Often people use hydrogen peroxide to clean wounds instead of alcohol. The reason for this is that, it does not have a burning sensation after applying it, while alcohol on the other hand has a burning sensation. After the supplication of this chemical, the skin absorbs this chemical, it disrupts the homeostasis of the body. Hydrogen peroxide is often used for small cuts or an affected area. Once applied to the affected area, this chemical releases oxygen, which creates foaming that helps both the removal of dead skin as well as helps clean the affected area. Using this chemical as a replacement of alcohol is not sensible to do, as there are many issues that come along with this. Hydrogen Peroxide contains a large amount of oxygen, and if …show more content…
As seen in figure 1.0 (above), if there is a high percent concentration of the catalase than water in the catalase solution, then there time it would take for the filter paper to reach the top of the solution is faster. If there is a low percent concentration of the catalase than water in the catalase solution, then the time it would take for the filter paper to reach the top of the solution will be slower. For example, if the enzyme concentration is 80 percent, and the concentration of water is the remaining 20%, then it is more likely to have a lower amount of time, due to the rapid speed of the filter paper reaching the top of the beaker. Since there is a high concentration of enzymes, the reaction will occur faster than the lower percent of enzyme concentration. The enzyme (catalase) is the reason why the rate of reaction is different from the rest. Enzyme’s sole purpose is to speed up the process of reactions that take place, without being used up in the reaction (Dave, 2015). If there is a high amount of enzyme present in a reaction, then it will surely go faster than the reaction with a lower amount of enzymes. The percent catalase clearly affects the rate of reaction, due to the fact that time is affected, then the rate of reaction will be as well, it all depends on the time of the filter paper reaching the top. The time and the rate of reaction depends on the percent of enzyme catalase, while on the other hand, the distance is an independent variable. The important part of an enzyme is that it has an active site, which is a slight opening on the enzyme, to allow for the substrate to fit into the active site (Clark, 2007). If the substrate fits perfectly into the active site, then the reaction will take place, and those substrates that fit into the active site will also be known as reactants (Clark, 2007). The enzymes increase the rate of reaction, while they also lower the
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The objective of this lab was to determine the best pH level to increase enzyme activity. As this objective was met, it was discovered that water (pH level 7) was the best for percent absorbance. The hypothesis for this experiment was, “If peroxidase is an enzyme and therefore contains certain pH tolerances, then when placed in solution with pH levels of three, seven, and ten and the reaction is measured by a colorimeter, then water will be the optimal solution for maximum reaction rate.” As seen in the tables and graphs, the data supported the hypothesis due to the fact that most enzymes have an optimal pH of 4-9.
It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. At the end of the experiment the results prove the hypothesis to be incorrect. INTRODUCTION Enzymes are proteins that allow a reaction to speed up. These proteins are made up of monomers known as amino acids.
The purpose of this experiment was to analyze the effects of the variables: temperature, pH, and enzyme concentration, on the enzymatic reaction rate of catalase and the level at which its products are released, measuring the rate of absorption using the indicator solution guaiacol and a spectrophotometer to develop a hypothesis of the ideal conditions for these reactions. My hypothesis is that the extremes in concentration, temperature and pH will negatively affect the Au rate. This experiment used 11 solutions contained in cuvettes. Each cuvette, once mixed, is placed in spectrophotometer and then a reading taken every 20 seconds. Cuvettes 1, 8, and 10 are used as blanks to zero out the spectrophotometer.
Leslie G Hour 3 10-12-15 Thinking About the Problem For my science experiment project I am testing to see which chemical is the sanitizer for a hot tub or pool. This "Thinking About the Problem" will help me think about my topic and gather information to modify the variables in my experiment. The following chemicals are sanitizers that are used to control bacteria and algae growth. They also reduce the risk of viruses and microorganisms as well as help keep the water clear.
The results of the experiment were in fact really similar to my hypothesis. In Test Tube #1, the reaction was almost exactly what was predicted. The reaction rate of the enzyme was slowed but not stopped, it was still able to function just not as efficiently. Test Tube #2 was the control and did exactly what it was supposed to, give a base line reading for the reaction rate in the enzymes normal environment. Test Tube #3 also reacted as predicted, showing similar results to Test Tube #2 and after figuring in the standard error bars of both could easily be the same rate.
Enzymes are proteins that significantly speed up the rate of chemical reactions that take place within cells. Some enzymes help to break large molecules into smaller pieces that are more easily absorbed by the body. Other enzymes help bind two molecules together to produce a new molecule. Enzymes are selective catalysts, meaning that each enzyme only speeds up a specific reaction. The molecules that an enzyme works with are called substrates.
Nevertheless, the effects caused by the breakage of bonds will eventually lead to a decrease in the rate of reaction. As seen in the data, the reaction rate increased from 0.088 to 0.101 throughout the interval of -5℃ to 20℃ then decreased to 0.037 throughout the interval 20℃ to 56℃. This can be explained by the fact that 20℃ is the optimal temperature, therefore the active site of the enzyme is complementary to the substrate, causing the rate of reaction to be
7. In this experiment, if the sucrose concentration were increased to 70 g/l would you expect sucrase activity to be significantly higher than the activity at 35 g/l. Explain your answer. No, because based on the results once it reached 30 g/l 35 g/l the results had stayed the same. There, the activity is lessening and coming to what looks like a plateau. 8.
The 0.1% is the concentration amount. Just like temperature and pH, substrate concentration can speed the reaction only up to a certain limit. When we mixed pH 3 enzyme tube with substrate tube, we used 0.3 mL of hydrogen peroxide, but if we were to increase the amount, then the experiment would have been faster. Our
ABSTRACT: The purpose of the experiments for week 5 and week 6 support each other in the further understanding of enzyme reactions. During week 5, the effects of a substrate and enzyme concentration on enzyme reaction rate was observed. Week 6, the effects of temperature and inhibitor on a reaction rate were monitored. For testing the effects of concentrations, we needed to use the table that was used in week 3, Cells.
H20 + 2 O2 This experiment will use 1% catalase solution and 3% hydrogen peroxide solution, both diluted into water so the reaction slows down. Temperature will be controlled in this experiment to change the reaction speed of the enzyme and the substrate, this is what the experiment is looking at. The effect of the temperature will be determined by how much gas is released in two minutes, which will change the pressure inside the test tube and will be measured by a gas
The lab results would have been more accurate if they were based off quantitative properties instead. For instance, if the reaction between catalase and hydrogen peroxide was timed using a stopwatch to see how long the oxygen gas bubbled for, the times could have been compared to obtain a more accurate reaction rate for each reaction. Furthermore, the temperature of the solution after the test tubes were taken out of their respective water baths were not monitored. This could have been a factor that affected the reaction rate of catalase, since the reactions may have not occurred at the same temperature. A thermometer could have been used to measure the temperature of the contents in the test tubes once they were removed from the water baths to ensure that all the reactions took place at the same temperature as the baths they were placed
By observing figure 3, the more enzyme that is available, the faster the reaction rate is. The optimal enzyme concentration was chosen based on the R2 values from figure 2. The highest observable rate also had the best R2 number, which was closest to one. This enzyme concentration was used in part 2.
Introduction: Enzymes are biological catalysts that increase the rate of a reaction without being chemically changed. Enzymes are globular proteins that contain an active site. A specific substrate binds to the active site of the enzyme chemically and structurally (4). Enzymes also increase the rate of a reaction by decreasing the activation energy for that reaction which is the minimum energy required for the reaction to take place (3). Multiple factors affect the activity of an enzyme (1).
Bio Chem lab Report 04 Enzyme Biochemistry Group Member: Chan Man Jeun Duncan (16002621) Law Sze Man (16000478) Introduction Enzyme is a protein base structure substance in our body. It works at a biocatalyst that will catalyzing the chemical reaction, which helps to speed up the chemical reaction. Enzyme could only function in specific shape, and the shape of enzyme is depending on the environment, therefore it is hard for an enzyme to function well in an extreme environment. The aim of this experiment is to see can the enzyme functions normally in different environment(pH, temperature and salt concentration) via using starch solution, amylase from saliva, 0.5M HCl solution, 0.5M NaOH solution and NaCl solution, and using iodine solution