give the biological reason.

On Paper 1 a 1-mark question often asks you to explain the plateau on a rate-versus-substrate-concentration graph — the answer is saturation of the active sites.

IB-style question — explain a temperature graph

A graph shows the rate of an enzyme-controlled reaction against temperature. The rate rises to a peak at 40 degrees C and then falls steeply. Explain the shape of this graph. [4]

How to score all four marks

  1. Below the optimum — why the rate rises. As temperature increases, molecules gain kinetic energy and move faster, so substrate and enzyme collide more often, increasing the rate.
  2. At the optimum — name the peak. The rate is highest at the optimum temperature (40 degrees C), where collisions are most frequent and the active site is the correct shape.
  3. Above the optimum — name the cause. Above the optimum the high temperature denatures the enzyme.
  4. Above the optimum — explain the mechanism. Denaturation changes the shape of the active site, so the substrate no longer fits, and the rate falls steeply. (Award 1 mark each: rise = more collisions; peak = optimum; fall = denaturation; mechanism = active-site shape change so substrate cannot bind.)

Final answer

Rising part: higher temperature → faster molecules → more frequent collisions → faster rate. Peak: the optimum temperature. Falling part: heat denatures the enzyme, changing the active-site shape so the substrate no longer fits, and the rate drops.

✓ Why this scores full marks: It explains all three regions of the curve — the rise, the peak and the fall — and for the fall it gives both the keyword (denaturation) and the mechanism (active-site shape changes so the substrate cannot fit).

Saying only 'the enzyme denatures' without explaining the active site usually loses the final mark.

Read the temperature graph (left): the rate climbs to a peak at the optimum, then drops sharply because high heat denatures the enzyme — the active site changes shape and the substrate no longer fits.

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Try an IB Exam Question — Free AI Feedback

Test yourself on Temperature, pH and substrate concentration. Write your answer and get instant AI feedback — just like a real IB examiner.

On a graph of reaction rate against substrate concentration, the rate eventually stays constant at a plateau.

the term that describes the condition of the enzymes at this plateau.
[1 mark]

Related Biology Topics

Continue learning with these related topics from the same unit:

3.1.1Metabolism: anabolism and catabolism
3.1.2Active sites, specificity and induced fit
3.1.3Activation energy and energy profiles
3.1.5Enzyme experiments and immobilized enzymes
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