BiologyCode 9700
Factors that affect enzyme action
What this topic asks you to be able to do
- investigate and explain how the rate of enzyme-catalysed reactions is affected by temperature, pH (using buffer solutions), and the concentrations of enzyme, substrate and inhibitor
- explain that the Michaelis–Menten constant (Km) is worked out from the maximum rate of reaction (Vmax), and that Km is then used to compare how great an affinity different enzymes have for their substrates
- account for the influence that reversible inhibitors exert on enzyme activity, covering both competitive and non-competitive types
- investigate how an enzyme's activity differs when it is immobilised in alginate compared with when it is free in solution, and state the benefits of using immobilised enzymes