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Rate Of Peroxidase Lab Report

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Abstract To figure out how temperature effects the change in the rate of an enzyme, test tubes were filled with solutions of buffer with a pH of 5, peroxidase, H2O2, and guaiacol and placed different water baths of the following temperatures: 4°C, room temperature (23°C), 32°C, and 60°C. To help determine the rate of reaction of peroxidase, a spectrophotometer was used to measure the absorbances of the solution. There was also a recovery portion to check the functionality of the enzyme after being tested under varying temperatures. We had discovered that there were increases in the rate activity of reaction of peroxidase around 4°C and 32°C and that the enzyme had ceased in activity once it reached 60°C. This indicated that the rate of reaction …show more content…

Two test tubes were then paired with each of the following temperatures: 4°C, room temperature (23°C), 32°C, and 60°C. 4.0 ml of buffer with a pH of 5 and 1.0 ml of peroxidase was filled into one test tube from each of the temperatures. The other test tubes were filled with 2.0 mL of H2O2 and 1.0 mL of Guaiacol dye. As the 4°C, 32°C, and 60°C test tubes set in its corresponding water bath for 15 minutes, the room temperature test tubes proceeded with the experiment. A blank test tube was used to calibrate the spectrophotometer to zero. After calibrating the spectrophotometer, the room temperature test tubes were mixed together by pouring its contents back and forth twice. Once mixed, the solution was poured into a cuvette and placed in the spectrophotometer. The absorbance of the solution was analyzed in 20-second intervals for two minutes. After 15 minutes elapsed, the other test tubes were taken out of their baths and the mixing and absorbance processes were repeated. To test if peroxidase can regain its functionality after it has been affected by the temperature, the procedure was repeated but the solutions were allowed to return to room temperature after being its respective temperature baths for another 15

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The effect of pH on the speed of enzyme interaction with substrate chemicals Hypothesis: About pH: If the pH level is less than 5, then the speed of the enzyme reaction will be slower. About temperature: If the temperature stays the same, then the speed of the enzyme reaction will not be completely affected. Background information: The function of enzymes is to speed up the biochemical reaction by lowering the activation energy, they do this by colliding with the substrate.

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ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.

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Enzymes speed up chemical reactions enabling more products to be formed within a shorter span of time. Enzymes are fragile and easily disrupted by heat or other mild treatment. Studying the effect of temperature and substrate concentration on enzyme concentration allows better understanding of optimum conditions which enzymes can function. An example of an enzyme catalyzed reaction is enzymatic hydrolysis of an artificial substrate, o-Nitrophenylgalactoside (ONPG) used in place of lactose. Upon hydrolysis by B-galactosidase, a yellow colored compound o-Nitrophenol (ONP) is formed.

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7. Will the temperature effect the pH Scale? Hypothesis: The hypothesis of this experiment is that the rate of reaction will increases well as the hydrogen peroxide concentration. If the temperature, pH and enzyme concentration is kept constant then the rate of reaction will start to decrease as well as the hydrogen peroxide concentration. Aim: To investigate the effects of changing the concentration of the enzyme catalase that it has on the rate of breaking down the Hydrogen Peroxide solution.

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Through the oxidation of those phenols, a chemical reaction that causes a loss in electrons is present which usually results in a red or brown color. Due to the varying levels of reaction possibilities that catechol can undergo when in contact with DNA makes it toxic to humans (Eggen RI, Schweigert, Zehnder AJ). In order to measure enzyme activity through the different environmental parameters, the experiment will need utilization of a spectrophotometer to record the change in absorbance and compare how different temperatures either support or inhibit enzymes. In this, ethylenediaminetetraacetic acid (EDTA) was used to act as a chelator which aids in the removal of ions, this provided favorable environments for enzymes to speed up the reaction process. On the other hand, phenylthiourea (PTU) was used as an inhibitor that only worked if catechol oxidase had copper as a

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The data received in the experiment only somewhat supported my hypothesis. My group tested how changing the pH of the hydrogen peroxide substrate would affect enzyme activity and the rate of reaction. Our hypothesis was that the solution with a pH closest to the pH of hydrogen peroxide, which is fairly acidic, would have the fastest rate of reaction. After conducting the experiment, we found that an acidic pH of 2 resulted in the reaction having a reaction rate of 0 sec-, while when conducted with a substrate pH of 7, the reaction proceeded at the fastest rate of 0.051 sec-. These results show that a pH of 7—a more neutral solution—actually caused the enzyme to work the best, as opposed to the predicted acidic substrate.

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3.6.4 Assay of Catalase (CAT) Catalase activity was assayed by measuring the inhibition rate of Hydrogen peroxide at 240nm according to the method described by Luck (1974). For this assay, • A 20% homogenate of the leaf extracts of different plants was prepared in phosphate buffer, 0.067 M (pH 7.0). The homogenate was then centrifuged.

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These enzymes have a secondary and tertiary structure and this could be affected by increases and decreases in temperature beyond the optimum temperature of the enzyme to work in. Mostly enzymes are highly affected any changes in temperature beyond the enzymes optimum. There are too

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For example, between pH 5 and 7, there is an almost 500 mL difference, even though they are only 2.0 away on the pH scale. This shows even small changes in pH can have a large difference in the rate of reaction. Evaluation of Conclusion: The data and conclusion does match with previous background research. Background research suggests that reaction rate increases with pH until a point where optimum pH is reached, after which the enzyme is denatured and no longer can perform its function. This research was also shown in the data, even though the point at which the enzyme denatured was not

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