Specific environmental conditions may play a role in how enzyme activity is affected. We conducted an experiment to observe whether the change in temperature altered the reaction rate of an enzyme. The activity rate of our enzyme, catechol oxidase, was collected by analyzing the changes in absorption rate of the enzyme in a buffered catechol solution after being placed in four different temperatures. In which one solution remained out in room temperature being to be our negative control. Each of the four solutions were placed in their respective temperature environment and for every two minute intervals, over a twenty minute time process, we read the concentration levels through a spectrophotometer. Solutions placed in higher temperatures read
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After we extracted our catechol from potato juice, we as a group, set five separate cuvettes aside and measured one milliliter of catechol and placed it in cuvettes one through four under the fume hood, also with one milliliter of water and five drops catechol oxidase. Our fifth cuvette acted as our negative control so this one contained no catechol solution and only two milliliters of water. Once the spectrophotometer was zeroed to our negative control we began the actual experimentation process. We then placed all four of the solutions into their respective temperature bathes, the first one at 0 degrees Celsius, the second at 23 degrees Celsius, the third at 37 degrees Celsius, and finally one at 60 degrees Celsius. With our negative control staying at room temperature. Once placed in their appropriate location we immediately set a timer for 2 minutes and took the readings of the concentrations of each solution. Once this data was recorded the solutions were measured on every two minute intervals for a total of twenty minutes by the spectrophotometer in which was set at a wavelength of 440nm. Data was collected and …show more content…
Temperature clearly alters the enzyme reaction rate and the results of our experiment greatly defends our first hypothesis. However, if you single out the data recorded from the solution placed in the 0 degree Celsius and compare it to the rest of the data from the solutions placed in the other heating bathes you will see a quiet interesting result. What we believe that seems to be happening here is a discrepancy in our data because it does not quiet seem to follow the pattern of our other three recordings. We came to the conclusion that the particles inside our solution that was placed in the 0 degree bathe caused the reading in the spectrophotometer to be inaccurate and misread. In future work of similar experiments or use with the spectrophotometer, one should make sure the solution inside the cuvette it is well agitated and shaken to decrease the error of misreading the concentrations. Now, results from the solutions heated in the bathes at twenty three and thirty seven degrees Celsius show us a clear indication that by increasing the temperature we get a higher concentration of enzymes when we measure. And finally, our sixty degree bathe, the hottest bathe, showed the highest reading of concentration. The data collected from this solution really does a great job on complementing our hypothesis because it is our
After we extracted our catechol from potato juice, we as a group, set five separate cuvettes aside and measured one milliliter of catechol and placed it in cuvettes one through four under the fume hood, also with one milliliter of water and five drops catechol oxidase. Our fifth cuvette acted as our negative control so this one contained no catechol solution and only two milliliters of water. Once the spectrophotometer was zeroed to our negative control we began the actual experimentation process. We then placed all four of the solutions into their respective temperature bathes, the first one at 0 degrees Celsius, the second at 23 degrees Celsius, the third at 37 degrees Celsius, and finally one at 60 degrees Celsius. With our negative control staying at room temperature. Once placed in their appropriate location we immediately set a timer for 2 minutes and took the readings of the concentrations of each solution. Once this data was recorded the solutions were measured on every two minute intervals for a total of twenty minutes by the spectrophotometer in which was set at a wavelength of 440nm. Data was collected and …show more content…
Temperature clearly alters the enzyme reaction rate and the results of our experiment greatly defends our first hypothesis. However, if you single out the data recorded from the solution placed in the 0 degree Celsius and compare it to the rest of the data from the solutions placed in the other heating bathes you will see a quiet interesting result. What we believe that seems to be happening here is a discrepancy in our data because it does not quiet seem to follow the pattern of our other three recordings. We came to the conclusion that the particles inside our solution that was placed in the 0 degree bathe caused the reading in the spectrophotometer to be inaccurate and misread. In future work of similar experiments or use with the spectrophotometer, one should make sure the solution inside the cuvette it is well agitated and shaken to decrease the error of misreading the concentrations. Now, results from the solutions heated in the bathes at twenty three and thirty seven degrees Celsius show us a clear indication that by increasing the temperature we get a higher concentration of enzymes when we measure. And finally, our sixty degree bathe, the hottest bathe, showed the highest reading of concentration. The data collected from this solution really does a great job on complementing our hypothesis because it is our