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Effects of pH on enzyme activity
The activity of catalase
The activity of catalase
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The Effect of Varying Environmental Factors on Catalase Activity
I. Introduction
A. Background
Proteins are one of the main building blocks of the body. They are required for the structure, function, and regulation of the body’s tissues and organs. Even smaller units create proteins; these are called amino acids. There are twenty different types of amino acids, and all twenty are configured in many different chains and sequences, producing differing protein structures and functions. An enzyme is a specialized protein that participates in chemical reactions where they serve as catalysts to speed up said reactions, or reduce the energy of activation, noted as Ea (Mader & Windelspecht).
The way an enzyme decreases the energy needed is through
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Purpose
The purpose of this experiment was to determine the effects that varying temperatures, enzyme concentration, and pH had on catalase activity.
C. Hypothesis
In this experiment as a whole, there were three individual experiments conducted, each with an individualized hypothesis. For the effect of temperature on enzyme activity, catalase activity will be decreased when catalase is exposed to temperatures greater than or less approximately 23 degrees Celsius. For the effect of enzyme concentration on enzyme activity, a concentration of greater or less than approximately 50% enzymes, the less active catalase will be. Lastly, the more the pH buffer deviates from a basic pH of 7, the less active catalase will be.
II. Materials and Methods
A. Materials
• 11 flat bottomed
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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
After conducting this experiment and collecting the data I would have to say that the optimal temperature for enzyme activity would have to be room temperature which in my experiment was thirty-four degrees Celsius. I came to this answer because the glucose test strip showed that at room temperature there was more glucose concentration that at either of the other temperatures. Due to temperature extremes in the boiling water the enzymes could no longer function because the breakdown of lactose stopped. The cold water also hindered the breakdown of the lactose but as the water warmed the enzymes were more active which can be seen in the results for the cold water at 20 minutes B. Describe the relationship between pH and the enzymatic activity of lactase.
This indicated that the effect of high temperature on the activity of peroxidase was irreversible and so if the optimum temperature was restored the enzyme activity will not increase again because denaturation resulted in a permanent change in the shape of the active site of the peroxidase enzyme. In conclusion, the results of this experiment supported the hypothesis that enzymes including peroxidase enzyme are sensitive to temperature changes[George
The purpose of this study is to analyze the activity of the enzyme, catalase, through our understanding
In both solutions of catalase there is a steady increase in reaction relative to the hydrogen peroxide concentration as it increases. A significant jump is observed in the carrot catalase solution between .25% and .5% whereas the pinto bean catalase solution has a steady increase. Each solution doesn’t generate much more reaction to the next increment of hydrogen peroxide concentration, 1%. In general it stayed level. This continued to be a trend for the pinto bean catalase solution, plateauing through to the 6% concentration of hydrogen peroxide. This is known as the point of saturation.
The affects of pH, temperature, and salt concentration on the enzyme lactase were all expected to have an effect on enzymatic activity, compared to an untreated 25oC control. The reactions incubated at 37oC were hypothesized to increase the enzymatic activity, because it is normal human body temperature. This hypothesis was supported by the results. The reaction incubated to 60oC was expected to decrease the enzymatic activity, because it is much higher than normal body temperature, however this hypothesis was not supported. When incubated to 0oC, the reaction rate was hypothesized to decrease, and according to the results the hypothesis was supported. Both in low and high pH, the reaction rate was hypothesized to decrease, which was also supported by the results. Lastly, the reaction rate was hypothesized to decrease in a higher salt concentration, which was also supported by the results.
The alternate hypothesis is that there exists an optimal temperature for catecholase enzyme in which the catecholase enzyme can operate with the highest possible activity.
To determine the effects of two environmental factors, temperature and pH, on the enzyme peroxidase, a spectrophotometer was used to measure the absorbance of each reaction every twenty seconds for two minutes. The temperatures tested were 0°C, 23°C, 32°C, and 48°C; the pH levels tested were pH 3, pH 5, pH 7, and pH 9. The temperatures were kept constant by keeping the tubes at room temperature, or placing them in an ice bath, warmer, or a hot water bath. Peroxidase, hydrogen peroxide, guaiacol and a pH buffer were mixed together to produce a reaction for both the temperature and pH experiments.
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).
The three repeats of each experiment was found to be inadequate as it did not give a large enough range of results, in future experiments a larger variety of tissues should be used, a wider range of temperatures, aand at least five repeats should be carried out in order to obtain wider, more interesting and reliable results on catalase activity in plant tissue. The use of tissue kept at room temperature for the entire experiment was successful as it provided a clear comparison with the tissue that had been boiled or frozen. During the investigation, the same pieces of equipment ie the centrifuge and scale were used for every measurement to ensure that there was no variation in results due to technical
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.
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
...remain the same at 4ºC and 25ºC. The final result of this experiment was that glucose was more present in environments of higher temperatures. Our hypothesis and predictions were wrong because lower temperatures do not break down the enzymes because they become denatured. The enzyme activity decreases once the temperature decreases, as well. Enzyme activity increases when there is a rise in temperature, which is why lactose is broken down in much higher temperatures, resulting in a high presence of glucose.
In this lab, it was determined how the rate of an enzyme-catalyzed reaction is affected by physical factors such as enzyme concentration, temperature, and substrate concentration affect. The question of what factors influence enzyme activity can be answered by the results of peroxidase activity and its relation to temperature and whether or not hydroxylamine causes a reaction change with enzyme activity. An enzyme is a protein produced by a living organism that serves as a biological catalyst. A catalyst is a substance that speeds up the rate of a chemical reaction and does so by lowering the activation energy of a reaction. With that energy reactants are brought together so that products can be formed.