SACE Stage 2 Biology Investigation

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Discussion Hypothesis 1 Overall, as the concentration of the substrate increases, the enzyme activity increases up to a 70% of solution, where the enzyme activity starts to level off. The curve is polynomial because of the fact that the enzyme activity exponentially increases as the concentration of substrate increase; additional evidence for this is the fact that the gradient graph is constantly changing. The polynomial curve is shown because until 70% (the saturation point); this is because there are more casein substrate molecules that can successfully collide with the renin enzyme molecule, therefore increasing the rate of reaction. However, once it reaches 70% of concentration, the enzyme becomes saturated, meaning that there are no active sites for the substrates to fill, which leaves casein (milk) molecules suspended in the curd; the saturation point for this curve was located at 6.5x 10-3 seconds. This was clearly evident in some of the visual results of the practical, where we could see that there was still milk that could be decanted when the curd was poured out. Therefore, even if we added more casein substrate, the curve enzyme activity would still flatten, indicating again that all or most of the active sites of the renin enzyme were full. Moreover, the class average curve shows a similar trend, as the curve flattens, at 70% but with an enzyme activity of 5.3 x10-3 seconds. This indicates that even though the saturation point is the same it was considerably lower than our results, which could indicate sources of systematic error in the design of the practical. The control for both curves was the beaker with 0% concentration of substrate, which produced no enzyme activity, as there were no substrate molecules for... ... middle of paper ... ...rting the stopwatch itself. Alternatively, we could also exclude milliseconds when calculating out results. This would therefore eradicate any reaction times and as a result, make the data more reliable and accurate. To conclude, an important random error was the idea that the renin enzyme solution was inconsistently stirred with the casein: as if we were almost encouraging the curd to form. This meant that because each of the renin and casein molecules had more kinetic energy, it was more likely that they would collide. Consequently, the rate of reaction would minutely increase. Even though we tried to consistently stir the mixture, it was hard to keep this continuous for the duration for both practicals. Therefore, to keep the stirring more constant, we could use a magnetic stirrer, in order to make the kinetic energy used to stir the mixtures a control factor.

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