Rb Scavenger

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

9. What is the policy on Late Assignments? (Please answer for your program if it has specific requirements.)

The role of an enzyme is to catalyse reactions within a cell. The enzyme present in a potato (Solanum Tuberosum) is catechol oxidase. In this experiment, the enzyme activity was tested under different temperature and pH conditions. The objective of this experiment was to determine the ideal conditions under which catechol oxidase catalyses reactions. In order to do this, catechol was catalyzed by catechol oxidase into benzoquinone at diverse temperatures and pH values. The enzyme was exposed to its new environment for 5 minutes before the absorbance of the catechol oxidase was measured at 420 nm using a spectrophotometer. The use of a spectrophotometer was crucial for the collection of data in this experiment. When exposed to hot and cold temperatures, some enzymes were found to denature causing the activity to decrease. Similarly, when the pH was too high or low, then the catechol oxidase enzyme experienced a significant decrease in activity. It can be concluded after completing this experiment that the optimal pH for catechol oxidase is 7 and that the prime temperature is 20º C. Due to the fact that the catechol oxidase was only tested under several different temperatures and pH values, it is always possible to get a more precise result by decreasing the increments between the test values. However, our experiment was able to produce accurate results as to the

Kinetics is the study of the rate of chemical processes. The kinetics of the reaction between crystal violet and NaOH was studied. In order to monitor crystal violet concentration as a function of time, a spectroscopic colorimeter was used. What is the rate law for decolorization of crystal violet? In order to figure this out, the rate of the reaction of crystal violet and sodium hydroxide must be found. In this experiment, the initial goals were to determine the overall rate law for the rate of decolorization of crystal violet in basic solutions as a function of time and to determine the rate law for the reaction including the actual value of k; Rate = k[A]x[B]y. The rate of a reaction was expected to depend on the concentrations

This is largely because they are relatively cheap and simple to manufacture. Furthermore, they produce vibrant shades of color and are reasonably soluble in water (Liu, Wan, Nan, n.d.). However, these dyes are now manufactured at such a large scale that they bring up numerous health and environmental concerns. In recent years azo dyes, especially Allura Red AC, have been connected to child hyperactivity, which also raises concerns over other potentially toxic effects they can have on living organisms (“FDA Probes Link”, 2011). This is only amplified by the fact that azo dyes such as Allura Red AC and Azo Grenadine are also especially recalcitrant to conventional methods of wastewater treatment. Research on this topic led me to an article on electrochemical advanced oxidation processes and their potential as a solution to mineralizing especially recalcitrant compounds in the environment, "Decontamination of Wastewaters Containing Synthetic Organic Dyes by Electrochemical Methods: A Review." This led me to pursue the investigation in my extended essay on the topic of electrochemical advanced oxidation processes and the effect they have on azo dyes such as Allura Red AC and Azo Grenadine. In order to evaluate the effect of this process, I made the decision to do a comparison of the two dyes. This led me to the question, “How does the effect of electrochemical advanced oxidation processes vary between Allura Red AC and Azo

Within the experiment, pure catechol was mixed with different concentrations of catechol oxidase and the rate at which each solution produced benzoquinone was measured. The amount of benzoquinone made throughout the trials was measured by using a colorimeter to measure the level of “brownness” of the liquid. The colorimeter worked by shining a light through the liquid and then measuring that light on the other side to see how much of it was absorbed. In this experiment, absorbance of blue light was measured because blue light is absorbed by the color brown. The amount of blue light absorbance was measured every 15 seconds for five minutes. Because enzymes speed up reactions, more enzymes would cause the reaction to be even faster.1

The great Green Bay Packer coach Vince Lombardi said, “The only place success comes before work is in the dictionary”(Brainyquote). Success is a moment that must be worked for first. It takes a lot of work to be an NFL running back. The mixture of blood, sweat, tears, hard work, passion, pain, adversity, and a love for the game is the combination necessary to have a career as an NFL running back.

In order to see the effects of pH and temperature on the enzymatic reaction of catechol oxidase when separated from potato tissue. We used a spectrophotometer to measure how much blue light energy is absorbed by benzoquinone. Benzoquinone is a product of catechol when it has been oxidized by different temperatures and pHs. We hypothesized that the benzoquinone absorbance rate would be faster when the pH added to the cuvettes were greater than the pH of the potato tissue. The pH of the potato tissue was pH 6. Our results show that pH 7 had the faster absorbance rate, slightly slower at pH 4, and slowest at pH

The purpose of this experiment was studying the reaction rate of crystal violet with NaOH by observing the concentration using the MicroLAB colorimeter, monitoring how the reactant concentration affects reaction rate constant, determining the reaction order, and to calculate the reaction pseudo rate constants and the true value rate constant. The rate of the reaction of crystal violet with NaOH is given by the generalized rate law, rate = k [OH-]x [CV]y where k is the rate constant for crystal violet and CV is crystal violet, C25H30N3+. Where x and y are the reaction orders. The equation can be rewritten as:

With all living organisms, a process known as cell respiration is integral in order to provide the body with an essential form of energy, adenosine triphosphate (ATP). Oxygen, although an essential part of this process, can form reactants from colliding with electrons associated with carrier molecules. (pb101.rcsb.org, 2017). Hydrogen peroxide is an integral product of this reaction but is known to impose negative effects on the body if high levels are introduced. Explicitly, this reaction is caused “If oxygen runs into (one of these) carrier molecules, the electron may be accidentally transferred to it. This converts oxygen into dangerous compounds such as superoxide radicals and hydrogen peroxide, which can attack the delicate sulphur atoms and metal ions in proteins.” (pdbh101.rcb.org, 2017). Research has suggested that the hydrogen peroxide can be converted into hydroxyl radicals, known to mutate DNA, which can potentially cause bodily harm due to DNA’s role in the synthesis of proteins. These radicals can cause detrimental effects on the human body, and studies have suggested a link to ageing. Due to the harmful effects of these H2o2, it is important that the body finds a way to dispose of hydrogen peroxide before concentrations are too great.

Catechol, in the presence of oxygen is oxidized by catechol oxidase to form benzoquinone (Harel et al., 1964). Bananas and potatoes contain catechol oxidase that acts on catechol which is initially colorless and converts it to brown (Harel et al., 1964). In this experiment, the effect of pH on the activity of catechol oxidase was conducted using buffers ranging from pH2 to pH10. Two trials were conducted due to the first trial results being altered by an external factor. The results were acquired by taking readings every 2 minutes for 20 minutes from a spectrophotometer and then recorded on to the table. The data collected in the table were then made into graphs to illustrate the influence of pH on the catechol oxidase catalyzed reaction. After analysis, the data revealed that pH did have a significant influence on the enzyme as recorded by absorbance per minute. However, the data was collected was not accurate due to external factors, thus the results are debatable and should be experimented again for validation.

Abstract. Peroxidase is an enzyme whose main function is to break down hydrogen peroxide. It is rich in content in the organism Brassica rapa, or the turnip. The purpose of this study was to investigate and observe the effects of pH, temperature conditions and the inhibitor Hydroxylamine on Peroxidase ‘s ability to break down Hydrogen Peroxide. By observing the absorbance change of different solutions of differing concentrations of Peroxidase, pH5 buffer and Guaiacol, a color changing dye, enzyme activity was measured. Each solution was exposed to a unique temperature, pH or Hydroxylamine. The temperatures tested were 5℃,

Peroxidase is an enzyme that breaks down hydrogen peroxide in our cells (Bansal et. al., 2016). Peroxidase is essential in life because hydrogen peroxide can cause damage to the cell. Hydrogen peroxide is the substrate to the peroxidase enzyme, where it binds to the active site and is broken down into water. In order to monitor the breakdown of hydrogen peroxide, the colorless dye guaiacol binds to the peroxidase and becomes oxidized as hydrogen peroxide is reduced to water, which then turns brown. Hydroxylamine is an inhibitor that has a similar structure to hydrogen peroxide. When hydroxylamine binds to the active site of peroxidase, it inhibits hydrogen peroxide from binding, thus preventing the breakdown of hydrogen peroxide (Lab Handout,

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.

Turnips and horse radish roots are rich source of this enzyme. In this experiment, we would carry out a reaction between hydrogen peroxide and guaiacol which is colorless dye, using peroxidase as a catalyst, to produce water and an oxidized form of guaiacol which is brown. The formation of brown color would serve as an indicator that the breakdown of Hydrogen Peroxide took place. The enzyme activity would be directly proportional to the brown color intensity. The color intensity would be measured using a spectrophotometer and standardized to find the corresponding concentration for each absorbance unit.