Biology 1 Enzymes and Catalase Lab Report

Biology 1 Enzymes and Catalase Lab Report - Taylor West ...

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Unformatted text preview: Taylor West Biology 1440 CRN 12424 11- 02- 12 Enzymes and Catalase Introduction: A protein’s reaction occurs when a substrate binds to an active site causing a reaction. Enzymes are biological catalysts that increase the rate of the reaction without being changed or destroyed by the chemical reaction. When enzymes are added they can speed up the rate at which the substrate binds to an active site anywhere from 10 to 20 million times at which the substrate binds to an active site be if left uncatalyzed. When we added 3% H2O2 it acted as a catalyst speeding up the chemical reaction similar to yeast forming. This caused an increase in pressure in the test tube, which we measured. We formed our first research question: what is the effect of changing substrate concentration on the rate of catalase activity? For this study we changed the substrate concentration, H2O2, which we added to our catalse, yeast. We tested the hypothesis that the higher the concentration of H2O2 the faster the rate of catalase activity would occur. We also formed a second research question: what is the effect of changing catalase concentration on the breakdown of H2O2? For this experiment we changed the concentration of our catalase, yeast, that we added to our substrate concentration, H2O2. Results: For the first experiment the data we collected showed an increase in the rate of catalase activity (mmHg/s) as the concentration of H2O2 increased. Between 1% and 1.5% concentration there is a huge increase in the rate of activity by 85.6%. Between the 1.5% concentration and the 2% there was a slight increase of 15.5% in Taylor West Biology 1440 CRN 12424 11- 02- 12 the rate of activity. Between 2% concentration and 2.5% concentration there is an increase of 36%. The final increase of rate between 2.5% concentration and 3% concentration is a slight increase of 16.8%. There was a constant increase in rate of activity but after the 1%- 1.5% increase the rate of increase decreased dramatically. Figure 1. This figure relates the concentration of H2O2 in % to the rate in catalase activity in mmHg/s. There is a huge increase from 1% to 1.5% concentration and after that concentration the rate of increase starts to slow down. There was an extreme increase in the rate of activity of 85.6%, everything after 1.5% concentration increased slightly but not significantly. The second experiment had a huge initial increase from the control group to 20% concentration. After 40% concentration the graph has an almost steady increase. There is a 56% increase from the 40% concentration to 60% concentration. From 60% increase to 80% there is a 58.4% increase in rate of Taylor West Biology 1440 CRN 12424 11- 02- 12 activity. From 80% concentration to the 100% concentration the rate of increase is only 29.5%. Figure 2. This figure relates the rate of catalase activity (mmHg/s) to the concentration of yeast (%). The data has a steady increase throughout the whole experiment but after the initial increase the data’s rate slows down. After the 40% concentration the rate has a slightly different percentages of increase but still increases steadily. The points represent averages of three trials and the bars represent the minimum and maximum range. Conclusion: Our data supported both of our hypotheses, as the concentration of the yeast or H2O2 increased so did the rate of catalase activity. We initially asked what would be the effect of changing substrate concentration on the rate of catalase activity. The rate of catalase activity increased dramatically up to the 1.5% concentration, after that the rate was still increasing but Taylor West Biology 1440 CRN 12424 11- 02- 12 started to slow down. This means that the enzyme has used up the initial activation energy. The H2O2 keeps reacting with the yeast but not as fast as with the catalyst helping. Next we asked what the effect of changing catalase concentration would be for the breakdown of H2O2. We thought that by increasing the concentration of catalase would also increase the breakdown of H2O2. The data increased initially but after 20% concentration of yeast the reaction kept increasing but not as dramatically. The fact that it behaved like that is interesting because the results suggest that changing the catalase activity doesn’t have as much effect on the rate of catalase activity as changing the substrate concentration does. There were a few errors in this experiment. One major error was our vortexer kept speeding up and a few times we couldn’t get it to slow back down fast enough. This could be responsible for the large range bars in our graphs. Another main error was that our pressure probe kept popping off of the top of the test tube right after we finished collecting data. Based on these results in the future it would be interesting to find the best concentration of yeast and H2O2 that would cause the highest initial activation energy and highest increase in rate of catalase. ...
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