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Importance of enzymes in metabolism
Introduction on catalase
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Recommended: Importance of enzymes in metabolism
To investigate the amount of oxygen foam (cm) produced by the enzyme catalase when it breaks down hydrogen peroxide in the animal (liver, milk, honey) and plant cells(potato, purple cabbage) into oxygen and water
Motivation:
The reason I chose this topic was because I wanted to find out what enzymes are used for, to what extent they are used in our bodies and, how vast are their applications in food industries.
Enzymes have been used in research, mainly because of their ability to facilitate reactions without being changed themselves as well as their ability to speed up these reactions, which would otherwise take a much longer period of time to complete. And it is these two features that compel me to conduct further research into the applications of enzymes.
Their applications in the processing of foods are what interest me the most. Food enzymes are proteins that are used as catalysts in a variety of biochemical processes that are done to enhance the quality of different food products like milk and baked goods like bread. Enzymes have also been used in wine production, food packaging, processing of dairy products. For this is why I chose to investigate the amount of catalase found in animal products (liver, milk, honey) and plant products (potato, purple cabbage) by measuring the amount of oxygen foam produced (cm) when these products are exposed to hydrogen peroxide.
Catalase is found in every cell of every organism on earth, in humans it is used to breakdown hydrogen peroxide which is toxic to humans to useful elements to the body like water and molecular oxygen.
Concept Diagram
Literature review
Before one can even begin to understand catalase one must first understand what an enzyme is. Enzymes are biological...
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...l of distilled water, blend for 2 minutes on high speed until mixture is smooth with no lumps (measure the weight of the cabbage using the scale).
12. Label five test tubes; A, B, C, D, and E with the permanent marker.
13. Place 5ml of honey in test tube A using a syringe.
14. Place 5ml of milk in test tube B using a syringe.
15. Place 5ml of blended liver into test tube C using a measuring cylinder.
16. Place 5ml of blended purple cabbage in test tube D using a measuring cylinder.
17. Place 5g of potato in test tube E
18. Be sure to clean the syringe and measuring cylinder after every use to prevent cross contamination.
19. Place all five test tubes on the test tube rack.
20. In each test tube, place 5ml of pure hydrogen peroxide into each test-tube using the syringe.
21. Observe outcome.
22. Record results by measuring the amount of foam produced and tabulate.
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
Catecholase is an enzyme formed by catechol and oxygen used to interlock oxygen at relative settings, and it is present in plants and crustaceans (Sanyal et. al, 2014). For example, in most fruits and vegetables, the bruised or exposed area of the pant becomes brown due to the reaction of catechol becoming oxidized and oxygen becoming reduced by gaining hydrogen to form water, which then creates a chain that is is the structural backbone of dark melanoid pigments (Helms et al., 1998). However, not all fruits and plants darken at the same rate. This leads to question the enzymatic strength of catecholase and how nearby surroundings affect its activity. The catecholase enzyme has an optimal temperature of approximately 40°C (Helms et al., 1998). Anything above that level would denature the tertiary or primary structure of the protein and cause it to be inoperable. At low temperatures, enzymes have a slower catalyzing rate. Enzymes also function under optimal pH level or else they will also denature, so an average quantity of ions, not too high or low, present within a solution could determine the efficiency of an enzyme (Helms et al., 1998). Also, if more enzymes were added to the concentration, the solution would have a more active sites available for substrates and allow the reaction rate to increase if excess substrate is present (Helms et al., 1998). However, if more
The Effect of pH on the Activity of Catalase Planning Experimental Work Secondary Resources Catalase is a type of enzyme found in different types of foods such as potatoes, apples and livers. It speeds up the disintegration of hydrogen peroxide into water because of the molecule of hydrogen peroxide (H2O2) but it remains unchanged at the end of the reaction.
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
Background information:. Enzyme Enzymes are protein molecules that act as the biological catalysts. A Catalyst is a molecule which can speed up chemical reactions but remains unchanged at the end of the reaction. Enzymes catalyze most of the metabolic reactions that take place within a living organism. They speed up the metabolic reactions by lowering the amount of energy.
Three flat-bottomed vials were obtained and labeled one through three. 3 mL of hydrogen peroxide was distributed to each of the vials. One drop of liquid soap was then added to each of the vials. The contents of the vials were gently swirled to ensure mixture of the hydrogen peroxide and soap. In each vial, a pH buffer was added; vial one received pH 2 buffer, vial two received pH 7 buffer, and vial three received pH 12 buffer. 1mL of catalase was then placed into each vial and the reaction was timed for 2 minutes. At the end of two minutes, the bubble column produced was measured and recorded into Table 3. The results were then graphed, as shown in Figure
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.
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.
Enzyme peroxidase is essential in any cell metabolic reaction as it breaks down the harmful hydrogen peroxide to harmful products in the body. The report analyzed its effect on changes in temperatures by determining the optimum temperatures and the effects of its reversibility. Through the method of extracting the enzyme by blending it with potato tissue in phosphate buffer, the effects were analyzed on the effect of the dye guaiacol and the activity measured under different temperatures. The optimum temperature was obtained at 22.20C and above this temperature, the enzyme was denatured. Conclusively, increase in temperature increases
Introduction / Background Information. This is an experiment to examine how the concentration of the substrate Hydrogen Peroxide (H2O2) affects the rate of reaction of the enzyme Catalase. In this experiment I will be using yeast as a source of catalase. Enzymes are catalysts which speed up specific reactions. Enzymes such as catalase are protein molecules, which speed up a specific reaction within the cell.
The Effect of Surface Area on the Rate of Reaction Between Catalase from a Potato and Hydrogen Peroxide
In our body, chemical reactions are happening constantly. Now, how are the chemical reactions in our body able to occur quickly, to massly create the needed materials such as energy, to support our every second need? Enzymes! Enzymes are proteins that speed up chemical reactions in our body. Our goal for this lab was to see if the change in pH level or temperature would affect the rate of enzyme activity. To do this experiment we had to first find a way to use enzymes. We had chose potato puree to act as our subject to experiment with, since it contained catalase, which is an enzyme. To actually see the rate of enzyme activity, we decided to mix the potato puree with hydrogen peroxide. The reason behind that was because catalase breaks down
The pH level was measured from all 10 tubes before the catalase solution was added to the tubes. When the catalase solution gets added to the tubes, the outcome of this solution is that bubbles are seen during this process. The bubbles are considered the oxygen production of the catalase solution. The bubbles were scaled depending on how strong the bubbles were seen. The tubes that had an oxygen production of 5 were numbered 5 through 10. Tubes 1 and 4 had no bubbles. The oxygen production of tubes 2 and 3 had a number of 1. The enzyme activity was compared to the pH level of tubes 4 through 8 to determine the activity bases on the liquids these tubes have (fig
The use of enzymes can be traced to ancient civilizations. Nearly 4000 enzymes are known today but still very few are in commercial use. Most of the industrial enzymes are of microbial origin. Total market sales of the enzymes was only a few millions till 1960 but then market has grown dramatically and demand for the enzymes is growing day by day(Wilke, 1999). Improved understanding of production biochemistry, fermentation processes, and recovery methods has resulted in the production of many enzymes in an affordable manner. Advances in methods of using enzymes have greatly increased demand. Furthermore, because of the many different transformations that enzymes can catalyze, the number of enzymes used in commerce continues to multiply.