Chemical reactions take place in all living organism. All Most all chemical reactions require an enzyme. These enzymes act as a catalyst to help regulate the rate of a chemical reaction. Three small lab experiments were performed to find the optimum pH, temperature, and concentration of the enzyme and substrate. The lab used the reaction of Catalase converting H2O2 into H2O and O2. The reaction was measured by the production of oxygen, using quaiacol that turns brown when oxidized. A spectrophotometer set to an absorbance of 500 nm was also used to measure the reaction rate. The procedure can be found in the biology 1 lab manual on pages, 243,244,245. After preparing the tubes following the instruction in the procedure section, two test
The rate of reaction between Catalase and the hydrogen peroxide (H2O2) can vary depending on many factors including the enzyme concentration in a solution. In this investigation, the rate of reaction will be measured by the change in temperature of the liquefied spinach (catalase) over a period of 30 seconds, once the hydrogen peroxide (H2O2) has been added into the solution.
Hydrate the yeast packets in a beaker with 400 mL of distilled water at a 10% concentration. In a 50 mL
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.
Living cells within our bodies perform an abundance of chemical reactions very speedily because of the participation of enzymes. Enzymes are biological catalysts that speed up a chemical reaction without being depleted or altered in the reaction (Garrette & Grisham, 1999). The
Objective: Measure the rate of decomposition of hydrogen peroxide with and without the addition of an enzyme catalase at different time intervals.
This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.
The role of an enzyme is to catalyse reactions within a cell. The enzyme present in a potato (Solanum Tuberosum) is catechol oxidase. In this experiment, the enzyme activity was tested under different temperature and pH conditions. The objective of this experiment was to determine the ideal conditions under which catechol oxidase catalyses reactions. In order to do this, catechol was catalyzed by catechol oxidase into benzoquinone at diverse temperatures and pH values. The enzyme was exposed to its new environment for 5 minutes before the absorbance of the catechol oxidase was measured at 420 nm using a spectrophotometer. The use of a spectrophotometer was crucial for the collection of data in this experiment. When exposed to hot and cold temperatures, some enzymes were found to denature causing the activity to decrease. Similarly, when the pH was too high or low, then the catechol oxidase enzyme experienced a significant decrease in activity. It can be concluded after completing this experiment that the optimal pH for catechol oxidase is 7 and that the prime temperature is 20º C. Due to the fact that the catechol oxidase was only tested under several different temperatures and pH values, it is always possible to get a more precise result by decreasing the increments between the test values. However, our experiment was able to produce accurate results as to the
Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.
As seen on table 1, the hypothesis in the introduction of this lab has been supported by the procedures. As the temperature varied from catalases optimal of 37° C, the reaction rate of catalase decreased. 37°C had the highest reaction rate of the three, at 3, while 4°C had the middle rate of reaction at 2.5, and 100° C had the lowest reaction rate of 0.5.
The overall purpose of the lab was to study an enzyme found in the liver called catalase and how its rate of reaction was dependent on the specific conditions surrounding it. The research question provided for this lab was: “How do pH, temperature and surface area affect the action of catalase?”
A rate is a measure of change that occurs in a given time whilst a
This investigation will be carried out to investigate the rate of reaction of the enzyme catalase on the substrate hydrogen peroxide.
The purpose of this experiment was to record catalase enzyme activity with different temperatures and substrate concentrations. It was hypothesized that, until all active sites were bound, as the substrate concentration increased, the reaction rate would increase. The first experiment consisted of five different substrate concentrations, 0.8%, 0.4%, 0.2%, 0.1%, and 0% H2O2. The second experiment was completed using 0.8% substrate concentration and four different temperatures of enzymes ranging from cold to boiled. It was hypothesized that as the temperature increased, the reaction rate would increase. This would occur until the enzyme was denatured. The results from the two experiments show that the more substrate concentration,
A catalase is a molecule that speeds “up the rate of a reaction without themselves being used up or permanently altered” (Audesirk & Byers 2008). They do this by lowering the activation energy required for the reaction to begin. This allows a higher proportion of molecules to move fast enough to react when the molecules collide. Enzymes are biological catalysts. They are proteins that promote specific chemical reactions. In this lab experiment, the chemical equation is: 2H2O2 2H20 + O2. Catalase, an enzyme that destroys hydrogen peroxide (H2O2), is used here to facilitate the chemical reaction from the substrate (2H2O2) to the product (2H20 + O2). This demonstrates how catalase operates in our body to destroy harmful toxins. However, the reaction
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.