Yeast cells contain an enzyme, catalase, which catalyses the release of oxygen from the substrate hydrogen peroxide. You will investigate the effect of temperature on the activity of catalase in yeast suspension Y. You are provided with the materials shown in Table 1.1. Table 1.1 labelled contents hazard volume/cm³ Y 3.0% yeast suspension none 100 H 3.0% hydrogen peroxide solution irritant 20 If any of Y or H comes into contact with your skin, wash off immediately under cold water. It is recommended that you wear suitable eye protection.
- (a)(i)Think about the hazards of using the materials in Table 1.1. State whether the risk of using hydrogen peroxide solution, H, is low, medium or high. Give a reason for your answer. risk reason[1]
- (a)(ii)You will test the activity of catalase in yeast suspension Y at room temperature and at other temperatures up to a maximum of 70 °C. Use the thermometer to measure the temperature of the room. State the room temperature and the other temperatures you will use in your investigation. room temperature other temperatures[1]
- (iii)Decide how you could determine the rate at which drops are released from the syringe. The method that you decide should take no longer than two minutes. State the measurements that you will need to make.[2]
- (iv)Record your results in an appropriate table.[5]
- (v)State the concentrations of hydrogen peroxide solution that the student could prepare to provide a suitable range for this investigation. Outline how these concentrations could be prepared from 5.0% hydrogen peroxide solution. concentrations how prepared[2]
- (vi)The student standardised the volume and concentration of the catalase solution. State one other variable that would need to be standardised. Describe how this variable could be standardised. variable how standardised[1]
- (b)(i)Plot a graph of the data in Table 1.2 on the grid in Fig. 1.3. Use a sharp pencil for drawing graphs.[4]
- (ii)Use your graph to estimate the enzyme activity when the pH is 4.0. Show on your graph how you estimated this value. enzyme activity =[2]
- (iii)Describe the trend in the results shown by your graph plotted on Fig. 1.3.[1]
- (iv)Explain the effect of pH on this enzyme.[3]
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Mark scheme
Marking points from the official mark scheme (Feb/Mar 2020). The mark or mark type is shown in brackets.
- [1] assesses the risk of using H as medium or high and reason e.g. H is an irritant;
- [1] states room temperature and at least three more temperatures between room temperature and 70 °C ;
- [1] states number of drops ; [2] reference to time;
- [1] heading for independent variable: temperature / °C and before heading for dependent variable and no units in the body of table ; [2] heading for dependent variable: number of drops and reference to time; [3] readings for all temperatures ; [4] correct trend: highest number of drops for the highest temperature; [5] results recorded as whole drops ;
- [1] at least four stated concentrations other than 5%; [2] proportional or serial dilution correctly described ;
- [1] any one from : pH and use of buffer; volume of hydrogen peroxide and use of appropriate apparatus for measuring volume ; temperature and use of thermostatically controlled water-bath;
- [1] x-axis: pH and y-axis: enzyme activity / arbitrary units ; [2] scale on x-axis: 1 to 2 cm or 2 to 2 cm, labelled at least every 2 cm and scale on y-axis: 5 arbitrary units to 2 cm, labelled at least every 2 cm ; [3] correct plotting of all points using small crosses or dots in circles ; [4] points joined with thin line passing through all points as either a smooth curve or straight lines joining each point to the next;
- [1] shows on the graph how value estimated; [2] correct pH stated from candidate's graph;
- [1] as pH increases the rate of enzyme activity increases and then decreases ;
- [1] (from pH 3.2 to pH 5.7) more enzyme-substrate complexes or (from pH 5.7 to pH 7.5) fewer enzyme-substrate complexes ; [2] (from pH 3.2 to pH 5.7) more successful collisions or more substrate can bind to active site or (from pH 5.7 to pH 7.5) fewer successful collisions or less substrate can bind to active site ; [3] reference to, ionic / hydrogen bonds and active site changes shape; [4] enzyme becomes denatured ;
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