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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,
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“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
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 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: = == ==
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
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 ...
Enzymes have the ability to act on a small group of chemically similar substances. Enzymes are very specific, in the sense that each enzyme is limited to interact with only one set of reactants; the reactants are referred to as substrates. Substrates of an enzyme are the chemicals altered by enzyme-catalysed reactions. The extreme specific nature of enzymes are because of the complicated three-dimensional shape, which is due to the particular way the amino acid chain of proteins folds.
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
We were not given any instructions either to shake or not to shake the test tubes with the coloured solutions before inserting them in the spectrophotometer to read the absorbance. By shaking each test tube a certain number of times before putting it in the spectrophotometer could have improved the accuracy of the of absorbance of the solutions.
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 function to catalyze a change in a chemical reaction they are normally made of
The definition of an enzyme is a type of protein that induces reactions. Many enzymes have their own shape that is there because of a certain amino acid(“Biology” 79). Each enzyme has a small part called the active site. The active site is what makes up the enzymes abilities. The active site decides whether an enzyme can bond with a specific type of molecule,and this is known as the substrate of the enzyme. An enzyme substrate complex forms when there are weak, noncovalent chemical bonds, and the the substrate and enzyme intertwine. The ability for the substrate to bind is reduced when the shape of the active site is changed.
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.
In part B of the experiment, the amount of peroxidase to use for the rest of the experiment was standardized, and it was concluded that 250μl of peroxidase should be used in the experiment for optimal results. In part C of the experiment, the effect of temperature was tested. Six cuvettes were numbered, and three mL of peroxidase was added to a test tube to then be placed in a hot/boiling water bath for 15 minutes. After the test tube was taken out and let cooled, 250μl of the boiled water was added to cuvette six. Cuvette two was placed in ice, cuvette four was placed in the 32°C water bath, and cuvette five was placed in a 48°C water bath for ten minutes. After the ten minutes was up, 1000μl of buffer was added to cuvettes one through six, 500 mL of guaiacol was added to all cuvettes as well, and 250mL of normal peroxidase was added to cuvettes two through five. Cuvette one was used to calibrate the spectrophotometer. All of these values can be seen in the table
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 specialized protein that acts as a catalyst and facilitates complex metabolic processes. An enzyme, like any protein, is a polymer made up of a long chain of amino acids. The sequence of amino acids is determined by the DNA template in which it was made, and the amino acids are attached together by peptide bonds. Cross linking takes place between the R groups of the amino acids and forms a unique three dimensional molecules. The structure and spatial configuration of an enzyme, especially its binding site, is key to its optimal function and activity. This 3-dimensional structure can easily be altered by environment factors, such as salinity and pH. Each enzyme has a binding site in which chemical bonds are achieved with their
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.