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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________________________________________________ Introduction: What was your null hypothesis? be specific A change in temperature in the reaction of catechol and catecholase will not change the absorbance of reaction over time. What was your alternative hypothesis? be specific As the environment and temperature is changed from 0 °c to 20°c to 95°c‚ the absorbance of catechol and catecholase reaction will increase over time. The rate of reaction increases as the temperature increases. Results: What were the
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The first part of the experiment was broken into three sections. The first section showed the pH and color changes that an enzyme can create. It was predicted that when potato extract‚ the enzyme‚ was added to catechol‚ the substrate‚ an enzymatic reaction would occur. The second section of the experiment demonstrated enzyme specificity. It was predicted that potato extract‚ when hydroquinone was introduced‚ would not exhibit the characteristics of an enzymatic
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competitive inhibitor‚ thereby impeding the forward reaction. In this experiment‚ o-diphenol oxidase‚ an enzyme that causes the browning in fruits‚ was extracted from banana and reaction rate of this was established with various concentrations of catechol‚ the substrate‚ using the Michaelis-Menten‚ Lineweaver-Burk‚ Hanes-Woolf and Eadie-Hofstee plots. The plots were generated using the slope of absorbance readings against time plots. Absorbance can be used to detect reaction rate as this notes color
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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 1cm of dH2O. We tapped each tube to completely mix the solution and recorded the time at zero. - At zero time‚ each test tube was scaled for color concentration
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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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Abstract This lab was performed in order to discover the activity of the enzyme catecholase in different pH levels as well as its absorbance in differently concentrated solutions. A spetrophotometer was used to measure the absorbance of the enzyme catecholase in different pH solutions as well as to measure the absorbance of catecholase in solutions with different concentrations of potato juice and phosphate buffers. Absorbance of the enzyme catecholase was at an optimum level when pH was close
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the potatoes extract in phosphate buffer was made. We began this experiment by measuring seven constant amounts of 1ml of 0.1% catechol using a 1 mL pipet into each seven cuvettes. The catechol is our substrate solution. Next‚ different amounts of phosphate buffer ph.6 of 0.5ml‚ 1.0ml‚ 1.5ml‚ 2.0 ml 2.5ml‚ 3.0ml and 4.0ml were added to each of the solution of the 0.1% catechol. The purpose of adding phosphate buffer pH6 is to maintain the particular ph6 for the polyphenol-oxidase (enzyme)‚
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apple out for long‚ you’ll notice that after a while‚ it will turn brown. The reason for this is an enzyme named catechol oxidase‚ a ubiquitous plant enzymes containing a dinuclear copper center (Klabunde‚ Eicken‚ Sacchettini‚ & Krebs‚ 1998). In this experiment‚ we used two different chelators‚ ethylene diamine tetraacetic acid and phenylthiourea to test which would stop the effects of catechol oxidase on potato cells by testing the change in absorbency over time. Our data supported our hypothesis that
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