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Determination of enzyme activity lab report
Determination of enzyme activity lab report
Biology lab report determination of enzyme activity
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Effects of Modifying Concentration, pH , and Boiling on Activity of Peroxidase Abstract An enzyme is a catalysis and catalysis s substance that increases the rate of a chemical reaction without itself going through a permanent chemical change. In this lab we will discover exactly how the substrate connects with the active site. The main substance we use throughout this lab is peroxidase a eukaryotic organelle from plant tissues. Once there is a color change we test that using a spectrophotometer. Introduction Organisms have their own creative structures that helps them function properly. The main structure that has been discussed in the enzyme. A pure definition of an enzyme is a “protein that catalyzes a specific metabolic reaction” (Coleman, …show more content…
“Peroxidase is a heme-containing enzymes found in peroxisome (eukaryotic organelle) and can be obtained from a variety of plant tissues” (Coleman, 2015). Peroxidase breaks down different compounds and adds hydrogen to make it harmless. Peroxidase was a number of substrates such as cytochrome C and many more dyes (Ahmad, 2014). PH is 7 which is neutral and what is does to higher or lower the activity results in activity loss of an enzyme. The purpose of this lab is to observer effects different environments have on an enzymes (Lockwood, 2012). If the pH is changed then the speed of the enzymes will change (Urry, 2013). Prediction when the pH is changed of course it will speed up the enzymes because the pH changes the enzymes shape and when changing the enzymes shape is affects the function of the chemical …show more content…
After five the test tube was removed and cooled to room temperature. Three more test tubes were obtained and labeled 1, 2, and 3. The correct reagent was added to each test tube as seen. The spectrophotometer was adjusted using the control (“Blank”) as you did in the previous experiments. The contents of test tube 2 and 3 were mixed in a clean (clear of fingerprints) and the absorbance changes at 15 second intervals for 60 seconds were measured. The results were recorded in Table 9. Effects of temperature on enzyme activity The enzyme assay was repeated in water baths at four temperatures: an ice bath (approximately 4 degrees celsius), room temperature (approximately 23 degree celsius), 32 degree celsius, and 48 degree celsius. Test tube 9 was obtained and labeled 19. The appropriate solutions were added to each test tube. All tubes were preincubated at the appropriate temperature prior to the mixing of tubes. The tubes were then set aside to acclimate for 15 minutes. After the equilibrium was reached and the spectrophotometer was adjusted with the control (tube 1) the pairs 2 & 3, 4, & 5, 6 & 7, and 8, & 9 were mixed one at a time. The absorbance changes at 15 second intervals for 60 seconds for each temperature were
The color that was chose to be shined through the sample was purple. The spectrophotometer was set at a wavelength of 400nm to represent the purple color. It was zeroed using the blank meaning the spectrophotometer read zero as absorbance amount. The blank consisted of 5mL of water and 2.5 mL AVM and it was placed in cuvette. A solution with a known concentration of 2.0x10-4 M was used in the spectrometer. For this solution, 5 mL of the solution with 2.5 mL of AMV was placed in the cuvette. The cuvette was placed inside of spectrophotometer and the amount of absorbance was recorded. This procedure that involves a solution with a known concentration was repeated for the concentrations:1.0x10-4 M,5.0x10-5 M,2.0x10-5M, and1.0x10-5M.A unknown solution absorbance was measured by putting 5 mL of unknown solution with 2.5 mL AMV in a cuvette. The cuvette was placed in the spectrophotometer and the amount of absorbance was recorded. The procedure that deals with the unknown solution was repeated 2 more times with the same solution and the same amount of solution and AMV. The average of the three unknown solution was calculated and the concentration of the unknown solution was
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: = == ==
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).
Enzymes are biological catalysts - catalysts are substances that increase the rate of chemical reactions without being altered itself. Enzymes are also proteins that fold into complex shapes that allow smaller molecules to fit into them. The place where these substrate molecules fit is called the active site. The active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of residues that form temporary bonds with the substrate and residues that catalyse a reaction of that substrate. (Clark, 2016)
Introduction: According to the textbook Biology Life on Earth with Physiology 10th edition enzymes are biological catalysts that are made of protein, and they speed up the rate of a specific biological reaction. (Audsirk, Audsirk, and Byers 100-105) and chemical reaction rates go up without changing the chemical equilibrium between reactants and products. (Cooper, 2000). All enzymes have a pocket, which is called an Active Site where reactants, which are called substrates, were substrates could enter. (Audsirk, Audsirk, and Byers 100-105) Enzymes regulate both exergonic and endergonic reactions, and enzymes are found in almost all cells (Audsirk, Audsirk, and Byers 100-105). Enzymes are regulated by three different regulations; Allosteric Enzyme Regulation, Competitive Inhibition, and Competitive Inhibition. (Audsirk, Audsirk, and Byers 100-105). In Allosteric Enzyme Regulation a molecule that is inhibited causes an active site to change shape. In Competitive Inhibition the enzyme and substrate are binding normally, and in noncompetitive inhibition a substrate imposter ...
According to Elmhurst, an enzyme is a protein molecule that is a biological catalyst with three characteristics. First, the basic function of an enzyme is to increase the rate of a reaction. Second, most enzymes act specifically with only one reactant called a substrate to produce products. The third and most remarkable characteristic is that enzymes are regulated from a state of low activity to high activity and vice versa (Elmhurst). According to Princeton, catalase is a common enzyme found in nearly all living organisms that are exposed to oxygen, where it functions to catalyze the decomposition of hydrogen peroxide to water and oxygen. Catalase has one of the highest turnover
Enzymes are biological molecules that are a catalyst for chemical reactions within cells, they are made out of large proteins. Without enzymes these chemical reactions would still happen but not at a perceptual rate or one that supports life. “Enzymes
proteins and can be used repeatedly. The enzyme studied in this experiment is catalase an
Our bodies involve and require many different biochemical reactions, which is achieved through the help of enzymes. Enzymes are proteins in our bodies that act as catalyst as they speed up vital biochemical reactions by reducing the “activation energy” needed to get the reaction going. To sustain the biochemistry of life, enzymes maintain temperature inside our living cells balanced and the concentration of reaction molecules. Enzymes are extremely efficient because they remain remarkably unchanged, therefore have the potential to be used over and over again. They are extremely specific with the reactions they catalyze, like a lock and key and, extremely reactive. The molecule to which enzymes make accelerated changes to is the substrate. The molecule that is present after the enzyme-catalyzed reaction is the product. Most enzymes require specific environmental conditions such as temperature and pH levels to be met in order for them to function properly and efficiently. In the first part of the lab we specifically examined a simple enzyme-catalyzed reaction using catechol (the substrate) which will be catalyzed by the enzyme catecholase and will then result in color change. This familiar color
Having two people in the group, we had one person be a timer and a spectrophometer reader, and the other was the data recorder. After recording the time, we then mixed tubes 2 and 3. We then recorded the data of the combined tube and wrote down the results. After this, we mixed tubes 4 and 5 and completed the same procedure as with tubes 2 and 3 (“Biology” 80). We then had to determine the effect of temperature. We found the results of these four temperatures:
In the first experiment, temperature affects the rate enzyme activity, and the more temperature increases, the faster the reaction will proceed until the optimum temperature is reached. After that, enzyme activity will decrease. Furthermore, hydroxylamine and hydrogen peroxide have extremely similar structures. In the second experiment, hydroxylamine affects peroxidase’s activity. The more hydroxylamine, the less enzyme activity will occur due to the competitive inhibition of the
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.
The purpose of enzymes, also known as protein molecules, is to aid in the conversion of reactants to products by catalyzing the chemical reaction. In the experiment conducted in the BZ 310-L06 laboratory the enzyme catalase, which converted hydrogen peroxide into the products water and oxygen, was analyzed. The catalase enzyme was subjected to varied substrate concentration, inhibitors, and varied temperatures to determine the effects of the environment on the enzyme’s ability to function. The enzyme was first observed in a trial with a controlled environment where the hydrogen peroxide concentration was 30%, at room temperature, and without inhibitors present. This trial allowed a baseline measurement for catalase’s function as an enzyme.
An enzyme is a biological macromolecule protein which acts as a catalyst, it speeds up a specific chemical reaction without being consumed or changed in the process. When the substrate and enzyme are combined they form an enzyme substrate complex. Enzymes shape can change making their active site fit more tightly to the substrate entering.
Repeat this step until you have completed this process 6 times and have measures samples. Prepare a reagent blank by making a test tube containing 3 mL of water and 3 drops of potassium iodide. With the assistance of a pipette, remove 1 mL of this solution to place in a cuvette. Finally, use a spectrophotometer to measure the amount of absorbance at 605 nM of each of the samples collected. Also, use a regent blank in between each measurement.