Results
Enzyme activity experiment for this lab shows that in the decomposition of hydrogen peroxide with the enzyme catalase, the whole banana reaction produced 6.8 mL of oxygen while the diced banana produced 8.0 mL of oxygen gas (see table 1.0). The increase in the amount of oxygen produced when the diced banana reacted was because of the increase in the surface area of the diced banana which increased the rate of catalyzing the reaction with the hydrogen peroxide. The second experiment was on the effect of temperature on the liver. The result of the experiment proved the hypothesis that 37 ºC water bath would have the highest temperature since the optimum PH for catalase is 7 and the temperature is 37 ºC. The boiled enzyme had the lowest
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The last experiment was conducted to determine the effect of PH on the enzyme activity. The experiment corresponded with the hypothesis that at PH 7 the reaction would be faster. The reaction rate of PH 3 was extremely slow because the PH range is not close to the optimum PH of 7 and PH 10 was very high that it denatured the enzymes. That proves that extreme high and low PH levels would induce a low enzyme activity because the hydrogen bonds have been destroyed. (see table 4.0)
Discussion
The results that was obtained from the various experiments supported our hypothesis. In experiment 1 the whole banana was dropped into the test tube containing the solution of 3% hydrogen peroxide(H2O2). The whole banana reacted with the solution of hydrogen peroxide to form white fumes at the top of the test tube. The level of water was going down slowly while bubbles of water was going up slowly as well. When the diced banana was dropped in the test tube, the level of water was going down vigorously, and bubbles of water was rising vigorously as well. The observation behind this experiment was that the experiment is
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Based on the experiments conducted, I learned that enzymes are greatly needed as a catalyst to bring about a specific biochemical reaction. Enzymes speed up the rate of chemical reaction by lowering the activation energy. From my observations, I learned that most enzymes require a specific environmental condition for them to function effectively. Diced banana increased in the amount of oxygen it produced because of the increase in the surface area. Also, when the liver was exposed to hydrogen peroxide to determine the effect of temperature, PH and its reusability, the observations deduced was that enzymes work best at a specific pH which is known as the optimal pH and perform at their best in a small range of temperature. Finally, I learned that enzymes are not changed by the reactions the catalyze and hence the are not denatured or altered during a chemical
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
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
However, at 3% substrate concentration, the hydrogen peroxide decomposition showed an immediate peak of up to 3.8 mm in height. As the substrate concentration slowly increased, enzyme
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.
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.
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.
How the Concentration of the Substrate Affects the Reaction in the Catalase Inside Potato Cells Introduction Enzymes are made of proteins and they speed up reactions, this means that they act as catalysts. Hydrogen peroxide is a byproduct of our cell's activities and is very toxic. The enzymes in our bodies break down the hydrogen peroxide at certain temperatures they work best at body temperature, which is approximately 37 degrees. At high temperatures, the cells begin to denature. This means that the hydrogen peroxide is prevented from being broken down because they will not 'fit' into the enzyme.[IMAGE] Objective I am going to find out how the concentration of the substrate, hydrogen peroxide affects the reaction in the catalase inside the potato cells.
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
The Effect of Surface Area on the Rate of Reaction Between Catalase from a Potato and Hydrogen Peroxide
Discussion: Enzymes (catalase) are found in every living organism, helping to speed up chemical reactions. Enzymes function is to break down molecules into smaller substances. In our experiment we are seeing if the enzyme is able to break down the molecules. We are using hydrogen peroxide as the substrate, this is a substrate of hydrogen and oxygen atoms. as the hydrogen comes into contact with the enzyme (potato disks) the enzyme then breaks down the hydrogen peroxide substance into 2 smaller molecules.
Enzymes are catalysts which lower the activation energy of chemical reactions, thus making them occur more rapidly. Enzymes are in constant use because of their ability to increase the rate of the reaction without permanent alteration. Each enzyme has a different rate of reaction as well as a maximum speed; you can find this number by adding substrate into the concentration until the speed remains constant. The maximum velocity divided by two gives you the Km. In this experiment the efficacy of the enzyme peroxidase was tested.