Ppo Inhibits Lab Study

And finally into test tube 3, I pipetted 1.0 ml turnip extract and 4.0 ml of water. The contents of test tube 1 was poured into a spectrometer tube and labeled it “B” for blank. “B” tube was now inserted it into the spectrometer. An adjustment to the control knob was made to zero the absorbance reading on the spectrometer since one cannot continue the experiment if the spectrometer is not zeroed. A combination of two people and a stop watch was now needed to not only record the time of the reaction, but to mix the reagents in a precise and accurate manner. As my partner recorded the time, I quickly poured tube 3 into tube 2. I then poured tube 2 into the experiment spectrometer tube labeled “E” and inserted it into the spectrometer. A partner then recorded the absorbance reading for every 20 seconds for a total of 120 seconds. After the experiment, a brown color in the tube should be observed to indicate the reaction was carried out. Using sterile techniques, any excess liquid left was disposed

In the experiment we used Turnip, Hydrogen Peroxide, Distilled Water, and Guaiacol as my substances. On the first activity, Effect of Enzyme concentration of Reaction Rate for low enzyme concentration, we tested three concentrations of the turnip extract, and hydrogen peroxide. For the Turnip Extract I used 0.5 ml, 1.0 ml, and 2.0 ml. For hydrogen peroxide we used 0.1 ml, 0.2 ml, and 0.4 ml. We used a control to see the standard, and used a control for each enzyme concentration used. The control contains turnip extract and the color reagent, Guaiacol. We prepared my substrate tubes separately from the enzyme tubes. My substrate tube

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

This is because each kind of apple has a different concentration of catechol oxidase (Daniela Finkel, 2013). Therefore, each apple has a unique speed at which it will produce benzoquinone, and turn brown.

The first experiment begun by filling a 600-ml beaker, almost to the top, with water. Next, a 10-ml graduated cylinder was filled to the top with water. Once water was added to the beaker and graduated cylinder, a thumb was placed over the top of the graduated cylinder. This would ensure that no water was let out and no bubbles were let into the graduated cylinder. Next, it was turned upside down and fully submerged into the beaker. Then, a U-shaped glass tube was attained. The short end of the glass tube was placed into the beaker with the tip inside of the graduated cylinder. Next, a 50-ml Erlenmeyer flask was received. After, 10-ml of substrate concentration and 10-ml of catalase/buffer solution were placed into the flask. A rubber stopper was then placed on the opening of the flask. After adding these, the flask was held at the neck and spun softly

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.

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.

HRP has been around for a long time and used in a wide variety of products such as food taste enhancer or spices to pharmaceutical products. Horseradish peroxidase is an important heme-containing enzyme that has been studied for more than a century but the first ever recorded observation of a reaction catalysed HRP is found in a note published by Louis Antoine Planche (Veitch, Nigel C 2004). HRP was first detected by Theorell in horseradish roots.Horseradish peroxidase has been known to degrade certain recalcitrant organic compounds such as phenol and substituted phenols, but for the first time it is shown that HRP is effective in degrading and precipitating industrially important azo dyes(Bhuniaet al. 2001).

However one beaker received 100 mL of Deionized water with a molarity of 0.0. Afterwards a cork borer was pushed through the potato and was twisted back and forth. Once the borer was filled it was removed from the potato. Pushing the potato cylinder out of the borer, this this step was repeated six more times in order to get seven undamaged potato cylinders. Using a sharp razor blade, the potato cylinders were both cut to a uniform length of about 5cm, and were removed of their potato skins. The potato pieces were also cut in half to give the cells a greater surface area in which it was easier to absorb the solution. After the cylinders were weighed on a balance and the data was recorded in Table 4. Using the razor blade each potato was cut lengthwise into two long halves. Then the potato pieces were transferred to the water beaker and the time they were submerged was recorded. This step was repeated for all potato cylinders in which the pieces were placed in solutions 0.1 to 0.6 M. The potatoes were incubated for ninety minutes. At the end of the incubation period the time was recorded. Then the potato piece was removed form the first sample. Next potato pieces were weighed the and the final weight was recorded in Table 4. This procedure was repeated until all samples had been weighed and recorded in the chronological order they were initially placed in the test solution. Afterwards the table was completed by recording the

Additionally, Figure S4 illustrates a scavenger study due to pinpoint the most active species, which involve in the oxidation reaction. Corresponding to the graph, the photooxidation of RB5 assessed in absence/presence of scavengers. In this context, tert-butanol, benzoquinone and ammonium oxalate are exploited as, hydroxyl radical, superoxide radical and hole scavengers, respectively. After adding of tert-butanol, the RB5 degradation dramatically suppressed compared to the control solution (without scavengers), almost 80% decreasing in rate is observed in this solution. However, the addition of benzoquinone to the solution displayed a medium effect on dye degradation rate (acted as an inhibitor by 40% inhibition of the dye degradation). The

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.

Data: Effect of Solute Concentration on Osmosis in Potato Cells (for the 6 groups of our class)

Then, each group of students received the necessary materials to complete the experiment. When the students received the cups, they labeled cups to distinguish between the salt solution, distilled water, and control group. After weighing the cups and finding the mass of the cucumbers, the students poured 50 ml of water in one cup, 50 ml of salt solution in the other, and left the control cup empty. Then, the students placed the cucumbers into the cups and waited 30 minutes for the results. After the 30 minutes, the students removed the cucumbers from each solution and dried the cucumbers with paper towels. The students then weighed the cucumbers again and recorded their results. Lastly, the students found the difference from the original mass of the cucumbers and recorded their results.

Ascorbic acid, better known as Vitamin C, is a water-soluble vitamin that is important for the well being of humans and has the ability to inactivate radical compounds (Righetto and Netto, 2006). Ascorbic acid is a cofactor that is present in many enzymatic reactions that occur during biological processes such as digestion, absorption, anti-carcinogenicity, collagen formation, cataract prevention and detoxification (Vikram et al, 2004). Processing of fruits, into fruit juice, often involves a form of heat treatment which reduces the nutritional (vitamin C) content of the product (Mercali et al, 2012). Therefore, the purpose of this experiment was to investigate how prolonged exposure to heat leads to an increased degradation of ascorbic acid in mango juice. The juice was exposed to three treatments; 0, 3 and 5 minutes of being placed in a boiling water hot bath, and the concentration of ascorbic acid was determined via titration with potassium iodate.

Another study that was performed examined different prickly pear juices to examine potential antioxidant effects. The juices picked were the most frequently consumed varieties: red-purple, white-green, and yellow-orange. Methods used determined in vitro effects which only give a rough estimate of in vivo effects, but it was determined that the compounds and how they interact give a better idea of how much of an antioxidant the fruit is overall. In this study the researchers treated mice with a chemical that caused oxidative stress, and given prickly pear juice in order to counteract the effects of the oxidative stress. Blood analysis was used in order to examine the amount of protection the prickly pear juice had given to the mice. The results determined that the red-purple colored juice was a better antioxidant than the white-green and yellow-orange varieties indicating that the antioxidant properties may be due to the polyphenols the juices contain since the red-purple variety is