In this experiment, if the sucrose concentration were increased to 70 g/l would you expect sucrase activity to be significantly…
Lowest? The highest was at pH 7, and the lowest was at pH 2. The catalase enzyme works the best at an optimal pH of 7 (neutral) and works the worst at an acidic pH of 2. How does changing the pH affect the rate of enzyme activity? Does this follow a pattern you anticipated?…
Enzymes are protein molecules that significantly speed up the rate of virtually all of the chemical reactions that take place within the cell. In the following lab was to examine an enzyme that is found in pineapples. That enzyme is bromelain its breaks down protein into their protein into their amino acid by a process of hydrolysis. They are found in tropical areas like Hawaii, Thailand, and Brazil. For the first experiment the hypothesis was that the when gelatin was added to the water, fresh pineapple juice, and canned pineapple juice and submerged into the ice chest the solutions would turn into Jell-O.…
The difference between the two graphs is the speed of the reaction. The temperatures of the two tests were very similar throughout the experiment. when doing this experiment one should have a paper towel ready to wipe the side of the test tube to be able to read the temperature. Conclusion: This experiment tested the difference between a untreated and treated catalase enzyme.…
From 10oC to 20oC, the average rate of reaction of the class results is higher than the raw results rate of reaction by a maximum of 0.75mL/sec. However, from 30oC to 50oC, the raw results presented a slightly higher lot of rate of reaction than the average rate of reaction from the class results. The highest rate of reaction difference was for 50oC, with a difference of 0.3mL/sec between the raw and average results. This information supports the hypothesis, yet the result for 10oC and 20oC do not support the hypothesis, as due to the information known about enzymes, the lower the temperature, the slower the rate of reaction should be, therefore the average rate of reaction does not support the…
The purpose of this lab was to find the optimal temperature for the highest efficiency of Catalase. Catalase is a common enzyme almost present in all living organisms and was obtained by extracting the juice out of potatoes in a complex process that could be a lab itself. It was hypothesized that as the temperature was increased the rate at which the Catalase reactions would be speeded up. A 1% solution of Hydrogen Peroxide was placed in the Catalase and the speed at which the reaction occurred was measured with a stopwatch in seconds. (The stopwatch was stopped once a small filter paper disk soaked in the Hydrogen Peroxide rose)…
Our cells usually make toxic byproducts however they use enzymes to break them down into harmless chemicals. When an excess amount of H2O2 (hydrogen peroxide) is formed in the cell during metabolism/cell respiration catalase enzymes are utilized to break down the toxic chemical into oxygen gas and water. An experiment was conducted was to see if the Ph level affected the rate of which the catalase broke down hydrogen peroxide. A hypothesis was created, which stated that if the ph was lower than the control than the rate of hydrogen peroxide decomposition would be greater. In the experiment there were three trials, a control, a high level ph, and a low level…
The null hypothesis for this experiment reads a change in the substrate, Catechol, concentration then there will be a change in the rate of reaction. The alternate hypothesis states if there is a change in Catechol concentration then there will be no change in the rate of reaction. To explain the null, if one chooses to change the amount of substrate in each trial then you should expect to see a change in a number of products produced in those trails. I predict that the trials with less concentration of the substrate will yield a lower rate of reaction and vice versa. In the experiment, test tube 2 was filled with 6mL of the substrate, Catechol, and test tube 3 was filled with 4mL of the substrate.…
The goal of this experiment was to determine the Michaelis constant (Km) and also the maximal velocity (Vmax) and the inhibition of alkaline phosphate. In order to accomplish these goals, 5 samples were used. Each sample contained different volumes of 0.2 m MPNPP (p-nitrophenylphosphate) and 0.2 M Tris-Hcl at a pH of 8.0. To each sample 0.2 mL of the enzyme studied (Alkaline Phosphatase) were added upon insertion on the spectrophotometer apparatus. With intervals of 20 seconds their absorbance at a wavelength of 410 nm was recorded at time frame of 2 minutes for each solution.…
The experimental results do agree with the known optimum conditions of TEM-1 B-lactamase. Most proteins functions ideally when the temperature is 37oC, and the pH is 7.4. When there is no competition between the salt ions and the charge residues of the proteins for water, and when there is no detergents to denature the protein even at a low concentration. There were few sources of errors during the experiment. During experiment 1, the enzymes were kept in the heating block for little too long.…
In this lab we learned the basics of enzymes and how they work. We were able to perform a quantitative assay of the activity of an enzyme in a tissue extract using a spectrophotometer. Also, we had to organize the data that was provided into tables and graphs so we could have the ability to test a few hypotheses. For example, we tested the whether the rate of the reaction was influenced by enzyme concentration, whether the activity of the enzyme was influenced by temperature and also too see if the activity of the enzyme was influenced by the pH of the solution, which you will then see the results on the graphs and charts that I provided. In figure one we show results of the trial run from the enzyme activity where the absorbance was at 500nm.…
However, when the substrate concentration was increased, the intensity of color stopped increasing due to the enzymes being unable to to process at a faster rate. All of the alternate hypothesizes were supported; in the experiments, section one (with Figure 1) had an optimal temperature at approximately 24°C; section two (with Figure 2) had an optimal pH at approximately pH8; in section 3 (with Figure 3) the color continued to increase with the addition of more enzymes; and in section 4 (with Figure 4) the color continued to increase until it reached a maximum velocity with the addition of more substrates. One desired retrial for the experiment would be to test for more points after 20 drops of potato juice in Figure 3. Understanding the effects of how these properties alter the ability of the catecholase enzyme could allow for better insight into decreasing time needed for biochemical reactions, proper food storage, and the condition of…
This data was collected by placing a timer and acquiring the reaction every five seconds for a minute. (see pg. 35 lab manual) During the second experiment to observe the optimal pH of the enzyme. Additionally, five test tubes were prepared with different levels of pH. These tubes had 1 mL of the substrate mixture and every test tube had its own type of pH.…
The purpose of this experiment is to detect the presence of saccharides in different samples through the use of Benedicts reagent and Lugol’s solution. Monosaccharides have a double bonded oxygen atom that forms in one of its two possible chemical groups known as ketone or aldehyde. Disaccharides are two monosaccharides joined together by a glycosidic bond. The Benedicts reagent reacts with the double bonded oxygen atom in monosaccharides by reducing the copper sulfate found in the reagent. Therefore, Benedicts reagent is used in this experiment to detect the presence of monosaccharides and disaccharides.…
Many factors can affect the enzyme activity (including temperature, pH, substrate concentration), so all conditions apart from the one being quantified should be standardised. The…