Lab Report Part 1 Essay
Part 1 dilutions participated as a trail run to gather around the “full enzyme” that was used for the other parts of the experiment. Part 2 readings were in the time span of 10 minutes and the final results show a spontaneous increase in the first minutes of the absorbance readings. They then showed a steady reading towards the end of timing. The amount of enzyme is decreasing as the dilution occurred. The activity it catalyzes measures the amount of enzyme present in the reaction (Introduction to Enzymes). Part 3 had the similar steps so the rates must have been in a similar range when dealing with dilutions. In this part, it was displayed with the readings and rates that the substrate amount was decreasing. From the use of the formula, the
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reaction rate as shown in the table can confirm the decline of substrate. The line graph displays the opposite of the dilution process.
By theory, it’s known that when this maximum speed had been reached, all of the enzyme that is available has been converted to the ES (enzyme substrate complex) (Introduction to Enzymes).
Part 4 of the experiment had the addition of the inhibitor to see what sort of inhibition it was known as. After doing the steps of the experiment for Part 4, readings led us to determine the reaction rate with the inhibitor and without the inhibitor. Table shown below displays the results of the rates with the percentage inhibition which is calculated by this formula: ([rate without inhibitor – rate with inhibitor] / rate without inhibitor) times 100. Inhibitors are the substances that lower the rate of enzymatic activity;That occurs usually by binding with the enzyme and by the interference with the formation of the ES (Enzyme Kinetics - Factors Influencing Activity). Determined using the information of the table, data was transferred to make a line graph of percent inhibition versus the substrate concentration. Noncompetitive inhibition would have resulted in a different form of linear graph. It shows a constant substrate concentration because there is no competition at the active site, so everything flows in order unlike competitive inhibition. Active sites are more and more occupied that the substrate doesn’t end up sometimes binding to the active
site.
Part 5 had the procedure dealing with enzymes exposed to different temperatures. The absorbance of the enzyme was recorded in the time of every 60 seconds for 3 minutes.
Sometimes in experiments there are issues where the outcome is not what was intended to be such as what happened to the rate of the frozen enzyme. As the temperature increases, the reaction rate increases also unless it reaches a stop when extreme temperatures are reached since enzymes catalyze by random colliding with substrate molecules (Factors affecting Enzyme Activity). The frozen enzyme’s rate was more than what was expected. A problem like that could be caused by not letting the enzyme reach back to room temperature and take the reaction rate accordingly. Results in the graphed data show the problem being mentioned.
Part 1’s analysis proves the concentration of substrate by dilution to reach a different standard when added to a solution. There was a difference of reaction rate when the substrate is applied to the solution than when there was none added. The graph of Part 2 helps display that by the less dilution of the enzyme, the higher the reaction rate would become. Part 3’s illustration supports the conclusion that the more substrate that was less diluted, the more of the reaction rate would increase due to the substrate concentration taking a big role in the binding to the active sites and causing a higher enzymatic activity. The inhibitors in Part 4 were used to determine which of the inhibition was processing with the enzyme being used. Catechol being the substrate showed that it is competitive when wanting to bind to the active site once the enzyme was added. Part 5 shows the temperature difference affecting the reaction rate of the present enzyme although in this experiment it did not happened as it was intended to follow a literature optimum temperature chart, so we could run the trial again.
reaction rate as shown in the table can confirm the decline of substrate. The line graph displays the opposite of the dilution process.
By theory, it’s known that when this maximum speed had been reached, all of the enzyme that is available has been converted to the ES (enzyme substrate complex) (Introduction to Enzymes).
Part 4 of the experiment had the addition of the inhibitor to see what sort of inhibition it was known as. After doing the steps of the experiment for Part 4, readings led us to determine the reaction rate with the inhibitor and without the inhibitor. Table shown below displays the results of the rates with the percentage inhibition which is calculated by this formula: ([rate without inhibitor – rate with inhibitor] / rate without inhibitor) times 100. Inhibitors are the substances that lower the rate of enzymatic activity;That occurs usually by binding with the enzyme and by the interference with the formation of the ES (Enzyme Kinetics - Factors Influencing Activity). Determined using the information of the table, data was transferred to make a line graph of percent inhibition versus the substrate concentration. Noncompetitive inhibition would have resulted in a different form of linear graph. It shows a constant substrate concentration because there is no competition at the active site, so everything flows in order unlike competitive inhibition. Active sites are more and more occupied that the substrate doesn’t end up sometimes binding to the active
site.
Part 5 had the procedure dealing with enzymes exposed to different temperatures. The absorbance of the enzyme was recorded in the time of every 60 seconds for 3 minutes.
Sometimes in experiments there are issues where the outcome is not what was intended to be such as what happened to the rate of the frozen enzyme. As the temperature increases, the reaction rate increases also unless it reaches a stop when extreme temperatures are reached since enzymes catalyze by random colliding with substrate molecules (Factors affecting Enzyme Activity). The frozen enzyme’s rate was more than what was expected. A problem like that could be caused by not letting the enzyme reach back to room temperature and take the reaction rate accordingly. Results in the graphed data show the problem being mentioned.
Part 1’s analysis proves the concentration of substrate by dilution to reach a different standard when added to a solution. There was a difference of reaction rate when the substrate is applied to the solution than when there was none added. The graph of Part 2 helps display that by the less dilution of the enzyme, the higher the reaction rate would become. Part 3’s illustration supports the conclusion that the more substrate that was less diluted, the more of the reaction rate would increase due to the substrate concentration taking a big role in the binding to the active sites and causing a higher enzymatic activity. The inhibitors in Part 4 were used to determine which of the inhibition was processing with the enzyme being used. Catechol being the substrate showed that it is competitive when wanting to bind to the active site once the enzyme was added. Part 5 shows the temperature difference affecting the reaction rate of the present enzyme although in this experiment it did not happened as it was intended to follow a literature optimum temperature chart, so we could run the trial again.