Researchers followed how two enzyme-catalysed reactions developed, using dopa oxidase and neutrase. Because each reaction altered the look of its reaction mixture, the progress could be tracked by the change in appearance. The reactions are illustrated in Fig. 3.1. For dopa oxidase: L-dopa (colourless solution) → dopachrome (orange-brown solution). For neutrase: casein + water (white solution) → peptides (short chains of amino acids) (colourless solution). Since the appearance of the mixtures changes, a colorimeter can be used to monitor the reactions. Fig. 3.2 presents the progress of the reaction catalysed by dopa oxidase as recorded from a colorimeter. Fig. 3.3 presents the progress of the reaction catalysed by neutrase as recorded from a colorimeter.
(a)
Researchers followed how two enzyme-catalysed reactions developed, using dopa oxidase and neutrase.
(a(i))[3]
Using Fig. 3.1, Fig. 3.2 and Fig. 3.3 as evidence, describe and explain how the two reactions are similar in their progress.
(a(ii))[2]
Suggest two benefits of using a colorimeter to investigate the progress of reactions such as those shown in Fig. 3.1.
(b(i))[2]
Calculate the Michaelis-Menten constant, $K_m$, for enzyme VpSP37 by using the data in Fig. 3.4. Show your working.
(b(ii))[2]
The scientists identified other enzymes that could also be used for the industrial process. These enzymes had greater $K_m$ values than VpSP37. Explain the advantage of using VpSP37 in the industrial process instead of one of these other enzymes with greater $K_m$ values.