Rate Of Reaction Lab

The hypothesis is that catalase activity will increase exponentially with higher concentrations of hydrogen peroxide until all catalase active sites are filled, in which case the

The topic of this lab is on biochemistry.This experiment was conducted to show how cells prevent the build of hydrogen peroxide in tissues. My group consisted of Lekha, Ruth, and Jason. There were used two different concentrations of hydrogen peroxide through this experiment , 1.5% and 3%. By testing two different types it is easier to understand how the H2O2 and catalase react with one another. To do this both the yeast, which was our catalase, and H2O2 were mixed together in a beaker. Each concentration was tested out twice for more accurate results . 1.5% concentrated H2O2 had an average reaction rate of 10.5 seconds while 3% concentrated H2O2 had an average reaction rate of 7.5 seconds. From this experiment we learned that by increasing the concentration of H2O2 and chemically combining it with a catalase it will speed up the reaction. Enzymes speed up chemical reactions . The independent variable in this experiment was the concentration of the H2O2. Some key vocabulary words are Catalase, enzyme, hydrogen peroxide ( H2O2), and concentration.

This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide.

Lab six requires students to observe the effects of pH and enzyme concentration on catecholase activity. Enzymes are organic catalysts that can affect the rate of a chemical reaction depending on the pH level and the concentration of the enzyme. As pH comes closer to a neutral pH the enzyme is at its greatest effectiveness. Also at the absorbance of a slope of 0.0122 the enzyme is affected greatly. The pH effect on enzymes can be tested by trying each pH level with a pH buffer of the same pH as labeled as the test tube and 1mL of potato juice, water, and catechol. This is all mixed together and put in the spectrophotometer to test how much is being absorbed at 420nm. As the effect on enzyme concentration can be tested almost the same way. This part of the exercise uses different amounts of pH 7-phosphate buffer and potato juice, and 1mL of catechol mixed together in a test tube. Each substance is put in the spectrophotometer at a wavelength set tot 420nm. The results are put down for every minute up to six minutes to see how enzyme concentration affects reaction rate. The results show that the pH 8 (0.494) affects the enzyme more than a pH of 4 (0.249), 6 (0.371), 7 (0.456), and 10 (0.126). Also the absorbance is greatest at a slope of 0.0122 with test tube C that has more effect on the reaction rate, than test tube A, B, and D.

The time in the water bath was also controlled to ensure that the enzymes were left to react for the same amount of time, making the experiment

The null hypothesis for the first experiment was that substrate concentration would have no effect on the reaction rate. It was hypothesized that the reaction rate would increase with rising substrate concentrations, until all active sites were bound. The null hypothesis for the second experiment was that temperature would not have an effect on reaction rates. It was hypothesized that until the enzyme is denatured, as temperature increased, so would the reaction rate.

In both experiments, there was one environment that the enzyme worked best it. The graphs show that in the salt experiment 4% salt concentration was the optimum environment for the enzyme, and pH 6 buffer solution was the optimum pH environment for the enzyme. In the other environments the enzyme did not work as fast, therefore not creating as much product. The hypothesis was that the enzyme would work the most efficiently in the most neutral environment. The data does support this hypothesis; therefore we would accept the hypothesis. The neutral state for pH is pH 7, so the enzyme would be most active at exactly pH 7. With pH 6 buffer solution, the enzyme is working, but after pH 7, the enzyme begins to denature at becomes less effective. For the salt experiment, the hypothesis was that the enzyme would be more productive in the solution that had the least salt concentration. As the salt concentration increase, the enzyme would be being to denature. In this experiment, the hypothesis was incorrect, so it had to be

6. Plan and conduct your own investigation into one other factor that affects the activity of catalase, you may use this as the basis for your investigation but if it is to be for moderation of internal assessment you must modify it substantially.

Our results were more or less what we expected. Increasing the enzyme concentration decreased the time that the disc took to rise to the top of the hydrogen peroxide. In our procedure we quadrupled the the enzyme concentration, which decreased the time the disc took to rise to the top by 64% (from the average). Because of the outcome, we can say that our hypothesis was correct.

The making of the cuvettes (“tube#1,2,and 3) caused most of the data errors, so having premade and measured cuvettes would lead to accurate readings of the reactions. It is important to know which factors affect the reactions of enzymes in our bodies. The cellular reactions that are required to keep the organism functioning wouldn’t work fast enough to keep the organism functioning without enzymes. Also because enzymes allow our bodies to conduct chemical reactions at a faster rate than usual, it processes proteins into amino acids much quicker, which helps in digestion for example, the enzyme in our digestive system, pepsin. This could lead to further studies, which could include using a different type of enzyme, like pepsin, in this experiment since each enzyme reacts differently with their

In our lab, we checked the reaction rate of peroxidase and tried to find the

In this lab we attempted to find a relationship between pH and the productivity of the enzyme catalase. We used the method of testing called the ‘submarine’ method, and tested the velocity of the reaction in bubbles per 30 seconds. We measured this data by inserting 1 mL of H2O2, 1 mL of a vinegar and water solution that varies in pH, and 1 mL of H2O with 20 µL of liver puree into a narrow-mouthed piped base, dropped that into a flat bottomed test tube filled with 30 mL of distilled room temperature water, and then counted the number of bubbles that were produced. We found an exponential relationship between pH and enzyme velocity, as the pH increased the velocity first remained close to constant before dramatically increasing. This can be

The large problem in my experiment was that I should have put the hydrogen peroxide with my parsnips. In theory, it would have bubbled, therefore would have been a good measurement within the experiment. Forming a new hypothesis, if acidity is added to parsnips, through the use of pH, then enzyme activity will be affected because a difference in PH alters enzyme activity and the rate of reaction. The rate of reaction would have been measured using the peroxide as it bubbled because a substrate is needed. The best way to measure would be after every minute, for 10 minutes. For instance, after one minute of reaction time, the amount of bubbles would be measured and so on for the next 10 minutes of every pH level (2,3,4,5,8,9,10,11). When watching

This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.

The purpose of this lab report is to investigate the effect of substrate concentration on enzyme activity as tested with the enzyme catalase and the substrate hydrogen peroxide at several concentrations to produce oxygen. It was assumed that an increase in hydrogen peroxide concentration would decrease the amount of time the paper circle with the enzyme catalase present on it, sowing an increase in enzyme activity. Therefore it can be hypothesised that there would be an effect on catalase activity from the increase in hydrogen peroxide concentration measured in time for the paper circle to ride to the top of the solution.