Lab Report Catalase Hydrogen Peroxide

The preparation for the experiment started by gathering the solutions of enzyme Peroxidase, substrate hydrogen peroxide, the indicator guaiacol and distilled water. Two small spectrometer tubes and three large test tubes with numbered labels. In addition, one test tube rack, one pipet pump and a box of kimwipes were also gathered. Before the experiment, the spectrometer must be set up to use by flipping the power switch to on. Following, the machine was warmed up for 10 minutes and the filter lever was moved to the left. In addition, I set the wavelength to 500 nm with the wavelength control knob. Before the experiment, I had to create the blank solution by pipetting 0.1 ml of guaiacol, 1.0 ml of turnip extract and 8.9 ml water into tube #1. Following the creation of the blank, a control 2% solution was created.

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 human body is an incredible system that is capable of working a multitude of diverse functions. Without the help of the many different protein molecules, the human body would not be able to function properly. One major group of proteins called enzymes are mandatory for essential life. These proteins are constantly at work assembling molecules, metabolizing energy, and fighting off infections. An enzyme is a macromolecule that acts as a catalyst that speeds up a chemical reaction without being consumed by the reaction. Without these proteins, these reactions would take place too slowly to keep us alive. Essential parts in your body like vitamins and minerals cannot do any work without

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 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,

The name of the enzyme used in this lab is called peroxidase. “In plants the enzyme is called peroxidase. A related enzyme named catalase performs the same function in animals” (Pearce, 2017). These enzymes breakdown hydrogen peroxide (which is a by – product of metabolism).

pH along with temperature and concentration is a limiting factor of enzyme activity. Enzymes, which are proteins, have a distinct pH range in which they work most effectively. Beyond or below this specific pH, enzyme activity begins to diminish and eventually the enzyme is rendered useless. The optimum pH of an enzyme is the pH at which it is most effective and causes the fastest rate of reaction(source). This decrease in enzyme activity beyond the optimum pH is attributed to the change in shape of the active site(explained earlier) of the enzyme. This change in shape can be brought upon when the surrounding pH moves away from the optimum pH, and it can prevent the enzyme from binding with the substrate.

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?”

The experiment gave us an insight of how pH affects catalase activity. We hypothesized that the enzyme activity will be quicker near neutral pH levels, than in acidic or basic solutions. The expectation was the optimum rate of enzyme would be at near or at neutral solution, while the rate would be really slow in acidic or basic solutions, such as in solutions of HCl and NaOH. Our experimentation ran into some errors because we used tap water which didn’t have a neutral pH of 7; instead it was 5, which is considered to be acidic. So, our experiment included pH’s of 0, 5, and 13.

Certain bacteria contain proteins that can reduce oxygen, producing hydrogen peroxide, or superoxide as a result. Obligate aerobes and facultative anaerobes contain the enzyme superoxide dismutase, and either catalase or peroxidase. Most strict anaerobes, however, lack these enzymes and therefore O2 products are toxic to them. Superoxide dismutase destroys superoxide. Both catalase and peroxidase destroys hydrogen peroxide.

The biggest problem my group experienced was that as we moved into our second round of trails, we noticed consistently higher reaction times for the same concentration of enzyme. There are two possible explanations for this. The first is that we continued to use the same container of hydrogen peroxide every trail. The peroxide may have become diluted, reducing the rate at which the reaction could happen. This became apparent when we got to the lowest concentration trails. We were reasonably sure that these would both take a long time, so we did both trails simultaneously in two different containers: one old, one new. The trail conducted in the container of fresh peroxide finished in just over six minutes, however the trail conducted in the used

In the catalase experiment, the enzyme will act as a catalase that speed up the chemical reaction, in this case the yeast; moreover, the substrate is the hydrogen peroxide. The product of the enzyme-substrate complex is H2O and O2. The rate of oxygen that is being produced is caused by either increasing the amount of product or decreasing the amount of reactants. Factors that affect the results are the temperature, which will change the environment of the enzyme to cause the enzyme to either denature or increase the reaction rate.

Within a cell, enzymes are used as a catalyst to increase the rate of chemical reaction. They do not consume themselves, rather they help in increasing the rate of reaction. Within the body, enzymes vary depending on their specific functions. For instance, hydrogen peroxide is a toxic chemical, but it breaks down into harmless oxygen and water. This reaction can be sped up using the enzyme catalyst produced by yeast. Hydrogen peroxide is produced as a byproduct in cellular reaction, because it is poisonous and must be broken down, therefore this reaction is important. The speeding up of the reaction is shown below:

It was hypothesised that, if the Catalase is heated up to 37°C then it will produce oxygen faster that when it is at 23°C or 5°C because 37°C is the optimal temperature for Catalase. This was hypothesized because Catalase is a type of protein and when exposed to unfavorable temperatures, Proteins slow down or denature. It was hypothesised that, if the Catalase is heated up to 37°C then it will produce Oxygen faster that when it is at 23°C or 5°C because 37°C is the optimal temperature for Catalase. The hypothesis is supported by the data because the overall rate of reaction for 37°C is 3.0%, for 23°C its 2.4%, and for 5°C

Enzymes catalyze biological systems by speeding up the chemical reactions included. Enzymes developed from the peroxidase that is obtained from the different roots reacts with the hydrogen peroxide, which releases H2 and water. The extra hydrogen is indicated by the color change of the solution that is used to measure the rate of enzyme activity. When the rate of enzyme activity was high, the activity always occurred in the roots in the beginning stages of their development. However, when the rate of enzyme activity was low during the roots’ development, sucrose was present. Sucrose was not present in roots when the tissues consisted of high activities of acid invertase.