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Introduction of the effect of the concentration of enzyme peroxidase, ph, temperature, inhibitor at their different levels on the peroxidase reaction
Experiment of study of enzyme peroxidase
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Research on the Optimal Environment for Peroxidase to Survive with a focus on Temperature, pH, and Concentration Introduction Enzymes play a major role in virtually every single ecosystem as a conductor of reactions. They are important because without them reactions that need to take place in these cells would occur to slowly for DNA replication to occur as well as other reactions. The enzyme chosen for this experiments was peroxidase. “Peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor.” (Choi et al.). Enzymes are organic molecules that are made up of a string of carbons oxygens and hydrogens. The main component of bonding in these strings of molecules is …show more content…
The experiment will test the reactivity of various proteins, and such is determined by the change in color of the solution. The change in color of this solution occurred due to the addition of the guaiacol dye that reacted alongside the peroxidase. First, the amount of peroxidase solution used in each test needed to be constant, so we had to determine the optimum amount of solution to use. It was important to use accurate and precise data, so pipets were used to make sure the data was consistent. Through aligning seven test tubes, each with varying amounts of the peroxidase (.5mL, 1mL, 2mL) we found at which point the peroxidase is the most productive. By adding each solution to a spectrophotometer, we were able to determine the point at which the enzyme was the most absorbent, which in this case was 2mL, and this was carried though the whole …show more content…
Eleven clean test tubes were obtained, and reagents with the exact amount of buffer, hydrogen peroxide, peroxidase, and guaiacol were all mixed and spread out over the eleven test tubes in 5 segments. The Buffer and the peroxidase were in one tube while the hydrogen peroxide and the Guaiacol were in another. These were then exposed to water baths of varying interval temperatures at 4, 22, 45, 60, 100 Celsius. Once the solutions had reached their specified temperature, they were mixed together and immediately were tested with the spectrophotometer. The results were recorded in the lab notebook and were measured in
Data from Table 1. confirms the theory that as the concentration of glucose increases so will the absorbance of the solution when examined with the glucose oxidase/horseradish peroxidase assay. Glucose within the context of this assay is determined by the amount of ferricyanide, determined by absornace, which is produced in a one to one ratio.1 Furthermore when examining the glucose standards, a linear calibration curve was able to be produced (shown as Figure 1). Noted the R2 value of the y = 1.808x - 0.0125 trend line is 0.9958, which is statistically considered linear. From this calibration curve the absorbance values of unknowns samples can be compared, and the correlated glucose concentration can then be approximated.
In the lab, Inhibiting the Action of Catechol Oxidase we had to investigate what type of enzyme inhibition occurs when an inhibitor is added. Catechol oxidase is an enzyme in plants that creates benzoquinone.Benzoquinone is a substance that is toxic to bacteria. It is brown and is the reason fruit turns brown. Now, there are two types of inhibitors, the competitive inhibitor and non-competitive inhibitor. For an enzyme reaction to occur a substrate has to bind or fit into the active site of the enzyme. In competitive inhibition there is a substrate and an inhibitor present, both compete to bind to the active site. If the competitive inhibitor binds to the active site it stops the reaction. A noncompetitive inhibitor binds to another region
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
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.
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
The purpose of this experiment was to see if phenylthiourea (PTU) is a non-competitive or competitive inhibitor. Catechol, a phenolic compound found in the potato extract used will play the part of the substrate. Competitive inhibitors are known to bind to the active site of an enzyme and mimic the job of a substrate. This in turn causes the substrate to compete for a position at the active site and increase the concentration of substrate but the inhibitor is still at a constant level. If PTU were a competitive inhibitor the test tube carrying the extract would turn dark brown. Non- competitive inhibitors are known to bind on the enzyme and prevent the substrate from attaching
The purpose of this experiment was to discover the specificity of the enzyme lactase to a spec...
Figure 3: The absorbance of peroxidase reactions over two minutes using pH 3, pH 5, pH 7, and pH 9.
This is a type of reaction where a molecule is broken down into smaller pieces. It is called an anabolic reaction. This experiment is the breakdown of hydrogen peroxide to form water and oxygen in the air. Catalase is found in a cell organelle called the peroxisome. Peroxisomes in animal cells are occupied in the decomposition of
Purpose: The purpose of this lab is to explore the different factors which effect enzyme activity and the rates of reaction, such as particle size and temperature.
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: = == ==
Hypothesis: If a test tube filled with 3% hydrogen peroxide and catalase solution, the room temperature will increase the activity. Freezer, refrigerator, and boiling water will have
Many factors, for example, pH and temperature affects the way enzymes work by either increasing the rate or determining the type of product produced (). The report, therefore, analyses the effects of the enzyme peroxidase in metabolic reactions and determining its optimum temperature in the reactions.
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.
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