Saturday, April 6, 2019

Influence of pH on the activity of Potato catalase Essay Example for Free

Influence of pH on the activity of Potato catalase Essaythusly SA = 7. 065mmi. So, 7. 065mmi x 50mm bequeath provide the volume of the 5cmi space in the manometer tube, which is 353. 25mmi. The rate of reaction can at once be calculated as Rate of Reaction = Volume Time The results for the rate of reaction atomic number 18 displayed as follows pH Average Time/Seconds Rate of ReactionRate of Reaction Results Graph stopping point From the average beat and rate of reaction results, it can clearly be seen that the fastest and shortest reaction era was for the pH of 6. 3. Basically, this shows that the most appropriate pH for the enzyme Catalase to function in is a pH of 6. 3 as it the enzyme is forming a complex with the substratum and producing the by-products Hi O and Oi , at a faster rate. The least useful pH buffer to use in a Catalase reaction would be a pH of 2. 8, although in that location may be more inhibiting pHs outside the range used in the experiment.The longest reaction was for the pH 2.8 and the smallest rate of reaction was also, on that pointfore pH 2. 8. Moving up the pH range used in the experiment, the rate of reaction continues to increase until the optimal point of pH 6. 3, where the rate of reaction slows and average time taken begins to increase above this point, as shown in the pH 8. 3 results and graph. Evaluation Overall, the experiment was conducted in a suitable way that enabled the collection of relatively reliable results however as with most experiments thither were some sources of misapprehension in its conduction that will shake had an effect on the results.The main error in this experiment was the factor of human error this was mainly present in the measuring and clock stages of the experiment. The measurement of the buffer solutions, hydrogen peroxide and cutting of potato discs will concur had slight discrepancies in their quantities this will pay back had a small effect on the results as the enzyme and substrat e amounts will have varied and the rate at which products are formed will have increased or decreased. To fend off human error in the experiment the measurements and timing would have to be done by exploitation more technological equipment, in order to gain precise results.Another factor that will have influenced results is the presence of inhibitors when the reaction took place these occur naturally and can be either competitive or non-competitive A competitive inhibitor molecule has a similar structure to the normal substrate molecule, and it can rifle into the active site of the enzyme. It therefore competes with the substrate for the active site, so the reaction is slower. A non-competitive inhibitor molecule is instead different in structure from the substrate molecule and does not fit into the active site.It binds to another set off of the enzyme molecule, changing the shape of the whole enzyme, including the active site, so that it can no longer bind substrate molecules . Non-competitive inhibitors therefore simply reduce the amount of active enzyme similar to decreasing the enzyme concentration. In conclusion, the presence of these inhibitors will have altered the reaction by increasing or decreasing the rate at which the products are produced. There will have been limitations in the results as the range of buffer solution pHs used in the experiment were inadequate to determine an exact optimal pH for the enzyme Catalase to function.To find the optimal pH, further tests could have been conducted by using pHs with closer intervals within the range of 4. 5 and 6. 5, where the rate of reaction increases sharply, as shown on the graph by an arrow. By analysing the results and the graphs that were produced, there are no obvious anomalies in the results achieved however there may have been a slight discrepancy in one result which is marked on the graph/s with a circle. This could have been a consequence of any of the factors mentioned above in the milit ary rating section.

No comments:

Post a Comment