Sucrose phosphorylase is an enzyme found in some species of bacteria. One function of this enzyme is for the production of compounds that help to protect the cell from harmful osmotic changes in the external environment. Fig. 5.1 shows the reversible reaction that takes place within the bacterial cell. [Figure 5.1]
- (a)Name reducing sugar X in Fig. 5.1.[1]
- (b)In the absence of sucrose phosphorylase as a catalyst, the reaction shown in Fig. 5.1 would take too long to occur to allow the bacterial cell to function efficiently. Explain why the reaction shown in Fig. 5.1 proceeds at a much faster rate in the presence of the enzyme.[2]
- (c)An enzyme that catalyses a reaction of commercial interest needs to be investigated to see if it is suitable for use in industry. For example: • immobilised enzymes may be used as they have a longer shelf-life than the enzyme free in solution • many industrial reactions are carried out at higher temperatures to minimise contamination of products by microorganisms. Fig. 5.2 shows the results of an investigation to compare the activity of sucrose phosphorylase free in solution (free enzyme) with immobilised sucrose phosphorylase (immobilised enzyme) at different pHs. Fig. 5.3 shows the activity of the free enzyme and immobilised enzyme at different temperatures. [Figure 5.2] [Figure 5.3] With reference to the results shown in Fig. 5.2 and Fig. 5.3, discuss which sucrose phosphorylase enzyme, free or immobilised, is better for use in industrial reactions.[4]
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Mark scheme
Marking points from the official mark scheme (Oct/Nov 2020). The mark or mark type is shown in brackets.
- [1] fructose ; Ια or β
- [2] any two from:
- formation of enzyme-substrate complex / substrate fits into active site ;
- A substrate binds to active site
- (so) reactants held close together (e.g. for bond formation) ;
- lowers, activation energy / energy of activation ; A Ea / Ae
- can award annotated on a sketch
- detail; e.g. transfer of electrons
- strain on bonds
- alternative pathway
- holds substrate in a way that the bonds needed to be broken are exposed
- [4] I ref. to denaturation, either mp2 or mp10 can be awarded
- any four from:
- immobilised
- 1 higher optimum temperature ; AW e.g. peak/ max activity/ 100% activity;
- 2 74/75/76°C, v, 56 / 57 / 58 / 59°C ;
- A one correct value and calculation e.g. 17°C lower
- 3 idea that greater range of pH with, higher activity / greater stability; AW
- allow use of comparative data at one pH value to support if answer unclear
- 4 idea that if pH changes, less effect on enzyme activity;
- A resists changes in pH
- 5 ref. to more active at, higher temperatures / temperatures above 68°C;
- A more thermostable / less effect on enzyme at higher temperatures
- A free enzyme not active above 70°C
- allow use of comparative data at one temperature to support if answer unclear
- 6 one advantage of immobilised; e.g. reusable
- Ο less/no, contamination of product (by enzyme)
- Ο easier, downstream processing / separation of enzyme from product
- Ο longer shelf-life useful if enzyme, difficult to obtain A ref. to cost effective
- Ο can use in continuous processes so more productive
- Ο suggestion that (can carry out process at) lower pH (more acid conditions and) may be more effective against microorganisms
- free enzyme
- 7 higher activity, at lower temperatures / between 35°C to 68°C;
- in context of a range, quoting one temperature not enough
- 8 two temperatures, comparative values for both enzymes to support mp7 ;
- 9 optimum temperature lower so cheaper maintaining that temperature ;
- AW
- A lower temperatures cost efficient to maintain and enzyme works well/AW
- 10 (values of optimum) 74 / 75 / 76°C, v, 56 / 57 / 58 / 59°C ;
- A calculation, e.g. 17°C lower
- 11 lower optimum temperature still high enough to kill microorganisms;
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