Substrate Concentration Lab Report

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 topic of this lab is on biochemistry.This experiment was conducted to show how cells prevent the build of hydrogen peroxide in tissues. My group consisted of Lekha, Ruth, and Jason. There were used two different concentrations of hydrogen peroxide through this experiment , 1.5% and 3%. By testing two different types it is easier to understand how the H2O2 and catalase react with one another. To do this both the yeast, which was our catalase, and H2O2 were mixed together in a beaker. Each concentration was tested out twice for more accurate results . 1.5% concentrated H2O2 had an average reaction rate of 10.5 seconds while 3% concentrated H2O2 had an average reaction rate of 7.5 seconds. From this experiment we learned that by increasing the concentration of H2O2 and chemically combining it with a catalase it will speed up the reaction. Enzymes speed up chemical reactions . The independent variable in this experiment was the concentration of the H2O2. Some key vocabulary words are Catalase, enzyme, hydrogen peroxide ( H2O2), and concentration.

Temperature controls the speed the enzymes work at. Higher temperatures increase the kinetic energy which increases the chance of collision therefore speeding up the rate of

If different amounts of enzyme solution are added to the hydrogen peroxide, then the highest amount of enzymes will have the greatest reaction rate because enzymes catalyze reactions, meaning more oxygen will be produced quicker.

The result that we receive from the lab showed that as there are more ions in the water that was mix with the catalyses, there is less enzyme activity. Our hypothesis was that if we used ionize water for the experiment, then there will be more oxygen. To conduct the experiment, we added catalyze and peroxide in a test tube then put a stopper on it which is connected to a thin plastic tube. The thin plastic tube was put in a cylinder full of water that would be flipped upside down in a large beaker full with water. We would let it run for two minutes and record how much oxygen was obtained.

Hydrogen Peroxide, or H2O2, is harmful to most living organisms but can be converted to oxygen and water before the damage is permanent. This is thanks to enzymes, the biological catalysts that increase the rate of reactions. Enzymes can be studied by measuring the rates of enzyme-catalyzed reactions. This can be done in a number of ways, including measuring the pressure of the product as it appears, measuring the rate of disappearance of the substrate, and measuring the rate of appearance of a product.

It is predicted that enzyme activity will speed up from 0 to 37 degrees and then rapidly slow down or stop altogether at 55 degrees. Methods For this experiment the dependent variable will be the amount of product, oxygen, produced by the enzyme catalase breaking down hydrogen peroxide. The independent variable will be temperature. Four temperatures will be tested on the enzyme to see how much product will be produced. Controlled variables will be the amount of enzyme, hydrogen peroxide and water used in the test tubes, as well as the volume of the nalgene bottle (250 mL) used in testing to measure the product.

Introduction The purpose of this lab was to test the rate at which the catalyst enzyme reacts and how temperature affects it. Enzymes help to speed up reactions within objects by providing an alternative low energy route for the reaction to occur. In order for a reaction to occur two molecules must collide with each other. The substrate, molecule colliding with the enzyme then locks into it, allowing the enzyme to begin breaking it down.

Enzymes are biological catalysts that speed up the rates of reactions by lowering the activation energy necessary for the reactions to occur. Enzymes accomplish this through finding a lower energy pathway for the reaction to take place. The specific enzyme used in this experiment was amylase. It functions by breaking down starch into maltose. The overall question posed in this experiment was whether or not an increase in temperature would result in a significant change in enzyme activity, more specifically whether a 20° C increase from 4°C to 24°C would result in a significant change in enzymatic activity. The biological hypothesis was temperature has an effect on the rate amylase digests starch. The null hypothesis was there is no

If there is more heat involves in a reaction it will occur at a faster speed as the heat provides the particles with more energy. Likewise, if the temperature at which the reaction is occurring is low it will slow down the reaction. The experiment is being done at room temperature because then temperature does not play a great role in the reaction, and therefore the reaction is happening based solely on the acids, and metal. Something else that is required for a chemical reaction to occur is the Collision theory.

If the temperature of the catalase is increased, then enzyme activity will rapidly increase as well, because an increase in temperature increases the kinetic energy of the molecules, thus increasing the frequency of the collisions, and speeding up the rate of chemical reaction.

We used this information to form our hypothesis, which was that the 100% concentration test would have the highest reaction rate because the more enzyme is the more active sites there are, so more reactions can occur, and the the Hydrogen peroxide will be decomposed faster, giving it a higher rate. However, the results of our experiment did not support this. Like explained before, the test that resulted in the highest rate was the one with 50% concentration. It is unknown why this occurred. The sources provided in class, a graph, showed that there should be linear growth between concentration and rate, which supports our hypothesis. Fig. 2 shows that the reaction rate plateaus towards the end of the 50 seconds, but this is because of the limited and constant amount of substrate, so it slowed down when the Hydrogen peroxide ran out. Our data did not support our hypothesis, but the class source support our

Enzymes are proteins that serve as biological catalysts in a wide variety of life sustaining chemical reactions that take place in cells. A catalyst affects the rate of chemical reactions, by lowering the activation energy required to make the reaction occur. In an enzyme-catalyzed reaction, a substrate is a molecule that temporarily binds with the enzyme at an area on the enzyme called the active site. Each enzyme catalyzes only one specific reaction because there is only one type of substrate molecule that fits perfectly in an enzyme’s active site. The substrate temporarily joins with the enzyme to form an enzyme substrate complex. The substrate is then converted to its products and the enzyme is released. The process is then repeated with another substrate molecule. Different conditions may change the how the enzyme catalyzes, either making it slower, faster, or not catalyzing at all. The purpose of the enzyme lab is to measure the enzyme rate in different conditions, the pressure of the enzymes, and how much hydrogen peroxide is used in a chemical reaction.

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.