insert into cuvettes‚ a micropipette was then used to obtain 0.5ml of catechol and 0.5ml of the catechol oxidase. The pH buffer was made first to avoid any denaturation of the catechol oxidase. Our positive control for this experiment was pH 7 because that is the pH level of most cell membranes in the cytoplasm (Whitson‚ 2016.) Our negative controls varied for each pH buffer‚ but all “blank” cuvettes contained 0.5 ml of catechol oxidase and 4.5ml of the pH buffer. We prepared the negative control
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activation energy of the reaction. Enzymes are precise and catalyze only detailed reaction. Specificity is an outcome of active site of enzyme that acts on the substrate. Catecholase‚ which catalyzes a reaction in which catechol‚ then catechol becomes the product called benzoquinone‚ which is a reddish-brown color‚ which make it easier to determine the quantity that has been formed. (Dickey). Moreover‚ the enzyme activity is persuaded by ph‚ plus temperature. Change in ph will have effect on hydrogen
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Three test tubes were used: the first one containing water and catechol only‚ the second one containing water and enzyme only‚ and the third one containing water and both catechol and enzyme. The results showed that the first tube containing only catechol had a low change in absorbance‚ the second tube containing only the enzyme also had a low change absorbance but higher than the first one‚ and the third tube containing both catechol and enzyme had a high change in absorbance. The higher the change
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activity with 1-11 pH‚ varying temperature‚ catechol solution‚ hydroquinone solution‚ and different measurements of catechol. In Figure 1A and 1B‚ pH levels were tested with potato extract to see how pH would affect the amount of Benzoquinone is formed in the potato. Although it was hypothesized that enzymes would form Benzoquinone better in acidic pH levels‚ the absorbency recorded stated that the higher the absorbency‚ the higher amount of Benzoquinone was produced. The hypothesis wasn’t fully supported
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Detection of Benzoquinone: - Stations were set up having three test tubes‚ a wax marker and a ruler for measuring. We were to indicate measurements on each test tube at 1cm and 2cm from the bottom. We then identified each test tube as 2a‚ 2b‚ and 2c. - We filled each test tube with the following: 2a with 1cm of potato extract containing Catechol Oxidase and 1cm of 1% Catechol Solution; 2b with 1cm of potato extract containing Catechol Oxidase and 1cm of dH2O; 2c with 1cm of 1% Catechol Solution and
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chemical reaction. Catecholase catalyzes the reaction rate of catechol oxidation. Catechol is found beneath the skin of many plants such as apples and potatoes. When it is exposed to air‚ the oxygen in the atmosphere oxidizes it to benzoquinone‚ 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 catechol in the produce from oxidizing as quickly as it would at room temperature
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filled with 3 ml of their corresponding pH phosphate buffer. 10 drops of catechol and 10 drops of potato juice‚ which contains catecholase‚ were added to each of the seven tubes. The tubes were covered with Parafilm‚ stood for 5 minutes‚ and mixed every minute. After the 5 minutes‚ data was recorded based on the intensity of color with the “0‚+‚++‚+++”
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lowering the activation energy (Reece and Campbell). Because enzymes are so specific in their shape‚ they will only work on substrates that fit‚ and no others. In this lab we utilized Catechol Oxidase as our enzyme‚ and Catechol as our substrate. When exposed to oxygen catechol gradually changes to benzoquinone‚ catechol oxidase speeds up this reaction. We tested the effects of temperature‚ pH‚ and inhibitors on this enzyme system. This was all accurately timed and measured to ensure proper results
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3) Change in color of the solution The amount of potato extract‚ pH solution‚ and catechol used (1 cm +/- .1cm) Size of the test tubes Amount of time allowed for the catechol to sit with the potato extract and pH solution (20 minutes with 5 minute intervals for observation) Materials: 4 test tubes Test tube rack Wax pencil Small ruler Buffer solutions of pH 10‚ 7‚ 6‚ and 3 Potato extract Catechol Procedure: 1. Using the small ruler and the wax pencil‚ three markings are made on
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in colour of solution‚ Inhibitors prevent the reaction of the enzymes with substrates‚ the enzyme is relatively specific. Aim: To design and conduct an experiment to demonstrate enzyme activity of Polyphenol Oxidase and Peroxidase when mixed with catechol‚ caffeic acid‚ pyrogallad‚ tyrosine‚ guacol‚ and water‚ to test the effect of inhibitors on these enzymes‚ to show the specificity of Polyphenol Oxidase and also the effect of amylase on starch. Theory: Enzymes are large molecules that increase
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