Study of Oxalate Ion

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

The purpose of this experiment was to determine the formula of a hydrate CuSO4 specifically, determine the amount of water in that hydrate. In order to do so, a sample of the hydrate was placed in a crucible that sat above a flame. The flame, provided by a Bunsen burner, aided in the evaporation of the water existing in the hydrate. By recording the mass of the hydrate sample before and after it was heated, the water lost due to evaporation could be calculated; 5 molecules of H2O was concluded. This information allowed the formula of the hydrate to be determined: CuSO4 • 5H2O(s)

• Serially dilute the 4 mg/ml solution with buffer A to make working solutions of 400 µg/ml and 40 µg/ml.

But the result met the expectation because the color of the solution was reached the end point by changing from red to blue. The primary errors may occur because of misreading the buret while measuring the volume of EDTA. Another error can affect the result of the experiment was that letting the volume of EDTA excess the ending point; so that the volume of EDTA was overapply that lead error. The last source of error was that our unknown sample had high percentage in mass of Mg2+, so that we need more than 50 ml of EDTA( which was the capability of the buret) to reach the end point. We had to refill the buret while measuring; and also the large volume of solution made the color harder to recognize the end point. That also led to error.

The lab leaders and the Punk Rock Warlord prepared three different concentrations of catechol oxidase by extracting potato juice (because it contains lots of catechol oxidase). Pure catechol, a 5mL test tube, 1mL/5mL

In the blank cuvettes, the 2 mL of pH levels 2,5,7, and 10 were added first, followed by the 1mL of peroxidase. However our experimental cuvettes contained both hydrogen peroxide and guaiacol. Before the cuvettes were placed in the spectrophotometer we added 0.1 mL of H202, followed by 0.02 mL of guaiacol these two substances were added last immediately before they were placed in the spectrophotometer. Para film was placed over the cuvette opening, and the assay solution was shaken and placed into the spectrophotometer where its saturation level was then tested. We recorded the saturation level of the solution every 15 seconds for 3 minutes. This process was repeated two times for each pH level for a total of two trials.

The purpose of this lab was to determine the percent cobalt and oxalate by mass, and with that information, the empirical formula for cobalt oxalate hydrate, using the general formula Coa(C2O4)b.cH2O.

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 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

During a titration the pH of the solution will be monitored using a pH meter from that we get a titration curve. The titration curve is then used to determine the equivalent molecular weight and Ka value of the unknown weak acid, from that we are

1. 10 drops of 1 M K2CrO4 was added to the solution and stirred for about 10 minutes.

In this experiment, the Ksp for calcium sulfate dihydrate, CaSO4·2H2O, by titrating 4 times a calcium sulfate dihydrate solution with diprotic EDTA, H2(EDTA)2-. For each trial we found the Ksp by means of molarities and activities. The results for the Ksp using only molarities was very different than the Ksp using activities. The average Ksp using molarity only was 2.26 x 10-4 and the average Ksp using activity turned out to be 2.31 x 10-5. The actual Ksp however, is 3.14 x 10-5. A percent error of 26.6 % was calculated.

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.

The purpose of this experiment was to determine how much KMnO4 was needed to titrate approximately 1 mL of an Unknow X101 concentrated solution of Oxalic Acid. A standardized KMnO4 solution was used on a known solution of Oxalic acid to help determine the unknown percent oxalic acid in unknown X101. The unknown sample for this experiment was sample x101 which theoretically was a % Oxalic Acid dehydrate sample but, the average of all three trials determined it to be a 6.7% percent Oxalic acid.

2cm of a solution was tested and added 2 cm of 10% of potassium hydroxide solution and the test tube was shaked.