Peroxidase Temperature Lab Report

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

peroxide (H2O2). The enzyme breaks H2O2 into water and oxygen. The production of the oxygen

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

Temperature can affect the reaction of catechol oxidase by speeding up or slowing down the reaction. I was able to see what happened to the absorbance after changing the temperature of the catechol oxidase solution. I did this by heating and cooling the solutions to measure the absorbances in hot, cold, warm, and room temperature. Then the data was compared to see how the temperature effected the solution. The catechol oxidase solutions reacted best in room temperature (twenty-three degrees Celsius) and the worst in the cold (zero degrees Celsius). I concluded that temperature really does affect the way catechol oxidase reacts.

The data in proves that our hypothesis was correct. When we increased the temperature to 35°C, the the enzyme activity increased because kinetic energy increased, increasing the collisions between the substrate and the enzyme, and thus creating a higher chance of reaction. When we increased the temperature to 45°C, the enzyme activity decreased as the enzyme became denatured,because the atoms in the enzyme had enough energy to overcome the hydrogen bonds between the R groups that give the enzyme its shape From our data, we could conclude that the optimal temperature of turnip peroxidase is around 35°C and around 45°C, it will start to denature.

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

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.

In one tube went 0.1 ml guaiacol, 0.2 ml H202¬ and 4.7 ml dH20 for a total of 5 ml. In the other test tube 1.0 ml of peroxidase and 4.0 ml dH20 was combined for a total of 5 ml. The second part of this test was to observe the reaction rate between the peroxidase enzyme and the hydrogen peroxide substrate with guaiacol as the reducing agent every 20 seconds for 10 minutes. The contents of the two test tubes were mixed together and then transferred some of the mixture into a cuvette that could fit into the spectrophotometer. The liquids were combined, poured into the cuvette, put into the spectrophotometer and its absorption rates were recorded every 20 seconds for 10 minutes.

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

In this study, the effects of temperature and pH were measured on the catalytic ability of the enzyme catechol oxidase (also known as tyrosinase, diphenol oxidase, or polyphenal oxidase). Enzymes are defined as catalysts in biological systems that lower that energy of activation or Ea of a reaction. When a substrate bonds to a the active site of an enzyme, this forms an enzyme-substrate complex. An enzyme substrate complex consists of one or more substrates bonded to the enzymes active site, which changes shape slightly when bonded to, so as to appropriately fit the substrate(s). This slight change in enzyme shape is called induced fit.

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.

Enzymes are catalysts that lower the activation energy required to start a biological reaction and affects the rate of the rection. The enzyme can become denatured when its surroundings change in temperature or pH. Molecules in the environment could also affect the enzymatic activity. Inorganic substances known as cofactors and organic molecules known as coenzymes can enhance or inhibit the enzymes activity. The cofactors or coenzymes can act to activate or inhibit the enzymatic activity. Peroxidase is a catalyst that catalyze substrate oxidation when a peroxide is present. The indicator guaiacol is easily oxidized by peroxidases. Guaiacol is used to indicate if the peroxidase enzyme is present in a solution. Turnip peroxidase breaks down hydrogen peroxide into water and

Introduction: Enzymes are proteins that are used to catalyze a chemical reaction by reducing the activation energy necessary for the reaction to take place. Enzymes are highly specific to a particular substrate and function best at optimal pH ranges and temperatures (Bursal, 2013). Peroxidase is an enzyme which can be found in many plants and animals, such as horseradish and humans. The main function of peroxidase is to breakdown hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2) (Groves and Boaz, 2014). A catalytic process is used by peroxidase to breakdown H2O2 which can be harmful to an organism (Zazza et al., 2009). The purpose of this experiment was to test the functionality and efficiency of peroxidase at various pH values to determine the optimal pH of the enzyme. The hypothesis was that peroxidase would perform optimally at a slightly basic pH and

The purpose of this lab was to investigate the effect of enzyme concentration (hydrogen peroxidase), substrate concentration (H2O2), pH, and temperature on the rate of H2O2 breakdown. As seen in all Data Table: Procedure 1 Group A, and Procedure 1: Effect of Temperature on Rate Rate A, if the temperature was increased, then the rate of reaction will increase. This trend held true until the point of denaturation, in which the rate immediately became zero. This was because an enzyme is a protein, so when heated beyond its capacity, its structure was scrambled and therefore became denatured. Besides the fact that the time became infinite, causing the rate to be zero, the data seemed to support Hypothesis 1. This data should have been correct,

The purpose of this lab is to explore the effects of enzyme concentration, substrate concentration, temperature, and inhibitors on reaction rate, respectively. To test each of these factors, four activities were completed. The enzyme from Turnip Extract and the substrate Peroxide were tested. The turnip extract was tested at the following concentrations: .5ml, 1.0ml, and 2.0ml. Peroxide was tested at the following concentrations: 0.1ml, 0.2ml, and 0.4ml. In order to understand the effect of temperature on reaction rate the following temperatures were tested: 4C, 23C, 37C, and 60C. To achieve the desired temperatures, an ice bath and water baths were utilized. Lastly, the effect of the inhibitor Hydroxylamine was tested in the following amounts: 0 drops, 1 drop, and 5 drops. In the experiment, Guaiacol was used to determine the rate of reaction by the absorbance measured. When Guaiacol is oxidized it has a brownish color, the presence of the brownish color indicates Peroxide (substrate of peroxidase) has undergone the reaction and has been reduced to water. By this, the reaction rate can be determined by the color change or absorbance over time. For each activity, a spectrophotometer was used to measure the absorbance. After that, the data for each activity was translated to graph where linear regression was used to analyze the effects. The results of the enzyme concentrations on reaction rate are the following: low enzyme concentration (0.5 ml) had a reaction rate of