Abstract In this experiment it was examined whether the enzyme peroxidase will work fastest in a pH of 8.0. We placed the enzyme peroxidase in a reaction with guaiacol and hydrogen peroxide in four different pH solutions. Then recorded the absorbencies for each reaction until all substrates were used up, and calculated the initial reaction velocities for each. We found that the reaction in a pH 7.0 solution had the highest initial reaction velocity. Over-all this study shows that the enzyme peroxidase will work the fastest in a 7.0 solution. Introduction Enzymes are useful catalytic proteins that are needed in life that help with both the absorption of nutrients and break them down. They have appeared in both RNA and DNA which means that …show more content…
Test tube 1 contained water, test tube 2 contained pH 4.0, test tube 3 contained pH 7.0, and test tube 4 contained 8.0. A peroxidase enzyme solution was prepared by taking about 2 grams of turnip, cut from the inside, and placing it in a blender with 150 milliliters of deionized water. The final mixture was poured through a coffee filter to make sure there were no large lumps in the mixture. The first test tube received 300 micro liters of guaiacol and 300 micro liters of hydrogen peroxide both measured and dispensed using a micropipette. A pipette was filled with 1 milliliter of the peroxidase enzyme solution that was created earlier and placed in the test tube. The test tube was quickly inverted once or twice and then poured into the cuvette and placed into the calorimeter. The absorbency readings were recorded every fifteen seconds for about five minutes, or until the reaction was complete. The same steps were followed for each of the test tubes. We then calculated the initial reaction velocity for each of the different pHs using the following equation (absorbency as y and time as …show more content…
In test tube 2, when pH 4.0 solution was mixed with the reactants this reaction reached completion at 225 seconds. When pH 7.0 solution reacted with the reactants its reaction went to completion at 180 seconds. Finally, when pH 8.0 solution was mixed with the reactants its reaction came to completion at 210 seconds (Figure 1). Test tube 3 was filled with a pH 7.0 solution had the highest initial reaction velocity followed by test tube 4 containing a pH 8.0 solution. Test tube 2 had the pH4.0 solution which was second to last for the IRV calculation, and finally the base line test tube had the lowest IRV (Table
As pH increases or decreases to get closer to the optimal pH --in this case it is 7 for this particular enzyme-- the rate of reaction peaks and is highest at that point, which is described by the molecular shape and structure of the enzyme at its optimal pH. When turnip peroxidase is at pH 7, the active site is able to fit perfectly with the substrate, therefore explaining why the reaction rate is fastest at this point. Accordingly, if the active site is disrupted, the substrate cannot fit perfectly causing the reaction rate to slow down. This can be supported by the data because the reaction rate gradually increased from pH 3 to pH 7 and reached its maximum at pH 7. Once it did reach the optimal pH, the reaction rate continuously decreased
While conducting this experiment readings were took every 15 seconds for 5 minutes which equals to a total of 20 readings. This experiment had four different trials, a base line trail, a pH 4 trail, a pH of 7 trail, and a pH of 8 trail. Then the results were recorded. The enzyme peroxidase was taken from the inside of a turnip (2g), then blended with 150ml of deionized water, and then poured through a coffee filter into a beaker for a smooth solution. Secondly the colorimeter had to be calibrated by placing a clean cuvette only containing the enzyme solution.
It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.
1 “substrate” and another “ enzyme.” Instead of using the distilled water, this time you are going to use different pH buffer in the enzyme test tube. In the substrate tube, add 7 mL of distilled water, 0.3 mL of hydrogen peroxide, and 0.2 mL of guaiacol for a total volume of 7.5 mL. For the enzyme tube, instead of distilled water add the pH solution (3) and 1.5 mL of peroxidase which equals a total volume of 7.5 mL. Use the dH2O syringe for our pH solution. To clean the syringe, flush it by drawing 6 mL of distilled water.
The level of pH affects absorption of the peroxidase. According to the figure 6, closeness of pH 5 to 7 determines the enzyme’s reaction rates. It had the lowest reaction rate is at pH 3 and 9 while it had the highest at pH 5. In conclusion, the enzyme reaction rate is higher at the neutral state of pH and the pH level affects the enzyme’s activity. Therefore, I accept the hypothesis 3 which was the pH level would affect enzyme
The Purpose To test and analyze the effect of pH and temperature on the reaction rate of the enzyme catalase. HYPOTHESIS The more base you add to the liver the reaction will be faster The more heated the liver is the longer it will take the reaction to take place than if the liver is cold or at room temperature, MATERIALS 8 test tubes Safety goggles Test tube rack Water Ice Bunsen burner Liver Hydrogen Peroxide (H2O2) Hydrochloric acid (HCL) Sodium Hydroxide (NaOH) Liver(cut into small pieces) Test tube holder 2 beakers Pipette Stirring rods Paper Towels Beaker stand Method Gather all the material and put on the safety goggles.
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.26.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3.
LABORATORY REPORT Activity: Enzyme Activity Name: Natalie Banc Instructor: Elizabeth Kraske Date: 09.22.2016 Predictions 1. Sucrase will have the greatest activity at pH 6 2. Sucrase will have the greatest activity at 50 °C (122 °F) 3. Sucrase activity increases with increasing sucrose concentration Materials and Methods Effect of pH on Enzyme Activity 1. Dependent Variable amount of product (glucose and fructose) produced 2.
Introduction The purpose of this lab is to investigate the enzyme action of proteases in pineapple. Enzymes are biological catalyst which speeds up the chemical reaction without being used. Enzymes are protein that is folded into complex shape that allow smaller molecules to fit into them, and also speed up the chemical reaction. It does not get used in chemical reaction, so it can get reuse again.
In conclusion, the data from the experiment supports my hypothesis that catalase will function the most efficiently at a neutral pH of 7. As the pH of the solutions decreased, so did the amount of hydrogen peroxide consumed. Furthermore, after calculating the reaction rates, it is shown that the reaction rate in the solution with a pH of 7 (.5 mm/sec) was higher than any other solution. By looking at the graph above, you can see that as the pH of the solution rose to a pH of 7, catalase became more efficient and was able to better carry out its function. These results help support the idea that as a solution becomes more acidic than the optimum pH of an enzyme, the enzymes present in the solution will denature, and in turn will not be
Introduction 1.1 Aim: To determine the kinetic parameters, Vmax and Km, of the alkaline phosphatase enzyme through the determination of the optimum pH and temperature. 1.2 Theory and Principles (General Background): Enzymes are highly specific protein catalysts that are utilised in chemical reactions in biological systems.1 Enzymes, being catalysts, decrease the activation energy required to convert substrates to products. They do this by attaching to the substrate to form an intermediate; the substrate binds to the active site of the enzyme. Then, another or the same enzyme reacts with the intermediate to form the final product.2 The rate of enzyme-catalysed reactions is influenced by different environmental conditions, such as: concentration
There are many factors which affects the rate of an enzyme catalyzed reaction. The rate of an enzyme controlled reaction is measured by 1.The amount of substrate change per unit time 2.The amount of product formed per unit time 3. The time taken for the completion of the reaction In investigating the effect of one factor : All the factors should be kept constant They must be maintained at suitable levels Only the initial rate should be measured.
Effect of temperature on the reaction between the catalase and H2O2 Figure 1 shows that the optimum temperature for catalase to catalyze hydrogen peroxide is around room temperature (30℃) as it has a very fast reaction rate. The overall trend is that temperatures different from 30℃, will make the reaction rate decrease. Discussion This experiment supported the hypothesis, since catalase was the most effective with hydrogen peroxide when it was in an environment with a temperature of 30℃. It was expected that an extreme temperature would decrease the rate of reaction and results observed support that idea.
Along with being found in plants, they are also present in liver cells, kidney cells, leukocytes and erythrocytes. For the concentration of enzyme experiment, the hypothesis was if the concentration of an enzyme increases, then the enzyme activity will increase as well. The hypothesis was proven to be true, because there are more enzymes to react with substrates. For the enzyme—factors affecting, the hypothesis concluded was if the temperature increases, than the enzyme activity will increase. This however was proven wrong, because enzymes become unstable at higher temperatures.
In this practical, the enzyme that will be used for experimentation purposes is catalase. This molecule is usually found in animal and potato cells, and a substantial amount can be found in any potato extract. The substrate that will be catalyzed is hydrogen peroxide (H2O2,), a common but toxic end product of our metabolism, and highly dangerous if accumulated in the body and not decomposed. It can damage cells if it is not removed.