Effect of temperature on the enzyme and the amount of foam produced
Introduction
The enzyme used in this investigation was catalase, catalase is a type of protein called enzyme and the function of an enzyme is to catalyse(speed up) biochemical reaction. Catalysts such as enzymes are important in biochemical reaction, without them the reaction would occur too slow for an organism to survive. Catalase is present in most organisms which are in contact with oxygen, as it protects the organism from damage due to peroxide formed in the body from several metabolic processes. Catalase acts by speeds up the decomposition reaction of hydrogen peroxide to water. (Encyclopedia Britannica, 2017) Since liver plays a major key role in metabolism and hydrogen
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As oxygen is a gas and invisible to the naked eye, detergent was added to hydrogen peroxide and during the decomposition reaction when oxygen is produced, it would produce foam due to the detergent.
Picture 1. The picture shows how catalase breaks down hydrogen peroxide into 2 products oxygen and water. https://www.youtube.com/watch?v=BbYsp1kXuzw
The aim of the experiment was to investigate the effect of the increasing temperature on the activity of catalase in the dissociation of hydrogen peroxide. It was hypothesised that the highest rate of production of oxygen would be around 30℃, 30℃ since its found in the human body and the average temperature of the human body is 37℃.
The effect of the temperature on catalase is the independent variable and the result of it, the rate of production of foam was the dependent variable as it relied on the optimal temperature of catalase to produce the highest level of foam. The highest level of foam would represent the most oxygen produced signifying high rate of
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The marking of the foam height after 5 seconds was a challenge as human reflexes are not that quick.
The results were not reliability and this can be seen from the high standard deviation and the practical is not valid as there were too many error and the results were too imprecise. The low validity of the practical alludes to the improvements needed in the procedure of the investigation.
An improvement could be to add detergent separately so it doesn’t interfere with the measuring of the hydrogen peroxide. Recording the reaction and then using that to calculating the height of the foam formed in the 5 second timeframe would be a more accurate way of measuring. Using 2 thermometers throughout the practical and if there is an error then that error is consistent which will increase the accuracy even if the precision is affected. An electronic bath that maintains a certain temperature would increase the precision of the
In the lab, Inhibiting the Action of Catechol Oxidase we had to investigate what type of enzyme inhibition occurs when an inhibitor is added. Catechol oxidase is an enzyme in plants that creates benzoquinone.Benzoquinone is a substance that is toxic to bacteria. It is brown and is the reason fruit turns brown. Now, there are two types of inhibitors, the competitive inhibitor and non-competitive inhibitor. For an enzyme reaction to occur a substrate has to bind or fit into the active site of the enzyme. In competitive inhibition there is a substrate and an inhibitor present, both compete to bind to the active site. If the competitive inhibitor binds to the active site it stops the reaction. A noncompetitive inhibitor binds to another region
Acting as the controlled group to lessen the effects of all variables except the independent variable, at 0% concentration, the height of foam produced is 0 mm. Attributions to these results is because at 0% substrate concentration, no molecules were present to occupy all the available active sites. As an outcome, the final volume of oxygen is none since there were no collisions taken place between the enzymes and substrate. Therefore, prevented the number of collisions to reach the activation energy.
The purpose of this study is to analyze the activity of the enzyme, catalase, through our understanding
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
The null hypothesis is that there is not an optimal pH that will alter the enzymatic activity of catecholase.
The Effect of Temperature on the Activity of the Enzyme Catalase Introduction: The catalase is added to hydrogen peroxide (H²0²), a vigorous reaction occurs and oxygen gas is evolved. This experiment investigates the effect of temperature on the rate at which the enzyme works by measuring the amount of oxygen evolved over a period of time. The experiment was carried out varying the temperature and recording the results. It was then repeated but we removed the catalase (potato) and added Lead Nitrate in its place, we again tested this experiment at two different temperatures and recorded the results. Once all the experiments were calculated, comparisons against two other groups were recorded.
Investigating the Effect of Substrate Concentration on Catalase Reaction. Planning -Aim : The aim of the experiment is to examine how the concentration of the substrate (Hydrogen Peroxide, H2O2) affects the rate of reaction. the enzyme (catalase).
Investigating Factors that Affect the Rate of Catalase Action Investigation into the factors which affect the rate of catalase action. Planning Aim: To investigate the affect of concentration of the enzyme catalase on the decomposition reaction of hydrogen peroxide. The enzyme: Catalase is an enzyme found within the cells of many different plants and animals. In this case, it is found in celery.
Out of these variables I will use concentration as my input variable and amount of carbon dioxide released as my outcome variable. You can see how I will use and measure these variables in the method section of this investigation. My preliminary results can be found in appendix 1. These show what measurements of the input variables I decided to use and why I decided this.
Materials used in the experiment included 5-7 g of the potato tissue, 50ml of 2.0M phosphate buffer coffee filter and guaiacol dye.
The results of this experiment showed a specific pattern. As the temperature increased, the absorbance recorded by the spectrophotometer increased indicating that the activity of peroxidase enzyme has increased.At 4C the absorbance was low indicating a low peroxidase activity or reaction rate. At 23C the absorbance increased indicating an increase in peroxidase activity. At 32C the absorbance reached its maximum indicating that peroxidase activity reached its highest value and so 32 C could be considered as the optimum temperature of peroxidase enzyme. Yet as the temperature increased up to 60C, the absorbance decreased greatly indicating that peroxidase activity has decreased. This happened because at low temperature such as 4 C the kinetic energy of both enzyme and substrate molecules was low so they moved very slowly, collided less frequently and formed less enzyme-substrate complexes and so little or no products. Yet, at 23 C, as the temperature increased, enzyme and substrate molecules
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
The first experiments investigate the order of reaction with respect to the reactants; hydrogen peroxide, potassium iodide and sulphuric acid by varying the concentrations and plotting them against 1/time. An initial rate technique is used in this experiment so ‘the rate of reaction is inversely proportional to time.’ To find the order of reaction in respect to the reactants, 1/time is plotted against the concentration of Hydrogen Peroxide using the equation:
I shall be measuring how much gas is given off. This will be done by measuring the amount of froth on the surface of the liquid. The oxygen released is collected in the form of these bubbles. The equation for the reaction is: (catalase) [IMAGE] H2O2 2H2O + O2 (hydrogen peroxide) (2 part water) (oxygen) I will change the concentration of H2O2 and O2 (making sure the volume stay the same, when one part of a H2O2 particle is taken, an O2 particle is added. Prediction
The enzyme sped up the reaction of H2O2 and that allowed the H2O to remain while the O2 was released as bubbles. After the enzyme was used, it stayed on top of the remaining H2O in a form of black powder. To confirm this evidence, weigh an amount of MnO2 and H2O2 by themselves. After that, drop the MnO2 into a test tube with the H2O2.