As we study biomolecules, the subject of how do enzymes work comes up. The reasoning behind the catalase enzyme lab was to see how enzymes break down compounds. My objective being to see how the catalase enzyme will react to liver, potato and apple. We will also use a base or acid to see how these factors will affect the independent variable. My hypothesis is the liver and potato will react to the peroxide but the apple will not.
In order to complete this lab, you will need the following materials; six test tubes and a test tube holder, a ten-milliliter graduated cylinder, 40 milliliter of 3% hydrogen peroxide solution, scissors and tweezers, stirring rod, along with liver, apples and potatoes. First you will place a slice of liver in one
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The reaction of peroxide with liver creates oxygen. The reaction giving off heat. When it came to the potato and apple, the apple was the only one to contain more catalase. I think this because it had more of a reaction towards the peroxide. The optimum temperature for the catalase is cold. The base and neutral had a higher effect on the enzymes, which tells us acidity messes up the enzymes and it doesn’t produce a reaction. The catalase is the enzyme and the substrate is the peroxide. The peroxide helps the catalase break down into the oxygen. Catalase is reusable. Temperature can affect the reaction rate tremendously. If the temperature is too hot or cold, the enzyme shape cannot stay in place. If the pH levels are affected, the enzyme will become denatured and the enzyme shape will not stay in place. We had three different tests to run, a boiled liver test, a warm water test and a cold water test. With these factors, you can see how fast the reaction rate in the optimum temperature. We also tested out the pH level by using acetic acids, a bicarbonate solution and distilled water in order to see how it would affect the liver. Basically, unless the temperature or pH level were manipulated the liver would fizzle up because of the peroxide. The temperature or pH level manipulation will change the enzyme shape, creating a reaction or no
The hypothesis was that if we investigated samples from different kingdoms, then the rate of reaction run by enzymes would change, and enzymes in animal cells would run reactions at the fastest rate, while enzymes in plant cells would run reactions at the slowest rate. The independent variable for this experiment was the samples of different kingdoms; the dependent variable was the rate of reaction run by the enzyme. To prepare a 500 ml sample, 21g of chicken liver was blended and mixed with water; and the sample of potato and the sample of an active yeast was made the same way. Then, a fermentation tube was marked from the top by centimeters and filled with hydrogen peroxide solution. Next, 1 ml of chicken liver blend was added into the tube by a pipet, and the time for 1 cm peroxide solution to be consumed was measured.
In this laboratory exercise, studies of enzyme catalase, which accelerates the breakdown of hydrogen peroxide into water and oxygen. The purpose was to isolate catalase from starch and measure the rate of activity under different conditions. The laboratory was also conducted in association with a second laboratory that measured the effects of an inhibitor on the enzymes.
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.
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.
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.
The purpose of this lab is to test for enzyme activity by examining factors that may influence enzymes.
reaction rate increases. If the temperature of an enzyme gets to high the reaction rate will slow
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.
Enzymes are high molecular weight molecules and are proteins in nature. Enzymes work as catalysts in biochemical reactions in living organisms. Enzyme Catecholase is found on in plants, animals as well as fungi and is responsible for the darkening of different fruits. In most cases enzymatic activities are influenced by a number of factors, among them is temperature, PH, enzyme concentration as well as substrate concentration (Silverthorn, 2004). In this experiment enzyme catecholase was used to investigate the effects of PH and enzyme concentration on it rate of reaction. A pH buffer was used to control the PH, potato juice was used as the substrate and water was used as a solvent.
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 chemical hydrogen peroxide(H₂O₂) is broken down by the enzyme catalase. Hydrogen peroxide is a byproduct formed in cellular reactions that, if not broken down, could inflict severe damage to the cell. Catalase is an enzyme that breaks down hydrogen peroxide in to water and oxygen. How efficient and strong the enzymes reaction to break down H₂O₂ determines largely on temperature and pH level. An enzyme only functions within a set pH and temperature range. Beyond that it becomes denatured, rendering it useless. The purpose of this lab is to determine at which temperature and pH level the enzyme catalase reacts best. Catalase in chicken and beef livers will be used to do the lab because enzymes still function after death as long as they are kept refrigerated at a low temperature.
To conduct your laboratory exercises, use the Laboratory Manual located under Course Content. Read the introduction and the directions for each exercise/experiment carefully before completing the exercises/experiments and answering the questions.
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.
The independent variable in this investigation is pH. Each individual enzyme has it’s own pH characteristic. This is because the hydrogen and ionic bonds between –NH2 and –COOH groups of the polypeptides that make up the enzyme, fix the exact arrangement of the active site of an enzyme. It is crucial to be aware of how even small changes in the