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Effect of enzyme concentration on catalase activity
Effect of enzyme concentration on catalase activity
Investigation 2: the effect of enzyme concentration on catalase activity
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Recommended: Effect of enzyme concentration on catalase activity
The activity of an enzyme might be influenced by several factors such as temperature and pH. Each enzyme usually has a given optimal pH needed for its functioning. Within that particular pH value, the enzyme can perform a chemical reaction at the highest possible rate. An increase or decrease in pH from the optimal value usually result in decrease in the enzyme’s activity (Harkness & Cockburn, 2012).
Objective
The lab experiment aimed at investigating the effect of acid or pH on the activity of a catalase enzyme. Catalase enzyme is an enzyme that usually allow its cell to get rid of excessive hydrogen peroxide by splitting hydrogen peroxide into water molecule and oxygen.
Materials required
Fresh meat (fish) which is an acidic food, Yeast, H2O2, fresh vegetable (potato) which is an alkaline food, Dropper, and Scaled Beaker.
Hypothesis testing
Provided catalase enzyme is present within peroxisomes, the optimal pH of the enzyme is supposed to be equal to the pH value of the solution within the peroxisomes. Peroxisomes usually have a pH value that ranges between 6.9 and 7.1 (Rai, 2007). Therefore, the hypothesis for the experiment was that the highest possible rate of enzyme activity that would be observed within neutral pH values, with the pH values being lower that 7.0 would result in a decrease in reaction rate catalyzed by the enzyme
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Due to the catalase enzyme that was present in the yeast, oxygen gas was emitted from the hydrogen peroxide in form of bubbles. Through measurement of the magnitude of bubbles, the actions of the enzyme on food items could be easily observed. First, 1cm3 of fresh meat was placed in a 100ml cylinder before adding 2cm3 of yeast into the graduated
The purpose of this study is to analyze the activity of the enzyme, catalase, through our understanding
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
The alternate hypothesis is that there exists an optimal pH level for catecholase enzyme in which the catecholase enzyme can operate with the highest possible
The shape of the molecules is changing and so the enzyme molecules can no longer fit into the gaps in the substrate that they need to and therefore the enzymes have de – natured and can no longer function as they are supposed to and cannot do their job correctly. Changing the temperature: Five different temperatures could be investigated. Water baths were used to maintain a constant temperature. Water baths were set up at 40 degrees, 60 degrees and 80 degrees (Celsius). Room temperature investigations were also carried out (20 degrees).
The reaction for pH 5 went off scale at one hundred seconds; its reaction went faster than the other tested pH levels. At twenty seconds, the pH 9 reaction reached 0.244 absorbance, slowly increased, and then slightly dropped to 0.296 by the end of the reaction (Figure 3). The rate of absorbance for peroxidase with pH 9 was 0.0097, so peroxidase activity is least optimal at pH 9. The absorbance rate for pH 3 was 0.0866, and the rate for pH 7 was 0.1426. Because the rate of absorbance for pH 5 was 0.3493, it is the optimum pH level for peroxidase. Highly acidic and alkaline pH levels reduce activity. (Figure
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.
EDTA, the chelating agent that binds with magnesium, had a high absorbency and strong color change to red. The correct cofactor was copper which with the chelating agent of PTU and citric acid which both bind strongly to copper which keeps it from binding with the enzyme. This was determined because in the trails, both PTU and citric acid had low absorbency and were clear or roughly clear in color. The catechol in each tube, which was the control for this experiment, allowed the cofactor that would be used in this reaction to be singled out. The way each chelating agent would affect the different cofactors displayed which was not needed for the reaction and which cofactors were needed for the reaction. An inconsistency that may have affected the data would be if the calibration tube malfunctioned in balancing the spectrophotometer to zero. There also could be errors if the calibration tube wasn’t used before each tube was tested in the spectrophotometer. The relationship of the cofactor and amount of enzyme activity would be that if the cofactor is inhibited or not, the enzyme activity would be higher if the cofactor is not inhibited but lower if it was inhibited by the chelating
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.
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.
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
From looking at the results I can conclude that when the pH was 3 and 5. No oxygen was produced, therefore no reactions were taking place. This was because the pH had a high hydrogen ion content, which caused the breaking of the ionic bonds that hold the tertiary structure of the enzyme in place of the syringe. The enzyme lost its functional shape.