How Enzymes Work
In Different Environments
By Sarah Smith
Biology1111
October 20, 2011
Lab Partner:
Nellie Greer
ABSTRACT Peroxidase is an enzyme found in potatoes that catalyzes the breakdown of hydrogen peroxide, H2O2, into O2 gas and water. We examined the different pH environments that can affect the enzyme activity during the breakdown of H2O2. In order to do this, we added different levels of pH, low, medium, and high, into different test tubes with the enzyme and H2O2, and we then inverted the tube. The amount of O2 gas produced was then measured and recorded. The result was that the higher pH produced more gas, followed by medium pH, then low pH. The enzymes were more active in the pH of about 10. It increased
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The effectiveness of peroxidase was measured in a varying pH environment. The environment’s pH can range from 1-14, 7 being neutral, 7-1 being more and more acidic towards 1, and 8-14 being more and more basic towards 14 (Raven, 2011).
We hypothesized that a medium pH buffer added to the hydrogen peroxide an peroxidase reaction would be the best condition for the enzyme activity due to it being the more neutral than the high, being basic, and low, being acidic, pH.
Level of Solution Each Time Interval | Low pHLevel of Gas in mL | Medium pHLevel of Gas in mL | High pHLevel of Gas in mL | Time Zero | 1.5 | 1.5 | 1.6 | 5 Minutes | 2.7 | 2.5 | 3.5 | 10 Minutes | 3.1 | 3.4 | 4.5 | 15 Minutes | 3.5 | 4 | 5.8 | 20 Minutes | 4 | 4.5 | 7 | 25 Minutes | 4.5 | 5 | 7.9 |
Total Gas in mL | 3 | 3.5 | 6.3 |
Table 1: This table shows the position that the solution was at inside the graduated tube it was held in at each time interval it was measured.
Amount of O2 Produced in Time
Figure 1: Amount of O2 gas curves to the time at which it was measured according to low, medium, and high pH.
Bibliography
Raven, Peter H., & Johnson, George. 2011. Biology, 9th ed. McGraw-Hill, New York.
Kaiser, Gary E. 2001. Enzymes.
In this experiment, the naturally occurring peroxidase is extracted from homogenized turnip (Brassica rapa) pulp (Coleman 2016). Its role in the environment is to remove toxic hydrogen peroxide during metabolic processes where oxygen is used (Coleman 2016). The goal of this experiment is to evaluate the change of absorbency of turnip peroxidase within a metabolic reaction utilizing oxygen. Any change noted is indicative of the peroxidase removing hydrogen peroxide. Within this experiment, the extract will be prepared, the amount of enzyme will be standardized, and the effect of changing the optimal conditions will be observed. If the enzyme concentration is increased then the rate of the reaction decrease. If the pH of solutions used is increased
This experiment looked at how substrate concentration can affect enzyme activity. In this case the substrate was hydrogen peroxide and the enzyme was catalase. Pieces of meat providing the catalase were added to increasing concentrations of hydrogen peroxide in order to measure the effect of hydrogen peroxide concentrations on the enzyme’s activity. The variable measured was oxygen produced, as water would be too difficult to measure with basic equipment.
Most enzymes have an optimum pH of around 7, which is fairly neutral. To ensure the experiment is a fair test, I will use the same pH of hydrogen peroxide in every test.
The purpose of this experiment was to simply measure oxygen production rates released from decomposed hydrogen peroxide under different conditions (concentration of enzymes, temperature, and PH level).
Peroxidase is a turnip enzyme; it is used in the oxidation of hydrogen peroxide to lower activation energy, speeding up the reaction. The activity of peroxidase is highly dependent on its environment and most importantly the pH level. Peroxidase has been the focus of many recent studies and is believed to possibly reduce swelling among other things. We conducted an experiment testing the effect different levels of pH had on the reaction rate of peroxidase. In the experiment we created different solutions all containing hydrogen peroxide, peroxidase, and guaiacol. However each cuvette contained a different pH level, 2,5,7,or
The aim of my investigation is to see how pH affects the activity of potato tissue catalase, during the decomposition of hydrogen peroxide to produce water and oxygen.
The purpose of this experiment is to learn the effects of a certain enzyme (Peroxidase) concentration, to figure out the temperature and pH effects on Peroxidase activity and the effect of an inhibitor. The procedure includes using pH5, H202, Enzyme Extract, and Guaiacol and calibrating a spectrophotometer to determine the effect of enzyme concentration. As the experiment continues, the same reagents are used with the spectrophotometer to determine the temperature and pH effects on Peroxidase activity. Lastly, to determine the effect of an inhibitor on Peroxidase, an inhibitor is added to the extract. It was found that an increase in enzyme concentration also caused an increase in the reaction rate. The reaction rate of peroxidase increases at 40oC. Peroxidase performed the best under pH5 and declined as it became more basic. The inhibitor (Hydroxy-lamine) caused a decline in the reaction rate. The significance of this experiment is to find the optimal living conditions for Peroxidase. This enzyme is vital because it gets rid of hydrogen peroxide, which is toxic to living environments.
The purpose of this report is to find out the effect of change in the Temperature, PH, boiling, concentration in peroxidase activity. Peroxidase is an enzyme that converts toxic hydrogen peroxide (H2O2) into water and another harmless compound. In this experiment we use, turnips and horseradish roots which are rich in the peroxidase to study the activity of this enzyme. The activity of peroxidase with change in temperature was highest at 320 Celsius and lowest at 40C. The activity of peroxidase was highest at a pH of 7, while it was lowest at pH of 9.Peroxidase activity was very low and constant with boiled extract, while the activity was moderate
will be working at the pH 7 the majority of the time and our bodies
Abstract: Enzymes, catalytic proteins that at as catalysis which makes the process of chemical reactions more easily. There are two main factors that actually affects enzymes and their functions which are temperature and pH. Throughout this experiment, the study how pH and peroxidase affects each other and the enzyme was made. The recordings of how the enzymes responded when it was exposed to four different pH levels to come up with an optimum pH which was predicted in the hypothesis and the IRV at the end.
Observing how the enzyme catalase found in chicken and beef livers breaks down hydrogen peroxide at varying pH levels and temperatures.
(Raven 53) There are several factors that affect the ability of the enzyme to catalyze a reaction. In this study, the effects of the substrate concentration, pH, and temperature will be examined. To test the effects of these environmental factors on enzymes catalase, a common enzyme found in the majority of all aerobic cells, will be examined. Catalase protects cells from the toxin hydrogen-peroxide, which is a byproduct of cell metabolism by catalyzing the decomposition of hydrogen peroxide into oxygen gas and water. The measure of oxygen gas and water under various conditions is an indicator of the effects environmental factors have on enzyme activity. (German
The results support the hypothesis by revealing that there is a correlation between the higher the concentration of Peroxidase, the faster the Enzyme Activity rate is. The more intense the color is, the faster the Enzyme Activity rate is, and base on the graph, since one minute of the experiment, there is already differences in color intensity between all three groups. Group two with the highest concentration of 3.0mL, during the first minute was at the color intensity of four, while the control group with the second highest concentration of 1.5mL was at the color intensity of two, and group one with the lowest concentration of 0.75mL was only at the color intensity of one. As time continue, all three groups rise in color intensity; however,
This experiment is designed to analyze how the enzyme catalase activity is affected by the pH levels. The experiment has also been designed to outline all of the directions and the ways by which the observation can be made clearly and accurately. Yeast, will be used as the enzyme and hydrogen peroxide will be used as a substrate. This experiment will be used to determine the effects of the concentration of the hydrogen peroxide versus the rate of reaction of the enzyme catalase.
This does not mean that these reactions have to be examined within the body in order to understand them, and in fact it is generally much easier to examine chemical reactions as they tae place outside organisms, in order to better understand what might be taking place within organisms. The following pages will present the details of an experiment involving a specific class of proteins, peroxidases, that act as enzymes in many organisms to breakdown potentially toxic byproducts from other reactions into non-harmful waste products that can be disposed of. An historical and chemical overview of peroxidases will be provided first, followed by an examination of certain