The purpose of this experiment is to measure the rate of catalase enzyme activity under different temperature conditions. The catalase enzyme is to be experimented on 4 different temperatures of 0oC,
23oC, 37oC, and 55oC, to determine which temperature has the fastest and slowest rate of enzyme activity, Introduction
All organisms are made of the basic unit of life called cells. From bacteria to fish to plants to humans, they are all supported by the cell theory. The cell theory “states that all living things are composed of cells and that all cells come from other cells” (Reece, 2012). For these cells to contribute to grow and function they must use the organelles and molecules accessible to them to maintain sustainability.
Organelles like ribosomes and cytoplasm help with the cellular activity. There are also complex molecules like nucleic acid and protein in which are important factors for organisms. These complex macromolecules of our cells are rich in potential energy. Although rich in energy, complex molecules do not spontaneously burst open. That reason being “there is an energy barrier that must be overcome before a chemical reaction can begin” (Reece, 2012).
Thus where enzymes come in and play an important role in breaking down these complex molecules or reactants. Enzymes speed up the cell’s chemical reaction by lowering energy barriers. “Energy must be absorbed to contort or weaken the bonds in reactant molecules so that they ca break and new bonds can form”
In this lab or experiment, the aim was to determine the following factors of enzymes: (1) the effects of enzymes concentration the catalytic rate or the rate of the reaction, (2) the effects of pH on a particular enzyme, an enzyme known and referred throughout this experiment as ALP (alkaline phosphate enzyme) and lastly (3) the effects of various temperatures on the reaction or catalytic rate. Throughout the experiment 8 separate cuvettes and tubes are mixed with various solutions (labeled as tables 1,3 & 4 in the apparatus/materials sections of the lab) and tested for the effects of the factors mentioned above (concentration, pH and temperature). The tubes labeled 1-4 are tested for pH with pH paper and by spectrophotometer, cuvettes 1a-4a was tested for concentration and cuvettes labeled 1b-4b was tested for temperature in four different atmospheric conditions (4ºC, 23ºC, 32ºC and 60ºC) to see how the enzyme solution was affected by the various conditions. After carrying out the procedures the results showed that the experiment followed the theory for the most part, which is that all the factors work best at its optimum level. So, the optimum pH that the enzymes reacted at was a pH of 7 (neutral), the optimum temperature that the reactions occurs with the enzymes is a temperature of 4ºC or
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 use of multiple test tubes and Parafilm was used for each experiment. Catechol, potato juice, pH 7 phosphate buffer, and stock potato extract 1:1 will be used to conduct the following experiments: temperature effect on enzyme activity, the effect of pH on enzyme action, the effect of enzyme concentration, and the effect of substrate concentration on enzyme activity. For the temperature effect on enzyme activity, three test tube were filled with three ml of pH 7 phosphate buffer and each test tube was labels 1.5 degrees Celsius, 20 °C, and 60 °C. The first test tube was placed in an ice-water bath, the second test tube was left at room temperature, and the third test tube was placed in approximately 60°C of warm water. After filling the test tubes with three ml of the
Students will be observing normal catalase reaction, the effect of temperature on enzyme activity, and the effect of pH on enzyme activity in this experiment. The enzymes will all around perform better when exposed in room temperature than when it is exposed to hot and cold temperatures. This is based on the fact that the higher the temperature, the better the enzymes will perform, but as the temperature reaches a certain high degree, the enzymes will start to denature, or lose their function.
Enzymes are biological catalysts, which speed up the rate of reaction without being used up during the reaction, which take place in living organisms. They do this by lowering the activation energy. The activation energy is the energy needed to start the reaction.
These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.
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,
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 purpose of this investigation is to discover the effect of pH on the activity of catalase, an enzyme which plays the integral role of converting hydrogen peroxide into water and oxygen, and discover which pH level it will work at the most efficient rate (the optimum). The original hypothesis states that that the optimum would be at a pH is 7, due to the liver, where catalase usually resides, being neutral. The experiment consists of introducing the catalase to hydrogen peroxide, after exposure to certain solutions; hydrogen peroxide, water and hydrochloric acids, all containing the adjusted pH, and measuring the height of froth formed, an observable representation of the activity of the enzyme. The final data indicated that
Proteins are a perfect example. The 3D structure and folding determine the use of the protein, such as the protein becoming an enzyme to fuel cellular respiration. However, before folding can occur, amino acids, which are the monomers of proteins, must be joined together through dehydration synthesis. In order for a protein to be used within an organism’s body, the polypeptide chain must first be built. Dehydration synthesis occurs by reacting the carboxyl group of one amino acid with an amine group in another amino acid. This can be pictured in Figure 1. The OH from the carboxyl group is removed, along with a Hydrogen from the amine functional group. This results in the byproduct of water, which is later used by the cell. The Carbon in the carboxyl group forms a bond with the Nitrogen in the amino group, which is called a peptide bond. The final product of this reaction is an H2O molecule, and the start of a polypeptide chain. The protein that was made through dehydration synthesis can now be used throughout the body for a variety of different processes. The protein made can be used for tissue and cell repair. A large portion of organs and bones are comprised of protein. Other ways that the protein are used is to be made into enzymes that control reactions in the body such as cellular respiration. The creation of a protein strand via dehydration synthesis is not exclusive to
A chemical reaction requires that bonds in the reactants be broken. The initial energy that must be absorbed in order to break the bonds of the reactant molecule is called the energy of activation. Enzymes work by lowering the energy of activation. For example,
The rate of decomposition due to catalase did not gradually increase at a constant rate because although the substrate concentration was increasing, it is unable to help increase the optimum activity of the enzyme. Although the number of substrate available for the enzyme is increasing,
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:
important role because every living organism needs proteins in order to speed up the biochemical