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Exam Style Question 2

A student investigated the effect of temperature on the activity of the enzyme amylase.She put 5 cm3 of starch solution, 1 cm3 of buffer solution and 1 cm3 of amylase solution in separate tubes in a water bath at the test temperature for 5 minutes. She then mixed them.Every 30 seconds she added one drop of the mixture to iodine solution on a spotting tile. She recorded the time taken until the iodine solution no longer turned blue-black.Her results are shown in the table.
Temperature / °C2030405060
Time taken for starch to be digested / s36018090150not digested after 600
(a) Explain why the time taken decreased between 20 °C and 40 °C. (2 marks)(b) Explain the result at 60 °C. (3 marks)Mark scheme
(a) 1. More kinetic energy (of enzyme and substrate molecules).
2. More (successful) collisions between amylase and starch, so more enzyme-substrate complexes form per second.(b) 1. Hydrogen bonds (and ionic bonds) in the tertiary structure of amylase break, so the enzyme is denatured.
2. The shape of the active site changes.
3. Starch is no longer complementary to the active site, so no enzyme-substrate complexes form.

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Specification: AQA Biology (7401), AS-level, 3.1.4.2 Many proteins are enzymes. Topic: Enzymes.

Key terms in this lesson

hydrogen bond
A weak electrostatic attraction between a slightly positive hydrogen atom on one polar molecule and a slightly negative atom, such as oxygen or nitrogen, on another.
ionic bond
A strong bond formed by the electrostatic attraction between oppositely charged ions.
tertiary structure
The further coiling and folding of a polypeptide into a specific three-dimensional shape, held by ionic bonds, hydrogen bonds and disulfide bridges between R-groups.
active site
The region of an enzyme, formed by the tertiary structure, with a shape complementary to its substrate, where the substrate binds.
denaturation
A permanent change to the tertiary or quaternary structure of a protein, caused by heat or pH extremes, that alters the shape of the active site so it is no longer complementary to its substrate.

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