On a single graph, sketch a qualitative velocity profile (velocity vs. time) for the enzymatic breakdown of the substrate by the enzyme for each condition: A-C.

100 90 80 70 M pts) Some enzymes can catalyze substrate reactions which result in the production of H+ ions. If the batch Activity of WarEaglease reactor is not sufficiently buffered, this can lead to a change in pH. Because pH is an important factor in optimizing enzyme activity, the reaction velocity v can be altered during the reaction by the appearance of H as a product. On a single graph, sketch a qualitative velocity profile (velocity vs. time) for the enzymatic breakdown of the substrate Auburn by the enzyme, WarEaglease for two conditions: 3 4 5 6 7 8 9 10 11 A. An unbuffered solution that starts at pH 8. B. A well-buffered pH 8 solution. C. A well-buffered pH 7 solution. The substrate, Auburn, is a weak base, and the reaction is carried out in a batch reactor. Assume a high substrate concentration, so depletion of [S] does not cause the reaction to slow during the experiment. The relative activity of WarEaglease as a function of pH is given in the graph above. Relative Activity (%) o 8888888 2 8 12 13 14 PH a