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Baseline Peroxidase Reaction Lab Report

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For experiment A, we expected that the absorbance values for the baseline peroxidase reaction between guaiacol and hydrogen peroxide would increase over time. This would be due to the increase of color intensity from colorless to brown as the product becomes oxidized towards the end of the reaction. When compared to experiment B, we expected that as the enzyme concentration gets doubled, the absorbance values will increase faster than the baseline over time. The reason why is due to the double concentration of the enzyme that will allow for a better chance of binding to a substrate, which means that the reaction can occur faster. As for half the enzyme concentration, we expected that the absorbance values will increase but at a slower rate …show more content…

We hypothesized that whenever the inhibitor was introduced into the reaction, the absorbance value would be lower than the baseline enzyme reaction. We believed that this was due to the inhibitor competing with the substrate for active site on the enzyme or altering the configuration of the enzyme depending on the inhibition type. If hydroxylamine was a competitive inhibitor, it would bind to the active site which prevents the substrate from binding. However, if it was noncompetitive inhibition, then the hydroxylamine would bind to the allosteric site of the peroxidase. and the substrate may or may not still be able to bind to the active site. We hypothesized that hydroxylamine was a competitive inhibitor that competes with the substrate for the active site. This was due to the fact that it has a similar structure to hydrogen peroxide, which means that it could fit into the enzyme active site, preventing the substrate from binding. The lab results were as expected since as soon as the inhibitor was introduced to the baseline enzyme catalyzed reaction, the absorbance value decreased from 0.254 to 0.017 as shown in Figure 6. In addition, our results show that the absorbance value of the inhibitor baseline reaction increased from 0.017 to 0.038 as the substrate concentration was doubled. This led us to the conclusion that hydroxylamine is a competitive inhibitor and not a noncompetitive inhibitor. The reason why is due to the fact that if the concentration of the substrate increases, then the effects of the inhibitor reverse if it is competitive. If the inhibitor was noncompetitive, then the increase of substrate would not change the effects due to the inhibitor binding to the allosteric site rather than the active

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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

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The addition of the extra catechol was supposed to have sped up the reaction with the enzyme and force the inhibitor out of the enzymes active site. If there was more time allowed to observe any possible color changes the results would have been more conclusive and our results more accurate. In other

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The objective of this lab was to determine the best pH level to increase enzyme activity. As this objective was met, it was discovered that water (pH level 7) was the best for percent absorbance. The hypothesis for this experiment was, “If peroxidase is an enzyme and therefore contains certain pH tolerances, then when placed in solution with pH levels of three, seven, and ten and the reaction is measured by a colorimeter, then water will be the optimal solution for maximum reaction rate.” As seen in the tables and graphs, the data supported the hypothesis due to the fact that most enzymes have an optimal pH of 4-9.

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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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The disks rises to the top of the cup because the substrate, hydrogen peroxide, when sped up by enzyme, creates both water and oxygen as products. The released oxygen is attached onto the disks, allowing it to float to the top of the cup. The way the concentration of enzyme affect the rate of the reaction is because more concentration of enzyme the more active sites are present for the substrate to chemically react with.

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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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By using a spectrophotometer to measure absorbance at 420 nm, the rate of enzyme activity after all reactions have come to a stop can be

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Title: Enzymes Abstract: Enzymes can catalyze chemical reactions by speeding up the chemicals activation energy. Temperature and pH are just two of the factors that affects enzymes and their involvement with chemicals and the way they function. Throughout this experiment, we conducted a study on peroxidase, which is an enzyme. The following information consist of the recordings of when it was exposed to four different pH levels to come up with an optimum pH and IRV at the end. Introduction: Enzymes are proteins that are used in reactions in living organisms.

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After record your data and determine the absolute rate of the enzyme-catalyzed reaction. Based on the data and observations the hypothesis was accepted. It was accepted because when pH were changed to a variety of levels the transmittance began to get higher reaction rates. The increased absorbance means greater amount of product and a higher reaction rate will be produced.

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An enzyme is protein that acts as a catalyst. Catalyst is a chemical agent that increases a chemical’s reaction rate by decreasing the activation energy (initial energy). In this experiment we used Turnip Peroxidase as our enzyme. It was primarily designed to find out if changing different factors such as, the enzyme concentration, temperature, pH and an inhibitor could have an effect on the enzyme’s activity.

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The purpose of this experiment was to analyze the effects of the variables: temperature, pH, and enzyme concentration, on the enzymatic reaction rate of catalase and the level at which its products are released, measuring the rate of absorption using the indicator solution guaiacol and a spectrophotometer to develop a hypothesis of the ideal conditions for these reactions. My hypothesis is that the extremes in concentration, temperature and pH will negatively affect the Au rate. This experiment used 11 solutions contained in cuvettes. Each cuvette, once mixed, is placed in spectrophotometer and then a reading taken every 20 seconds. Cuvettes 1, 8, and 10 are used as blanks to zero out the spectrophotometer.

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The competitive inhibitor that was added was lactose. We predicted this because competitive inhibitors block and bind to the active site so it will slow down the binding of the desired substrate. An alternative hypothesis that came up was that the reaction of substrate would stay consistent as if no inhibitor was added. The enzyme could reject the inhibitor if it does not fit in the active site, causing the substrate to bind as it normally would. Our results showed that with the addition of lactose, the reaction did slow down a considerably

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By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.

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The relative enzyme activities were calculated as μmoles pNPP/minute and analyzed via a students’ T-test (Microsoft Excel 2010, Microsoft, Redmond, WA,

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They can only quicken reactions that will eventually occur, but this enables the cell to have a productive metabolism, routing chemicals through metabolic pathways. Enzymes are very specific for the reactions they catalyze; they make sure the chemical processes go in the cell at any given time. Peroxidase was the enzyme being testing in this experiment. A peroxidase is an enzyme that acts as catalysts, which occurs in biological systems. Peroxidase is found in plants, which they play a role in helping to minimize damage caused by stress factors or insect pests.

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