Lab Report Catalase And 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.

In this experiment, the 5mM catechol (substrate) reacted with catechol oxidase in the presence of 5 different pH buffers mentioned above. This experiment was used to measure the buildup of the colored product, benzoquinone, to observe the change in the absorbance of the mixture in a spectrophotometer at a wavelength of 486 nm. Ithypothesized that since each enzyme has an optimal pH and that the enzymes are proteins, the enzyme activity will increase with pH level and will be at its highest at pH 7, which is water. As seen in figure 1, absorbance is low pH 2 because catechol oxidase activity was minimal at low pH concentration due to the catechol oxidase denaturing in the acidic solution. The catechol oxidases also denatured at high pH concentration such as pH 11, which is a basic solution, lowering catechol oxidase activity and absorption. Catechol oxidase activity was highest at pH 8 making it an optimal pH for catechol oxidase to catalyze the reaction and create more product which in turn increased the absorption of blue

H2O2 is commonly known as hydrogen peroxide and it is a strong oxidizer and a naturally produced compound in humans as a by-product of oxidative metabolism. Because of this, humans also produce the enzyme catalase peroxidases in order to convert small amounts of H2O2 into oxygen and water. It uses the following chemical formula:

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

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

If another enzyme like lactase is used, no reaction would take place because the substrate, hydrogen peroxide, wouldn’t fit into the active site.

The Effect of Different Concentrations of the Enzyme Catechol Oxidase on the Rate of Benzoquinone Production When Mixed with Pure Catechol

In order to see the effects of pH and temperature on the enzymatic reaction of catechol oxidase when separated from potato tissue. We used a spectrophotometer to measure how much blue light energy is absorbed by benzoquinone. Benzoquinone is a product of catechol when it has been oxidized by different temperatures and pHs. We hypothesized that the benzoquinone absorbance rate would be faster when the pH added to the cuvettes were greater than the pH of the potato tissue. The pH of the potato tissue was pH 6. Our results show that pH 7 had the faster absorbance rate, slightly slower at pH 4, and slowest at pH

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,

An Enzyme is a protein, which is capable of starting a chemical reaction, which involves the formation or breakage of chemical bonds. A substrate is the surface or material on or from which an organism lives, grows, or obtains its nourishment. In this case it is hydrogen peroxide. This lab report will be explaining the experiment held to understand the effects of the changes in the amount of substrate on the enzyme’s reaction.

Cells are the building blocks of life. Life itself would not be possible without cells and the actions they carry out. Hundreds of biological and chemical reactions take place in the cell every second. Most of the reactions in a cell use enzymes to speed up the reaction. An enzyme is a protein catalyst used by living organisms to increase the rate of biological reactions (Freeman et. al. 2016, p90). A catalyst brings substrates together in a precise orientation that makes reactions more likely. Enzymes have an “active site,” which is where the reactants bind to the enzyme. The active site is where catalysis occurs. The reactants of the enzyme are called the substrates. Enzymes are extremely effective at catalyzing reactions because

The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.

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).

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:

Hydrogen peroxide is a toxic byproduct of cellular functions. To maintain hydrogen peroxide levels the catalase enzyme deconstructs hydrogen peroxide and reconstructs the reactants into oxygen gas and water. The catalase enzyme is found inside cells of most plants and animals. Regulating the levels of hydrogen peroxide is crucial in homeostasis and analyzing it’s optimal conditions for performance is just as important. To understand the optimal environment for this enzyme, they are put into different environments based off protein activity (enzymes are proteins). Catalase samples will be put into different hydrogen peroxide environments based off pH and temperature. The more active the enzyme, the more oxygen and water it will produce. Enzyme activity can be seen through the release of oxygen in the hydrogen peroxide. Since oxygen cannot be accurately measured, the data will consist of the longevity of the reaction in different environments. If the pH is higher than 7, then the reaction rate will increase due to the ample amount of hydrogen ions in the hydrogen peroxide. However the pH level cannot be higher than 10 or else there will be too many hydrogen atoms in the peroxide for the enzyme to be able to deconstruct them. If the temperature is increased, then the reaction rate will increase due to the ample amount of energy and movement in the hydrogen peroxide and enzyme.