In this lab an alternate hypothesis and a null hypothesis were created to help set a structure for the lab. The alternate hypothesis was: There will be a decent amount of variation in enzyme activity in the different pH solutions. The null hypothesis was: There will be little or no variation in enzyme activity in the different pH solutions. The two pH that were tested in this particular section of the lab were pH 8 and pH 9. The results are as following: pH 8 (.018%/min, .002%/min, .003%/min, .017%/min, and .002%/min); pH 9 (.013%/min, .005%/min, .003%/min, .002%/min, and .002%/min). These results are the rate of enzyme activity in the two different pH, judging by these results the null hypothesis can be accepted; there was little variation …show more content…
Enzymes have optimum pH levels for the most enzyme activity to occur and it looks like pH 8 and pH 9 were not the optimum pH levels for Amylase. In a report from JStage there was further proof that enzymes have optimum pH levels, in the case of Amylase it is from a pH of 5 to a pH of 7 that there will be a lot of enzyme activity. Since the section of the lab performed involved pH 8 and pH 9 it explains why there wasn’t much enzyme activity, the optimum pH level was not achieved. There was a lot of human error to take into account, this lab required high amounts of precision to be done by laboratory machines but instead it was performed by humans; the amount of enzyme was improperly measured, the amount of starch solution was improperly measured, the timing of the solutions was off despite the use of stopwatches, solutions had to be remade because of mixing them up, data was improperly read and improperly recorded, and too much of the lab was attempted at once causing mistakes to be repeated and sometimes missed. The function of Amylase is to break down plant starches while the function of Ligase is to join the gaps that form in DNA during replication. Amylase is usually used in baked goods, beverages, and conversion of starches to sugars; Ligase is usually used in DNA laboratory research. Amylase is normally found in the saliva of
Describe the relationship between temperature and the enzymatic activity of lactase. Of the three temperatures tested, which is the optimal temperature for enzyme activity? Use the results in Data Table 2 to support your answer. Hypothesize how the structure of the lactase relates to the results in Data Table 2. Answer-
This evidence alone suggests that higher increases in substrate concentration causes smaller and smaller increases in enzyme activity. As substrate concentration increases further, some substrate molecules may have to wait for an active site to become empty as they are already occupied with a substrate molecule. So, the rate of the reaction starts to level off resulting in a plateau in the graphs. This means that the reaction is already working at its maximum rate, and will continue working at that rate until all substrates are broken down. The only way the reaction rate would increase, is if more enzyme was added to the solution. This confirms that increases in substrate concentration above the optimum does not lead to greater enzyme activity. Therefore, the rate of reaction is in proportion to the substrate
For example, substrate concentration, enzyme concentration, and temperature could all be factors that affected the chemical reactions in our experiment. The concentration of substrate, in this case, would not have an affect on how the bovine liver catalase and the yeast would react. The reason why is because in both instances, the substrate (hydrogen peroxide) concentration was 1.5%. Therefore, the hydrogen peroxide would saturate the enzyme and produce the maximum rate of the chemical reaction. The other factor that could affect the rate of reaction is enzyme concentration. Evidently, higher concentrations of catalase in the bovine liver produced faster reactions, and the opposite occurs for lower concentrations of catalase. More enzymes in the catalase solution would collide with the hydrogen peroxide substrate. However, the yeast would react slower than the 400 U/mL solution, but faster than the 40 U/mL. Based on this evidence, I would conclude that the yeast has a higher enzyme concentration than 40 U/mL, but lower than 400
For example, incubating the samples at different temperatures would create more data points to establish an optimal temperature. From the results in the experiment in this study, it is known as temperature increases, enzymatic activity increase, and vise versa. However, what can not be observed is at what point does the increase in temperature begin to denature the enzyme, above 60°C. Furthermore, assays can be preformed to determine optimal pH, as well. From Dutta’s, and his partners, experiment it shows that there is a range where the Heliodiaptomus viduus’s lactase shows the most activity, which is between 5.0 and 6.0
For this experiment the null hypothesis is that the intensity of the step rate test (High and Low) has no effect on the persons’ heart rate and recovery time. While the alternate hypothesis is that the intensity of the step rate test (High and Low) has an effect on the persons’ heart rate and recovery time.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
If the amount of either hydrogen peroxide or yeast is different in any of the sections in the experiment then the results
...e substances at 37.5̊C due to the fact that in the previous experiment, this was found to be the optimum temperature that catalase reacts at. It was because of this constant that I used the set of data of the catalase at 37.5̊C from the first experiment to provide a neutral environment for the experiment. The way in which the data was collected for the first experiment was identical to that needed to be done by the second. From this data, it was determined that the neutral environment for the catalase had the best results, which makes it clear that when the enzyme is in a pH of the opposite extremes such as basic or acidic, it is un able to function properly. When it is too basic then the enzyme will become inactive and when the enzyme is too acidic then the enzyme will denature, both rendering it unable to function at its optimum efficiency that all enzymes need.
Investigating the Effect of Enzyme Concentration on the Hydrolysis of Starch with Amylase Aim: Investigate the effect of enzyme concentration on the rate of an enzyme-controlled reaction. Using amylase and starch as my example. Introduction: I am investigating the effect of the concentration of the enzyme, amylase on the time taken for the enzyme to fully breakdown the substrate, starch to a sugar solution. The varied variable will be the concentration and all other variables are going to be fixed. The different concentrations will be: 0.5% 0.75% 1.0% 1.5% 2% An enzyme is a class of protein, which acts as a biological catalyst to speed up the rate of reaction with its substrates.
Enzymes as mentioned before help speed up reactions, they generally work by bonding to a substrate, this bonding occurs at the active site. This link then forms a different molecule which will benefit its respective process. Every enzyme has its own optimum pH level to work under, if too low the enzyme will be very slow. However if too high the enzyme will then denature and be obsolete. This is why it is important to know the optimum pH level for whatev...
From looking at the results I can conclude that when the pH was 3 and 5. No oxygen was produced, therefore no reactions were taking place. This was because the pH had a high hydrogen ion content, which caused the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place of the syringe. The enzyme lost its functional shape.
or it may be optimum it depends on what is the best pH that the enzyme
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
5 test tubes were prepared for dilution respectively to 5 spec tubes that had the inhibitor and water and ready for the enzyme addition. Recordings were done every 60 seconds for 3 minutes. Reaction rate was then calculated after time ended. After having used the inhibitor, the steps were repeated but replace the inhibitor with water as control and experimented for the rates without the inhibitor. Percentages were graphed by the percentage inhibition versus the substrate concentration for the inhibitor. Part 5 of the experiment was to determine the effect of temperature or pH on the reaction rate. In doing so, each group in the lab was designated a particular enzyme that was exposed in different temperatures (Schultz, 2006). The enzymes were exposed before the beginning of the experiment into these different temperatures: boiling, warm (heat), room temperature, cold (ice bath), and frozen. Each enzyme was allowed back to room temperature before adding the buffered catechol with the 1 ml of enzyme into the spec tube (Schultz, 2006). Reaction rate was then determined from the reading. Absorbance versus time was plotted with the determined initial rate of each
Firstly, we need to keep the chemical at a constant concentration. So, in this experiment we have chosen to keep hydrochloric acid at a constant concentration (5cm3). We could have, however, used Sodium Thiosulphate as a constant, but we had chosen to use Hydrochloric acid. Next, we must make sure that the solution is kept at a constant volume throughout the experiment. If the volume is different, then it could give different results if it was at a constant volume.