The Effect Of Peroxidase Production On Stressed Plants Essay

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 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 type of peroxidase is used is called turnip peroxidase. Turnip peroxidase is made up of Guaiacol and hydrogen peroxide. The reactants to the product are turnip peroxidase or called tertraguaiacol and water. The color of the react is brown. In the experiment was conducted there were baseline experiment, temperature, pH, 10X substrate, Inhibitor, and half the amount of enzyme.

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 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

3. We measured 2.5 mL of turnip peroxidase (the enzyme) and 10 mL of neutral buffer (pH 7) with a syringe and disposed it into test tube ENB.

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.

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 experiment was to simply measure oxygen production rates released from decomposed hydrogen peroxide under different conditions (concentration of enzymes, temperature, and PH level).

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

will be working at the pH 7 the majority of the time and our bodies

Observing how the enzyme catalase found in chicken and beef livers breaks down hydrogen peroxide at varying pH levels and temperatures.

Sulfuric acid - was used to stop the reaction with catalase and hydrogen peroxide. It denatured the enzyme (catalase) and halted the reaction so the amount of hydrogen peroxide decomposed could be measured.

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 enzyme catechol oxidase, extracted from masticated potato (Solanum tuberosum) lowers activation energy, as it is a catalyst. This enzyme can react with catechol to produce benzoquinone and water. Catechol oxidase is tested against a multitude of phosphate buffers, acidic, neutral and basic pH values, and chilled temperatures to hot temperatures. The purposes of these testes were to determine the optimal temperature and pHs at which catechol oxidase performs at. The method to measure results was the usage of a spectrophotometer (Vernier Spectrouis Plus). The spectrophotometer measures the absorbance levels of the pigment excreted when catechol oxidase undergoes a reaction. The high the absorbance, the more products produced and vise versa. The highest absorbance for the catechol oxidase submitted to different temperatures measured an average 0.6018 nm, when at 20 C. The highest absorbance for the catechol oxidase submitted to different pH values measured two averages of 0.658 at pH 6 and 0.6464 at pH 7. The conclusion taken from the available data explains that the optimal pH for catechol oxidase was between pH 6 and 7 and the optimal temperature was at room temperature at 20C.