Effects of Changing Temperature of Catalase During Reaction
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Published: Mon, 14 May 2018
For each reaction trial, the amount of oxygen produced, final temperature of solution, final volume of solution, and total reaction time were recorded. The amount of oxygen produced was found by observing the amount of water displaced in the 100 mL graduated cylinder that was in the pneumatic trough. The final temperature of the solution was found by using a thermometer to find the temperature of the solution right after the reaction had taken place. The final volume was found by first taking the 100 mL graduated cylinder out of the trough and emptying it. Then the final solution was transferred from the Erlenmeyer flask into the 100 mL graduated cylinder where the volume was recorded. The total reaction time was recorded by using a stop watch, starting when the hydrogen peroxide was first mixed with the liver, and stopped when no more water was being displaced out of the 100 mL graduated cylinder.
The results for this experiment showed various things. Firstly, the results for this experiment initially went against the hypothesis, where all the responding variables were higher for the hypothermic and hyperthermic temperatures. When the data was manipulated however, to show the efficacy of oxygen production, the results were in favor of the control variable at human body temperature. This can be seen in Graph 1, as the temperature increases, there is an increase in the efficacy of oxygen production until 37°C ± 0.5°C where the efficacy again starts to decline.
These results show that though the rate of oxygen production were highest at slightly hyperthermic and slightly hypothermic temperatures, more of the reactants were used in the process in comparison to the amount used at human body temperature. This relationship between the volumes of reactants used to the temperature of the Catalase can be seen in Graph 2.
Therefore, there was a higher efficacy in the reaction at normal human body temperature (37°C) since there was a higher rate of oxygen production at a much lower amount of Catalase being reacted.
These results agree with other resources and experiments. According to scientific research, the optimum temperature of Catalase is normal human body temperature at around 37°C (Chelikani, 2004). As this temperature increases, Catalase is still able to react efficiently until 40°C, where the enzyme shows a significant drop in reaction efficacy due to the denaturing of the protein at higher temperatures (Chelikani, 2004). This research agrees with the efficacy of oxygen production trend in Graph 1, where it is highest at 37°C and then has a significant drop at 40°C.
The raw data for the responding variables in this experiment showed that the highest amounts of reactants used were in hypothermic temperatures. This could be due to the fact that since Catalase is a biochemical enzyme, its catabolic reaction is a subtle and elegant biological reaction which reduces the amount of activation energy required for a reaction (Sivrikaya, 2009). Therefore, an optimum reaction of Catalase reacts with minimal energy consumption.
However, other sources of research state that the Catalase in chicken liver differs highly from that of humans (Aydemir, 2003). The source also claims that Catalase in chicken erythrocytes have an optimal temperature of 25°C in experiments (Aydemir, 2003). This could explain why the experiment still had high amounts of oxygen productions at 25°C, which was in this case being tested as extreme hypothermia.
Sources of Error
One large source of error could have been the source of Catalase. Since Catalase can come from a variety of sources, using chicken liver may not have been the best choice. The choice of the source of Catalase in this experiment was to model Catalase in the human body in order to observe changes of the reaction in different human body temperatures. Chicken liver however, may not have been the most efficient at modeling Catalase reactions in human body conditions; this prediction also backed up by other scientific research (Aydemir, 2003). For a much more accurate experiment, a Catalase sample would be required from the human body, of course however this is very unlikely. Instead, more in depth research could have been done to find a better model of human liver. Using cow liver would have been a slightly better modification to cow liver, however still not a perfect match. This would have possibly given more consistent data, better modeling that of the human body.
Another source of error was maintaining the temperature of the Catalase. The method in this experiment brought the Catalase to a certain temperature but did not allow for the enzyme to maintain the temperature long enough to create a significant change. A correction to this would have been to bring the water to the increment temperature instead, and while maintaining the water temperature, adding the closed Erlenmeyer flask of liver into the water for approximately 5-10 minutes. This would have allowed the enzyme to become more denatured at higher or lower temperatures, respectively.
The hypothesis for this experiment was proven wrong, production of oxygen and reaction time were in fact lowest for the normal human body temperature of 25°C. However, the manipulated data found in Table 1, showed that since the oxygen production rate compared to amount of reactants used was highest at 37°C, it had a better efficacy then the other increments. The results however, failed to show significant changes in hypothermic temperatures. On the other hand, the data showed a moderate decrease in enzyme efficacy and rate of oxygen production at extreme hyperthermic temperatures of 41°C.
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