The end goal of this lab was to observe and compare the rate of reactions when they are affected by protein catalysts (enzymes) and non-protein catalysts under varying conditions. The reaction occurred the fastest when the liver and potato was crushed up to increase the surface area between the enzyme and the substrate. This proved the following hypothesis correct: it was hypothesized that if the liver and potato are broken up into smaller pieces, then the rate of reaction will increase because the surface area between the enzyme and its substrate will be increased, allowing the reaction to take place faster. This data fits with the induced fit model of enzymes because the more active sites that the substrates can react with, the faster the …show more content…
105-106). It was hypothesized that if the hydrogen peroxide was exposed to the liver, the hydrogen peroxide would decompose faster than the hydrogen peroxide exposed to the potato because complex organisms (like mammals and birds) require more ATP energy and therefore have an increased rate of cellular respiration, producing more hydrogen peroxide as a byproduct (Marziali, 2009). So, the enzymes in a complex organism are more likely to be able to decompose the hydrogen peroxide. This proved true in this lab, however, the enzyme in both potato and liver is the same, so it must be a different factor such as enzyme concentration that caused a different rate of reaction to be observed between the liver and the potato (Nuffield Foundation, 2011; Eed, …show more content…
This did not prove true as the reaction occurred the fastest at 37°C, the second fastest at 0°C, and the slowest at 100°C. When further research was conducted it became apparent that catalase denatures at 55°C and therefore could not effectively decompose the hydrogen peroxide in the experiment at 100°C (Clyde, 1950). On the other hand, there should not have been a significant difference between the sample at 0°C and the sample at 37°C because catalase is limited by the diffusion rate of hydrogen peroxide which is a process not heavily affected by temperature (Nicholls & Hewitson, n.d.). It was hypothesized that adding new enzymes will have no effect because the enzymes are not used up in the reaction, however, adding new hydrogen peroxide will cause an increase in the rate of reaction because there will be more products to react. This was proven true in this lab and fits the induced fit theory of enzymes and the basic chemical understanding of catalyzes (Clark, 2013; Giuseppe et al., 2002,
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
Whole carrots have a different reaction to the higher concentrations of hydrogen peroxide. There is a dramatic increase in the rate of reaction of catalase enzymes in the whole carrot, meaning that the saturations kinetics can be utilized at much higher rates of concentration.
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
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.
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.
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
Comparing the Reaction Rates Between Potato and Hydrogen Peroxide Against Liver and Hydrogen Peroxide Through Loss in Mass
The Effect of Surface Area on the Rate of Reaction Between Catalase from a Potato and Hydrogen Peroxide
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
Observations: Liver and Potatoes will be placed in hydrogen peroxide in order to observe the reactions due to the enzyme, catalase, found in both.
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.
Purpose: This lab gives the idea about the enzyme. We will do two different experiments. Enzyme is a protein that made of strings of amino acids and it is helping to produce chemical reactions in the quickest way. In the first experiment, we are testing water, sucrose solution, salt solution, and hydrogen peroxide to see which can increase the bubbles. So we can understand that enzyme producing chemical reactions in the speed. In the second experiment, we are using temperature of room, boiling water, refrigerator, and freezer to see what will effect the enzyme.
Researchers then hypothesized that the results would indicate the greatest amount of potato enzyme activity level will take place at room temperature. In this experiment, researchers used potato extract and different temperature levels to test the hypothesis. Moreover, researchers wanted to test the color intensity scale and how specific catechol oxidase is for catechol. In this experiment, researchers used dH2O, catechol solution, hydroquinone, and potato extract. Lastly, researchers tested the substrate concentration and how it has an effect on enzyme activity.
The temperature of the water shows if the temperature in which catalase reacts in has an effect on the amount of oxygen produced. Every enzyme has an optimum amount of pH, which allows it to have a higher reaction velocity (WBC).The higher the reaction velocity the more reactive the enzyme is. Measuring the different amount of pH solutions and their effect on the amount of oxygen produced can show the optimum pH for catalase and the effect pH has on catalase. The data that these three independent variables will yield will allow us to better understand the effects concentration, temperature and pH have on the enzyme catalase. If catalase reacts at full concentration, 37 degrees celsius and a pH of eight the enzyme catalase will produce more oxygen than if it is at room temperature, a lower concentration and a more acidic base because the higher temperature will allow molecules to move faster and have a higher chance to collide and react, a higher concentration will create a higher enzyme to substrate ratio which allows it to react more and finally a more basic pH will allow it catalase to have a higher reaction