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Enzyme concentrations experiments lab report
Enzyme concentrations experiments lab report
Enzyme concentrations experiments lab report
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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
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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
3.) Divide your 30g of white substance into the 4 test tubes evenly. You should put 7.5g into each test tube along with the water.
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.
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.
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
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).
Alkaline Phosphatase (APase) is an important enzyme in pre-diagnostic treatments making it an intensely studied enzyme. In order to fully understand the biochemical properties of enzymes, a kinetic explanation is essential. The kinetic assessment allows for a mechanism on how the enzyme functions. The experiment performed outlines the kinetic assessment for the purification of APase, which was purified in latter experiments through the lysis of E.coli’s bacterial cell wall. This kinetic experiment exploits the catalytic process of APase; APase catalyzes a hydrolysis reaction to produce an inorganic phosphate and alcohol via an intermediate complex.1 Using the Michaelis-Menton model for kinetic characteristics, the kinetic values of APase were found by evaluating the enzymatic rate using a paranitrophenyl phosphate (PNPP) substrate. This model uses an equation to describe enzymatic rates, by relating the
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.
This enzyme speeds up the break down of hydrogen peroxide into water and oxygen, as enzymes are biological catalysts. [IMAGE]The reaction: Hydrogen peroxide Water + Oxygen Catalase -------- [IMAGE] 2H2O2 2H2O + O2 Apparatus: Hydrogen Peroxide, Several sticks of celery, Stand, boss and clamp, 100ml conical flask, 25cm3 burette, 1800cm3 beaker, Rubber bung with delivery tube, Distilled water, Large container filled with water, 10cm3 measuring cylinder, 10cm3 syringe, 20cm3 syringe, Blender, Knife, Ceramic tile, Electronic balance (correct to 2 decimal places), Sieve, Stopwatch/timer. The variables: There are many possible variables in this investigation, such as pH, temperature, the concentration of substrate and the concentration of the enzyme.
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.
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.
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.
Setting up the apparatus was quick and easy, but measuring the DCPIP solution took a bit of time because they had to be the same volume so that they don’t affect the results. Although there were variables that were controlled, there was another variable which I did not identify until after our investigations were done.
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