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When it is exposed to air, the oxygen in the atmosphere oxidized it to bounciness, which acts as an antiseptic for the plant. When produce is stored in a freezer, it will stay for long without changing color. This is due to the cooler temperature preventing the cathode in the produce from oxidize as quickly as it would at room temperature. (Clapper, A, 2007) When cut open, potatoes turn to a brownish color which indicates enzymatic activity. Delimitation attracted acid (EDIT) is a preservative.

The magnesium and calcium that EDIT binds are the cofactors used by the enzymes of bacteria and fungi that can spoil food. Bounciness reflects light of orange avalanches and absorbs light of green wavelengths, which makes us measure enzymatic activity by measuring light absorbency. There is a hypothesis that enzyme kept at 37 degrees Celsius will show the most absorbency which shows most enzymatic activity. Also calcium and magnesium are hypothesized as the cofactors necessary in the functioning of enzymes in bacteria and fungi that spoil food, due to EDIT binding to them. Clapper, A, 2007) Material and Method Spectrophotometer suspects, A spectrophotometer, 18 ml of cathode solution, 10 ml of enzyme solution, 531 ml of distilled, 2 ml of EDIT and 2 ml of phenyl hairier (PUT) were used as possible chelating agents, 5 labeled pipettes, around 14 pieces of paraffin, skimpiest, cavetti rack, 37 and 60 degree Celsius water baths, one uncooked potato, potato peeler, refrigerated blender, 500 ml of the cold distilled water, and several squares of cheese cloth were used in this experiment.

Method. In preparing the catecholamine extract, a potato was skinned, washed, and then diced. Water was added to the diced potato and blended for two minutes. The solution formed was filtered and the extract stored in a container. Eight individually labeled spectrophotometer suspects were prepared using different mounts of the following reagents: a buffer of pH 7, a 0. 1% cathode substrate, and distilled water. The wavelength of the Spectroscopic 20 spectrophotometer was set at 540 NM.

To calibrate the spectrophotometer at zero absorbency, blank control suspects prepared with no cathode substrate and labeled “tube 1 ” was inverted and inserted into the spectrophotometer. The extract to be tested was added immediately to each suspects before they were placed to the spectrophotometer and each suspects was inverted and placed in the spectrophotometer. The absorbency was read for time zero (to), the ten minute ark (t 10), and each minute in between and recorded.

The suspects received the enzyme solution last to prevent the reaction from increasing until we were ready to begin measuring the reaction. The suspects were shaken frequently to ensure that the contents were properly mixed. After ten minutes, the suspects were removed from their environments. To conduct the cofactors procedure, the suspects were prepared first. Suspects 1, 2, and 3 received all contents other than cathode, at first. Cavetti 1 received 1 ml of enzyme, ml of cathode, and ml of EDIT. Cavetti 2 received 1 ml enzyme, ml cathode, and ml of PIPIT.

Cavetti 3 received 1 ml of enzyme, ml of cathode, and ml of 20th. Cavetti 4 received ml of 20th. The enzyme solution and chelating agent were allowed to sit for a minimum of 10 minutes before the cathode was added, so as to ensure mixing. The suspects were inverted and shaken every 2 minutes to continue mixing. After ten minutes of mixing, the cathode solution was added and initial measurements were taken like in the temperature procedure. Next, the suspects were placed into a 37 degree water bath and ten minutes elapsed before a second set of data was corded.

Two data charts were created to record the data for the temperature and cofactor results. The charts show the absorbency rate for each cavetti for the initial readings and the readings after ten minutes. The blank suspects, in each procedure allow us to calibrate the spectrophotometer. When the spectrophotometer is calibrated with the blanks, we are subtracting the amount of absorbency that occurs when only H2O is present in the cavetti. This allows us to measure the amount of enzymatic activity indicated by absorbency as we control absorbency that is not due to enzymatic activity.

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