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Cell Level Systems

Enzyme action, and investigating enzymes

  • 3 things to know
  • Paper 3

Overview

Measuring the rate of an enzyme reaction with amylase and catalase, controlling pH and temperature, the active site and lock and key model, and how temperature, pH and concentration change the rate.

What you need to know

Answer each one before you reveal it.

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Key term

Explain how enzyme activity changes as pH leaves the optimum, why extra substrate eventually stops raising the rate, and why extra enzyme raises it.

Key term

In an investigation of amylase, how can you tell when all the starch has been broken down?

Key term

Which variables must be kept the same when investigating the effect of pH on amylase activity?

Questions from this subtopic

Each one with the model answer underneath.

  1. 1

    How can the rate of a reaction controlled by an enzyme be measured?

    Model answer

    By timing how quickly the substrate disappears or how quickly a product appears.

  2. 2

    In an investigation of amylase, how can you tell when all the starch has been broken down?

    Model answer

    A sample no longer turns iodine solution blue-black but stays orange-brown.

  3. 3

    Which variables must be kept the same when investigating the effect of pH on amylase activity?

    Model answer

    The temperature, the concentration of enzyme and starch, and the volumes used.

  4. 4

    How is a steady temperature maintained during an enzyme investigation?

    Model answer

    The tubes are stood in a water bath set to the chosen temperature.

  5. 5

    Why is a buffer solution added in an enzyme investigation?

    Model answer

    It holds the pH steady at the chosen value while the reaction runs.

  6. 6

    How can the activity of catalase be measured using hydrogen peroxide?

    Model answer

    By collecting the oxygen given off and measuring the volume of gas produced in a fixed time.

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