Wait a second!
More handpicked essays just for you.
More handpicked essays just for you.
enzyme concentrations experiments lab report
enzyme concentrations experiments lab report
enzyme concentrations experiments lab report
Don’t take our word for it - see why 10 million students trust us with their essay needs.
Recommended: enzyme concentrations experiments lab report
An investigation of the enzyme succinate dehydrogenase. Introduction Enzymes are a catalysts that speed up a chemical reaction inside of a cell without being consumed or changed by the reaction. (Wright, W. 2015) Enzymes catalyse reactions by lowering the activation energy that is required for the reaction to occur. (Nature, 2012) In this experiment we will be using Succinate dehydrogenase which is an enzyme that has been extracted from chicken hearts, succinate dehydrogenase is an enzyme of the TCA cycle (citric acid cycle) and involves the catalyses the oxidation of succinate, this means there is a loss of 2 hydrogen atoms. The aims of this experiment are to use 6-dichlorophenolindophenol (DPIP) as a hydrogen acceptor. When DPIP is blue it is in a oxidised state, but when it accepts 2 hydrogen atoms it will become colourless, the disappearing of colour indicates that a reaction is occurring. After the colour is gone we use the time taken to work out the rate of the reaction. in this experiment we will …show more content…
lastly we will add 1ml of 0.0003M DPIP, we made sure it was mixed well so the tube contained the same uniform colour, as soon as the DPIP was mixed we timed the time taken for the blue to fade from the tube. The outcome for the time taken for the colour to disappear was 3 minutes and 40 seconds which gave us the baseline for our experiment. The normal range for this experiment is usually between 2 and 7, if the time taken was under 2 minutes we would of needed to reduce the volume of the enzyme added and if the time taken was over 7 minutes we would of needed to increase the volume of the enzyme, and adjusting the buffer to make sure the volume in the tubes are 7mls for each experiment. As no modifications where made we can move on knowing our enzyme is the correct volume to conduct our
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 rate of reaction of Succinate dehydrogenase. Introduction: Enzymes are protein molecules that function as biological catalysts that can help break larger molecules into smaller molecules while remaining unchanged. They speed up the chemical reactions by lowering the energy of the activation barrier, specific to one molecule. The enzyme’s specificity arises from its active site, an area with a shape corresponding to the molecule with which it reacts (the substrate).
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 Activity of an Enzyme Sucrose using the enzyme sucrase (invertase) can be broken down into. Glucose and Fructose -. The aim of this experiment was to find out about the activity of enzymes through measuring the micromoles of sucrase. expressed whilst the following reaction occurs:-. SUCRASE [ IMAGE ] SUCROSE GLUCOSE + FRUCTOSE C12H2201 H20 C6H12O6 C6H12O6
Test-tube C had the best concentration according to the results. Three test-tubes were labelled A-C. Test-tube A had 1ml enzyme solution which was added to test-tube B which had 4ml buffer (pH 5 was used). 1ml of the solution from test-tube B was then added to the test-tube C which also had 4ml buffer (pH 5). Test-tube C was used as the enzyme in all the reactions. Nine test-tubes were taken out of them one was used as the the blank, labelled as test-tube 9. The blank had 5ml buffer (pH 5), 2ml hydrogen peroxide, 1ml guaiacol and no enzyme. Then, 3ml of buffer (pH 3) and 2ml of enzyme were added to test-tube 1. Test-tube 2 had 2ml hydrogen peroxide and 1ml guaiacol. Test-tube 1 and 2 were mixed. The same procedure was used for test-tube 3 as test-tube 1, but this time the buffer was pH 5. Test-tube 4 was prepared the same way as test-tube 2. Then, Test-tube 3 and 4 were mixed. Test-tube 5 was prepared as test-tube 1 but with buffer of pH 7 and test-tube 6 was prepared as test-tube 2. Next, test-tube 5 and 6 were mixed. Last but not the least, test-tube 7 was prepared as test-tube 1 but with buffer of pH 9 and test-tube 8 was prepared as test-tube 2. Then, test-tube 7 and 8 were mixed. The spectrophotometer was set to 470nm and using the blank it was set to zero. The four test-tubes with different pH’s (pH 3, pH 5, pH 7, pH 9) were read
We hypothesized that the more heat that we put in or the more heat that we take out, would denature the enzymes and slow down the rate. We set up a plate of depressions the same way as above. We boiled water to 50o C, poured the water onto a tray and did the steps of placing the discs in same as above and timed it until they rose above the surface. We did the same process but instead of using heat, we put ice and cold water on a tray which was about 3.5o C. The control for this experiment was the one that we did before because it was at room temperature. The results for the hot tray showed no rate. The cold tray sped up the rate of reactions making it occur faster than at room temperature starting at 6 for 100% catalase. This lab supported and disproved our hypotheses. It supported our hypothesis for adding more heat because the enzymes were in such hot conditions that the heat denatured the enzyme, making it not possible to create a chemical reaction. So the rate of reaction was zero because the enzymes didn’t split apart hydrogen peroxide. The cold tray disproved our hypothesis. We thought that the cold tray would also denature the the catalase so that there would be little to no rate. Maybe the data came out this way because the catalase was left out in room temperature for a long time that maybe when we took away the heat, it sped up the reaction rate.
However, there were a few trials that showed slightly different results. The reason for this could be that since this experiment is one pertaining to colour change, the change in colour may not be clear at times, making the end point difficult to discern. One reason for inconsistent colour change could be that though two drops of iodine were used each time to test the colour change, the dropper is not precise and does not have an exact gauge of how many millilitres are being used each time, affecting the uniformity of each iodine test. Also, since the amylase-starch solution was extracted manually using a dropper, there could have been inaccuracy in adding the solution to the iodine at exactly the same time for each trial.
In the second experiment 4.2, the effects of inhibitors on the enzyme catechol oxidase were observed. Phenylthiourea (PTU) was the specific inhibitor that was used. The phenylthiourea inhibits catechol oxidase by combining with copper that is a cofactor for the enzyme. The first test tube had the same amount of catechol and phenylthiourea. The reaction from the first test tube didn’t take place. In the second test tube there were 2x as much catechol as phenylthiourea. The reaction took place, but at a slower pace. There was no phenylthiourea in the third test tube, which made allowed the reaction to be accomplished fully.
At the time of conducting the experiment, the intention was to analyse the effect that an increase in catalase concentration had on the amount of oxygen (O2) produced if the hydrogen peroxide (H2O2) concentration was constant. It was proposed that when the catalase increases in concentration at the increments of 0.5%, 1%, 2%, and 4% and the hydrogen peroxide remained at a fixed concentration, the oxygen production would rise gradually. It was suggested that this would occur due to the collision theory ("BBC - GCSE Bitesize: Collision Theory") and the greater number of active sites thus an increase in accessibility allowing enzyme- substrate complex’s to be formed. According to the data gathered from the experiment, it can be implied that the hypothesis was supported as the data indicates an incline in oxygen
Introduction: In this experiment it talked about enzymes and substrates. What are enzymes and substrates? Enzymes are proteins that act as catalysts and help complex reactions. Substrates are the substance that the enzymes act. The reaction studied in the exercise is the oxidation of an ethanol substrate, and an acetaldehyde product. The two electrons were removed from the ethanol to convert to the oxidized form of Nicotinamide Adenine Dinucleotide (NAD+) to form the reduced form, NADH. This reaction is called a dehydrogenation reaction. The reduced form of NADH represents a bond energy storage molecule. The enzyme alcohol dehydrogenase (ADH), used NAD+ as a cofactor is reduced in the reaction. The purpose of this experiment will be to determine
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.
Moreover, the class average curve shows a similar trend, as the curve flattens, at 70% but with an enzyme activity of 5.3 x10-3 seconds. This indicates that even though the saturation point is the same it was considerably lower than our results, which could indicate sources of systematic error in the design of the practical.
Without enzymes, reactions wouldn’t occur and living organisms would die. For instance, the enzyme in the stomach breaks down large molecules to smaller molecules to absorb nutrition faster. Researchers experimented with enzyme activity with a potato extract. Researchers will test enzyme activity by increasing and decreasing pH levels, lowering and increasing temperature, and substrate concentration effects. In the first experiment, researchers hypothesized whether different pH levels would change how much Benzoquinone are created and how will the enzymes function in neutral pH levels than higher and lower levels. Researchers used potato extract and different levels of pH to test their hypothesis. In addition, researchers questioned at what temperature does the greatest amount of potato extract enzyme activity take place in. Researchers then hypothesized that the results would indicate the greatest amount of potato enzyme activity level will take place in 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. In this experiment researchers used different measurements of catechol and 1cm of potato extract. Researchers hypothesized that the increase o substrate would level out the enzyme activity
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.