Catalase Enzyme Lab

Analysing the data, I decided to get the average height of the foam so I can juxtapose the data. The catalase with hydrogen peroxide and sodium hydroxide produced an average of 0.6 cm of foam. The catalase with sodium hydroxide produced an average of 0.4 of foam. The catalase with hydrogen peroxide and hydrochloric acid produced an average of 0.33 cm of foam. The catalase with hydrochloric acid produced an average of 0.3 cm of foam. The catalase with hydrogen peroxide and vinegar produced an average of 0.26 cm of foam. The catalase with vinegar produced an average of 0.03. Looking at the averages, the catalase that included sodium hydroxide produced the most foam. Sodium hydroxide is the only base out of the 3 solutions while the others were all acids. This means there’s the most enzyme when the pH is lower. Also, hydrogen peroxide is proven to make the catalase enzyme more active. When we first began the experiment, we only put hydrogen peroxide into the catalase and it produced the most foam. Additionally, if we compare the data set with the hydrogen peroxide and the data set without the hydrogen peroxide, the data set with the hydrogen peroxide had a significant greater amount of foam than the other data set. For example, the catalase with hydrogen peroxide and sodium hydroxide produced an

Problem/Info: Enzymes are large protein structures, also known as macromolecules and catalysts. They aid in the acceleration of chemical reactions by binding to another substance known as a substrate, converting it into different products that are more easily broken down called products. Only a small portion of the enzyme actually aids in catalyzing the substrate: the active site. When an enzyme is in specific conditions they tend to react quicker while in other, generally extreme, conditions the enzyme can be broken apart and rendered unusable, this is called denaturation. In the experiments conducted, an enzyme known as catalase, generally found in yeast, will be soaked onto a tiny paper circle and dropped into hydrogen peroxide H2O2. The catalase will break the hydrogen peroxide into oxygen and water. The oxygen inside of the paper will eventually be in a quantity that causes the paper to rise to the top of the hydrogen peroxide. The entire experiment is based off of observations of this piece of paper.

We know that enzymes are protein that helps to breakdown different molecules. But what if enzymes can be breakdown? Most enzymes need homeostasis environment to survive. Well we all know that as the amount of temperature increases the less the enzymes .Enzymes can be denatured using temperature, PH and salt concentration. As we know that protein structure are determined by DNA coding. We used temperature to see if increasing or decreasing temperature affected the amount of enzyme produced. So when the temperature is increased there will be more amount of enzymes denature due to high temperature and it would be opposite of temperature was dropped. And a denatured protein is biologically inactive hence it needs a homeostasis environment. Hydrogen peroxide is used for metabolic processes. The main purpose of this lab was to see that if increase in temperature resulted in denaturing of enzymes and comparing the time for h2o2 to bubble when using apples, onions and potatoes at room temperature. So the main questions for this lab were how does temperature affect the amount of enzyme present in potatoes? Will there be any change in amount of bubbles produced if apples and onions were used with potatoes at room temperature?

Proteins that are produced by living cells are known as enzymes. Enzymes are catalysts – they increase the rate of a chemical reaction by lowering the activation energy. The enzyme has an active site to which the substrate, or substance acted upon, binds, forming an enzyme-substrate complex. This active site, which is determined by the sequence of amino acids, is specific to which substrate it binds to, known as the lock-and-key theory. (This theory has been modified to the induced fit theory, which states that an enzyme will slightly change shape to accommodate a substrate.) The enzyme is not used up in the reaction; rather, it can be reused to keep converting substrate to products.

(Raven 53) There are several factors that affect the ability of the enzyme to catalyze a reaction. In this study, the effects of the substrate concentration, pH, and temperature will be examined. To test the effects of these environmental factors on enzymes catalase, a common enzyme found in the majority of all aerobic cells, will be examined. Catalase protects cells from the toxin hydrogen-peroxide, which is a byproduct of cell metabolism by catalyzing the decomposition of hydrogen peroxide into oxygen gas and water. The measure of oxygen gas and water under various conditions is an indicator of the effects environmental factors have on enzyme activity. (German

Aim: This experiment is conducted to find out whether different temperature (°C) can affect the reaction of breaking down hydrogen peroxide by an enzyme which then will be observed by measuring the time taken (in seconds) for the paper filler will reach the surface in the solution of cherry tomato juice and hydrogen peroxide. Background information: This experiment will examine how the variation of temperature can affect the chemical reaction of the enzyme Catalase with hydrogen peroxide. First of all, enzymes are proteins, which help a certain chemical process to take place. As chemical reactions always require a particular amount of energy to happen, this won’t be a concern with the presence of the enzyme. The enzyme will reduce the amount of energy needed for the chemical process that will take place.

As the pH level becomes increasingly further away from the ideal pH, the enzyme activity will diminish. This occurs as a result of a surplus in hydrogen ions, which will interfere with the hydrogen bonds of the enzyme, altering the active shape, inhibiting the binding of the specific substrate. For catalase, the pH level for optimal enzyme activity is about 7, as the peroxisome functions in the cytoplasm, which has a neutral pH. A temperature that progresses away from the ideal temperature of the enzyme will also result in a decrease in enzyme activity. As heat is applied to the enzyme, kinetic energy is derived, causing the hydrogen bonds of the enzyme to become unstable. As a result, the enzyme denatures, altering the shape of the active site, hindering the substrate ability to interact with the enzyme. Under lower temperatures, the movement of the enzyme and substrate are lowered, subsequently decreasing the enzyme activity as well. The temperature to optimize enzyme activity is 37℃, body temperature. In the case of potatoes, as used in this experiment, this optimal temperature will not vary by

The first tests that were conducted were the Catalase test and the Oxidase test. The Catalase and Oxidase tests can indicate that a bacterium can perform one of the following metabolic processes: the Krebs Cycle or the Electron Transport Chain.

In this experiment, the effect of various pH conditions on catalase enzyme activity was observed. For the enzyme-substrate complex of this experiment, hydrogen peroxide, H2O2, is the substrate and the enzyme is catalase, which is secreted by yeast. 3mL of a pH buffer, available in pH 4, 7 and 10, was added to an equal amount of 3% hydrogen peroxide, H2O2. Then, to each of these three solutions, three drops of yeast that has been activated with warm water was added to catalyze this reaction. As the yeast secretes more and more catalase, the rate of reaction increases considerably and hydrogen peroxide is broken down into water and oxygen gas (H2O2⟶ H2O+O2(g)). As this reaction occurs, the test tubes began to warm up since this is an exothermic reaction and bubbles started to form due to the formation of oxygen gas. The program Logger Pro and a gas pressure sensor were used to measure the production of oxygen gas as hydrogen peroxide is destroyed by the enzyme catalase at various enzyme concentrations.

The purpose of this experiment is to understand that enzyme at different conditions will react different such as temperature . By comparing the catalase at 0°c and boiled catalase . A 5 mL Catalase covered in ice was prepared prior to the experiment has to reach certain level of temperature . Hydrogen Peroxide and Water with 1% detergent were used in this experiment to analyze cold and boiled catalase reaction . The observation to measure the height of bubbles in each 3 paired of labeled test tubes after transferring the catalase boiled and cold one at time for 30 seconds . As noticed , without the presents of the catalase hydrogen peroxide and water (w 1% detergent ) did not able to produce as much as bubbles . Nor the boiled catalase transfers

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.

I knew that the catalase was working, because it was evident that it was speeding up the chemical reaction of the hydrogen peroxide. The decomposition reaction of hydrogen peroxide into products water and oxygen occured very quickly as soon as the enzyme for hydrogen peroxide (catalase) was added into the graduated cylinder with the hydrogen peroxide. As a result, an increasing amount of foam was being produced; a mixture of the products water and oxygen. Catalase speeds up chemical reactions by lowering the activation energy required to initiate the chemical reaction. Therefore, after adding catalase to the substrate that needed to be broken down into it’s products, the reaction’s activation energy was lowered, and it did not need as much

Enzymes are proteins created by cells within the body. They function as organic catalysts and work to speed up chemical reactions to a biologically specific rate. They are used to break down or build substances produced within the body. One toxic substance known as hydrogen peroxide is created in the body and needs to be broken down in time into water and oxygen before it becomes dangerous to health. If not broken down in time, it can reduce the amount of fibroblasts, cells that are necessary to repair damaged tissue or even cause death (“Hazardous Substance Fact Sheet"). A common enzyme found in calf liver, as well as nearly all other living organisms, known as catalase works to break it down, but it, like all other enzymes,

The purpose of this experiment was to study the effects of enzyme concentration on catalase activity.

The question being answered by these experiments is: How do different conditions affect the productivity of enzymes? Enzymes are produced by cells and they act as catalysts, which means they are organic molecules that speed up chemical reactions. How effectively they work depends on the conditions they are in, such as level of temperature, pH level, substrate concentration, and salt concentration. In these experiments, Catalase will be placed in different conditions with hydrogen peroxide. How active the enzyme is in these different conditions will be measured by the amount of oxygen gas being produced. A very high increase in oxygen will indicate a high reaction rate and a low production of oxygen will show that there is a low reaction rate. On the other hand, if there is no change in the level of oxygen, it will indicate that the Catalase is denatured and is no longer functioning.