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Catechol Oxidase Lab Report

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An Enzyme is a macromolecule that helps decrease the time for a reaction to take place [1]. They are very important to cells as they reduce the EA barrier, or the activation energy required to get a reaction en route [1]. The enzyme does not get consumed by a reaction it facilitates, and thus can be reused [1].
The enzyme used in this lab is Catechol Oxidase. This lab is separated into two experiments: one measuring the effects of temperature on the enzyme, and one testing the change of pH on the enzyme. To observe the effects of temperature and pH, spectrophotometry is used to test the absorbance of light in intervals of thirty seconds over a time period of three minutes. For the first experiment I hypothesize that when the temperature is …show more content…

After 5 minutes the substrate catechol is added and the solution placed in the spectrophotometer. Table 1 consists of my group’s data and another group’s data. My group’s ice bath trial failed so I will use the other group’s data for that temperature category. In table 1, my group’s room temperature absorbance reading initially started at 2.288, then proceeded to increase to the 2.4 range where the level stayed for the remaining time. For the boiling temperature, the initial reading was 0.220 with a very minimal increase in absorbance. At the end of three minutes the absorbance level was only 0.234. The hot temperature seems to have slowed the enzyme’s ability. The other group’s ice bath reading started at a low 1.326 it then grew rapidly over thirty seconds to the 2.4 range that the room temperature was also at. The cold temperature seemed to slow the enzymatic activity. The difference between the cold and room temperatures can be observed in graph 1 …show more content…

My group’s data is in column 2, the pH we tested the enzyme with was 4. In table 2 column 1 the pH used was a very acidic 2. At a pH of 2 the absorbance had a very minimal change gravitating around ~0.74. The pH 2 solution slowed the enzyme down significantly. In the next column the solution’s pH was 4. Initially the absorbance was 1.410, and steadily increased by ~0.1 every thirty seconds. At 180 seconds the absorbance hit 2.070 which is the largest change of absorbance level out of the pH experiment. With a pH of 7 the absorbance levels started at 1.186. From there it increased to 1.325, then decreased to 1.023. The pH 7 solution did not have much effect on enzymatic activity as the absorbance maxed out early on. Water stayed a consistent ~0.87 throughout the 180 seconds. In column 5 with a pH of 8, the absorbance started at 0.425 and then dropped to 0.402 at the 180 second mark. The solution with a pH of 10 initially started at 0.524, it too decreased in value ending at 0.474. The more basic solutions seem to stop enzymatic activity at the very

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