The enzyme amylase catalyses the hydrolysis (breakdown) of starch to reducing sugars, as shown in Fig. 1.1. A student investigated the effect of temperature on the hydrolysis of starch by the enzyme amylase. The student: - put $$\(2 \mathrm{~cm}^{3}\)$$ of amylase into a test-tube - put $$\(18 \mathrm{~cm}^{3}\)$$ of starch solution into a different test-tube - put the test-tubes into a water-bath at $$\(0^{\circ} \mathrm{C}\)$$ - left the test-tubes for 3 minutes - put the starch solution into the test-tube containing the amylase - left the test-tube for 2 minutes - immediately determined the relative amount of reducing sugars in the test-tube - repeated this procedure at $$\(40^{\circ} \mathrm{C}\)$$ and at $$\(100^{\circ} \mathrm{C}\)$$. You are provided with three beakers, S1, S2 and S3. These three beakers contain the same products of the reaction between starch and amylase as the test-tubes prepared by the student. You will determine: - the relative amount of reducing sugar present in each beaker - the presence or absence of starch in each beaker. You are provided with the materials shown in Table 1.1. Table 1.1 If any solution comes into contact with your skin, wash off immediately with cold water. It is recommended that you wear suitable eye protection. To investigate the effect of temperature on the hydrolysis of starch by the enzyme amylase you will need to: - carry out the test for reducing sugars on S1, S2 and S3 - determine the relative amount of reducing sugar in each solution - carry out the test for starch on S1, S2, and S3 - determine the presence or absence of starch in each solution. A student investigated the effect of temperature on the action of an enzyme that digests protein. The results are shown in Table 1.3. Table 1.3 Plot a graph of the data in Table 1.3 on the grid in Fig. 1.2. Use a sharp pencil. Fig. 1.2

Biology
IGCSE&ALevel
CAIE
Exam No:9700_w24_qp_35 Year:2024 Question No:1(b)

Answer:



Knowledge points:

3.2.1.1 temperature
3.2.1.2 pH (using buffer solutions)
3.2.1.3 enzyme concentration
3.2.1.4 substrate concentration
3.2.1.5 inhibitor concentration
3.2.2 explain that the maximum rate of reaction (Vmax) is used to derive the Michaelis-Menten constant (Km) which is used to compare the affinity of different enzymes for their substrates
3.2.3 explain the effects of inhibitors, both competitive and non- competitive, on the rate of enzyme activity
3.2.4 investigate the difference in activity between an enzyme immobilised in alginate and the same enzyme free in solution, and state the advantages of using immobilised enzymes

Solution:

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