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Temperature Of Peroxidase Lab Report

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How Temperature Effects the Catalytic Ability of Peroxidase from Potatoes Abstract In order to determine if temperature affects the ability of Peroxidase to react, we measured the reaction rate of the same solution exposed to different temperatures. Solutions were exposed to a 4-degree, 22-degree, 32-degree, or 60-degree Celsius environment then measured by a spectrophotometer. The solution left in the 22-degree environment had the highest reaction rate, while the solution exposed to the 60-degree water bath was not able to react at all. We also tested to see if Peroxidase was able to recover its catalytic ability after being exposed to sub optimal temperatures. After being brought to optimal temperatures the solutions were still able to react, …show more content…

That mixture was then filtered through a coffee filter. Nine test tubes were prepared in order to perform this dye coupled reaction. One contained 5.0ml of the potato and pH buffer mixture, 2.0 ml of hydrogen peroxide, and 1.0 of guaiacol to serve as a blank for the spectrophotometer. Four test tubes were filled with 2.0 ml of hydrogen peroxide and 1.0 ml of guaiacol, used for measurement by the spectrophotometer, each. The last four were filled with 4.0 ml of the potato and pH buffer mixture and 1.0 ml of peroxidase. Each were labeled and paired up with one containing the other set of ingredients. To determine if temperature affected the performance of peroxidase each set was isolated in a specific temperature. Two of the test tubes were set in a refrigerator of 4 degrees Celsius, another pair was left to sit in room temperature of 22 degrees Celsius, the third pair was left in an incubator of 32 degrees Celsius, and the last pair was left in a water bath of 60 degrees Celsius. All four sets were left in their designated temperature for 15 minutes. Before the 15 minutes were up the spectrophotometers were set at 470 nm and zeroed out using the blank. After the 15 minutes, each pair was removed from their assigned temperature and mixed with its partner. The mixed solution was then poured into the appropriate tube and placed in the spectrophotometer for 120 seconds. As peroxidase was broken down a brown color appears and is measured by the spectrophotometer. The absorbance readings were recorded every 20

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The temperature in our experiment was not very high which didn’t result in denaturation of peroxidase. The temperature seemed to be a constant that didn’t affect the experiment. If the temperature was higher in pH 3 and low in pH 10, then it would cause pH 3 to denature even more which would make the pH 3 total about 4.0. Substrate concentration basically means the amount used for the substrate. The substrate in our experiment was 0.1% hydrogen peroxide.

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Fill each cuvettes with its respective solution. Turn on the spectrophotometer, so it can warm up then calibrate it to 0% absorbance. Put the corresponding extract blank and set the spectrophotometer to 100% transmittance, then calibrate it to 540 nm. Once catechol is added in the cuvettes, make sure the solution is mixed. Place carrot cuvette in the spectrophotometer and record the resulting transmittance.

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ABSTRACT To catalyze a reaction, an enzyme will grab on (bind) to one or more reactant molecules. In this experiment we examined how increasing the volume of the extract added to the reaction would affect the rate of the reaction. The enzyme used was horseradish peroxidase which helps catalyze hydrogen peroxide. Using different pH levels, the absorbance rate of the reaction was measured to see at which condition the enzyme worked best. The rates of absorption were calculated using a spectrophotometer in 20 second intervals up to 120 seconds.

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These factors include the pH and the temperature of the solution (1). Most enzymes have a preferred temperature and pH range (2). The preferred temperature for catalase falls between the ranges of thirty five to fifty degrees Celsius (4). Temperatures that are too high denature the enzyme and halt the enzyme’s activity (2). Catalase denatures starts to denature at fifty five degrees Celsius (2).

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First, it was hypothesized that test tube "A", the control, would not show any red concentration, test tube "B" which contains supernatant II would show the most red concentration and test tube "C" which contains sediment II would only show a little red concentration. The second hypothesis states that the raw corn kernels would have mitochondrial activity while the boiled corn kernels would not. The last hypothesis interprets that the "gunk" and sediment I will both contain starch granules. It was only expected to find mitochondrial activity in Supernatant II. Unfortunately, after performing this experiment, we were not able to support this hypothesis and come up with a conclusion.

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This was accomplished by grinding spinach leaves which allowed for us to have the pigments migrate along a piece of filter paper with the help of an organic solvent. The varying masses and polarities of the different pigments causes them to segregate themselves to different areas of the filter paper. The use of a spectrophotometer then assisted in the analysis of each pigment band by returning absorbance values before the data was recorded in a

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Effect of Yeast on Temperature on Hydrogen Peroxide Solution in Water Khalid Al Sabeeh Ms. Dobrin 11-G Chemistry HL Jan 5, 2015 Abstract: Within this lab yeast was added to hydrogen peroxide solution in water. Temperature was the factor to be tested. In all trials, the initial and final, when yeast was added temperatures increased by 10˚C respectfully per trial.

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Increase in temperature beyond optimum level causes a sharp decline in the rate due to denaturation of the enzyme. At around 40 degrees Celsius most enzymes have an optimum temperature and when temperatures are reduced below freezing point enzymes are inactivated but they gain their catalytic properties once the temperature is increased. Figure: (www.bbc.co.uk)

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From this experiment, the data gathered support the hypothesis. For the first trial, in the cold hydrogen peroxide the reaction lasted six minutes and twenty-one seconds, in the warm hydrogen peroxide the reaction lasted two minutes and fourteen seconds, and in the room temperature hydrogen peroxide the reaction lasted for two minutes and thirty-one seconds. During the second trial, in the cold hydrogen peroxide the reaction lasted five minutes and fifty-seven seconds, in the warm hydrogen peroxide the reaction lasted one minute and fifty-five seconds, and in the room temperature hydrogen peroxide the reaction lasted for two minutes and sixteen seconds. The warm hydrogen peroxide reactions were about four minutes faster than the cold hydrogen

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These enzymes have a secondary and tertiary structure and this could be affected by increases and decreases in temperature beyond the optimum temperature of the enzyme to work in. Mostly enzymes are highly affected any changes in temperature beyond the enzymes optimum. There are too

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The 3 concentrations of enzymes were 0.5 ml, 1.0 ml, and 2.0 ml of turnip extract, while the substrate consisted of 0.1ml, 0.2 ml, and 0.4 ml of hydrogen peroxide. In a separate tube, the control was made up of turnip extract and guaiacol, known as the color reagent. This was recorded the absorbance every 20 seconds for 3 minutes.

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The enzymes are denatured because higher temperatures cause the enzyme

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1. The reaction is an oxidation and reduction reaction. Bubbles were observed because oxygen is being release from the reaction as a gas as part of the reduction part of the reaction. Enzymes work efficiently at a body temperature of 37o C therefore if the enzyme was boiled before adding it to the peroxide there would be no bubbles due to the fact that the enzyme would be denatured.

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In the same manor as the temperature decreases it slows down the enzymes not allowing them to break down the solution in a timely matter. The amount of pH in the solution didn’t match the hypothesis for this experiment. The fastest absorption rate of the enzymes was at the pH level 7 which was predicted to be the slowest rate. It absorbed the most at the pH level because it was at a neutral, not being to acidic which would slow down the enzyme break down. From this experiment it shows that the highest concentration of enzymes is what gives the fastest rate of enzyme absorption.

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