Conclusion:
The investigation supported the hypothesis that if the concentration of Catalase were to increase from 25%, 50%, 75%, and 100%, there would be an initial increase in the change in temperature (degrees) until the Catalase concentration no longer becomes the limiting factor and the graph starts to plateau.
As illustrated in graph 1, the change in temperature (degrees) appears to increase at a constant rate until it reaches the 50% Catalase concentration. The graph then starts to plateau up until the 100% Catalase concentration. At the lowest concentration of Catalase (i.e. 25%), the Catalase is the limiting factor as there is a higher ratio of hydrogen peroxide (H2O2) molecules compared to the catalase. As the concentration of Catalase
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It can be inferred that in order for chemical reactions to occur at their optimum, only a certain amount of enzymes are required. Therefore, increasing the concentration of enzymes will not necessarily increase the rate of reaction. Thus, this experiment illustrates how important it is for plant and animal cells to produce the correct amount of enzymes to accommodate for the substrates, as enzymes are recyclable and only need to occur in small …show more content…
If the thermometer was calibrated incorrectly, it would have given values that were different from the true value, which could account for the scattered data sets for the 25% and 100% concentrated Catalase. In addition, the timer may have been calibrated incorrectly resulting the temperature to be taken slightly before or after 30 seconds. Nevertheless, the margin of error would be constant, as the same thermometer and timer were used throughout the practical. Moreover, to ensure that the equipment used is calibrated correctly, the experiment should be repeated again using different equipment. This would improve the precision of the results, as there would be more data points to plot and will also give an indication if any of the equipment used were calibrated incorrectly, hence minimising systematic errors.
Sample Size:
This investigation consisted of two trials, each with 4 different data points (25%, 50%, 75%, and 100%), giving a total sample size of 8. As illustrated in graph 1, this was adequate enough to support the hypothesis and theory of the investigation.
Furthermore, the sample size enabled an average to be calculated, which ultimately minimises the effects of any outliers. This is evident in the graph were the impact of the outlier in the 25% concentrated Catalase for trial 1 has been reduced and is further supported by a very high r2 value which gives a
3) Adding less enzyme caused the reaction to proceed more slowly than when more enzyme was utilized.
Andra Larade Bio 30 B7 11/20/15 Liver Enzyme Lab The Effect of pH and Temperature on the Efficiency of Catalase Abstract: In order to determine how pH and temperature affect the liver enzyme catalase, an experiment was conducted. Catalase breaks apart hydrogen peroxide producing water and oxygen.
These results shown from this experiment led us to conclude that enzymes work best at certain pH rates. For this particular enzyme, pH 7 worked best. When compared to high levels of pH, the lower levels worked better. The wrong level of pH can denature enzymes; therefore finding the right level is essential. The independent variable was the amount of pH, and the dependent being the rate of oxygen. The results are reliable as they are reinforced by the fact that enzymes typically work best at neutral pH
Five different temperatures of enzyme (spinach extract) (5°C, 20°C, 35°C, 45°C and 65°C) were added to individual measuring cylinders -each filled with 7ml of Hydrogen Peroxide (H202). The height of foam (oxygen + water) produced by the reaction was recorded for each temperature of the catalase after 30 seconds, to find at which degrees the enzyme activity had the fastest reaction rate. The data collected from this experiment suggested that the enzyme extract had the greatest efficiency at 20 °C, and the temperatures greater displayed a decline in rate of reaction.
Catalase is an enzyme needed to break down hazardous hydrogen peroxide into nonhazardous oxygen and water. This is needed for organisms as the reaction rate of the decomposition of hydrogen peroxide is too slow to protect cells against the oxidation of hydrogen peroxide. The purpose of this experiment is to test the concentration of hydrogen peroxide on catalase and variation in temperature of catalase to find the optimal values that will produce the highest rate of products. It was hypothesized that as the concentration of substrates increases, the reaction rate will as well. The null hypothesis for this is that the substrate concentration will have no effect on the reaction rate. For the varying temperature of catalase, it was hypothesized that as the temperature increases, the reaction rate will increase as well until the enzyme is denatured. The null hypothesis for this is that varying temperature will have no effect on the reaction rate. The experiment was completed by using a 10mL graduated cylinder filled with water that collected oxygen gas that was produced by the reaction. From this experiment, one can see that as the amount of hydrogen peroxide concentration increases, the rate of the reaction increases as well. The results support this as the average reaction rate starts at 0.00 mL O2/min for 0.0% hydrogen peroxide and raises to 38.17 mL O2/min for 0.8% hydrogen peroxide. As the temperature of catalase was increased, rate of reaction continued to
The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case the
Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.
These results that were obtained support the hypothesis that as the temperature of both the solution and liver increases, the froth produced in the measuring cylinder will increase in volume. As the temperature is increased, the rate at which the catalase breaks down the hydrogen peroxide will increase. Once the optimum temperature of approximately 38°C is reached, the reaction rate will then decrease due to the high temperatures denaturing the catalase enzyme. The averages of both the collated froth volume produced and reaction rate, show that as the temperature increased from 10°C to about 30°C the reaction rate increased. Once 30°C the reaction rate generally started to decrease.
However the lab being investigated used the relative concentration of catalase as the independent variable and the oxygen produced in 10min as the dependant variable. However it was noticed that the amount of oxygen conceived by the experimenters with different catalase concentrations had quantitative values very similar to those of the data in question. The lab also proved how the greater concentration in catalase increased the amount of oxygen liberated, evidently the lab in question also had an increase in oxygen liberated however with a greater quantity of hydrogen peroxide. Furthermore it is important to notice the mean data for the lab in question is 42.86 cm^3, although the mean data for lab being investigated is 55cm^3, relative to the time and independent variable, the data remains quite similar. Likewise the lab in question was compared to that of a second lab, THE DECOMPOSITION OF HYDROGEN PEROXIDE BY LIVER CATALASE. By" JOHN WILLIAMS. The lab being investigated shared the exact same catalase solution for the lab thus making it more accurate to the lab in question. Similarly the following lab effectively proved that the greater amount catalase solution in the experiment, the greater velocity the decomposing will have. The results are quite different than the lab in question due to the fact that the IV and DV are both changed in the following lab. Although the results increase, the labs ultimately prove two separate things that are very much linked
During the lab various factors were changed in order to compare how different environmental changes affected the rate of the reaction. A first test was conducted with liver and hydrogen peroxide without an induced temperature change scored a 5. Next, the catalase (liver) was heated to a high temperature and then hydrogen peroxide was added. The reaction was not as fast, and produced a score of 3. A similar test was done using another piece of liver but was placed in an ice bath and then hydrogen peroxide was added. This produced an even slower reaction rate of 2. These three tests demonstrate how temperature greatly influences the rate of enzyme action. When enzymes reach above boiling point, they are denatured and no longer function. Optimal temperatures for enzymes to function is 35-40 degrees Celsius. When the temperature is lower than optimal, slow reactions occur. Further experiments were conducted to show how pH levels affected enzyme action. Two mL of hydrogen peroxide was added to three test tubes. Then, HCl was added to test tube 1, NaOH was
The group with the 4 discs of catalase has a faster reaction rate than the group with two discs of catalase. The control group had the slowest reaction rate. Using a calculator program, the increase in oxygen percentage per second for the group with 4 discs of catalase was 0.0115%, compared to the group with two discs (0.01%) and the control group (0.0062%). The three groups all had different oxygen percentages at the end of the 180 seconds as well. The group with 4 discs of catalase had a higher O2 percentage inside the Nalgene bottle at 0.74% compared to the control group and the 2-disc group, at 0.70% and 0.73% respectively.
· I predict that the enzyme will work at its best at 37c because that
The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,
Members of two groups had designed their experiment on the effect of temperature on catechol oxidase reactions. The graph that was interpreted for this discussion is as above (Figure 6). The independent variable for this experiment was temperature, and the dependent variable was the absorbance of benzoquinone. The first data set in Figure 6 showed that an increase in temperature resulted in a gradually higher absorbance of benzoquinone until the temperature reached 55° C in which the absorbance dramatically dropped. As the temperature went from cold ice to room temperature 55° C, the absorbance of benzoquinone also increased from 0.07 Au to 0.22 Au. This was due to the fact that higher temperature can increase the kinetic energy of particles (Reece et al., 2011). In this case, the temperature was initially cold, and the catechol substrate molecules and enzyme molecules were moving in a slow motion. These particles would collide less frequently; as a result, less absorbance of benzoquinone displayed. When the temperature increased to a room
The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.