Variables: Independent: pH‚ enzyme concentration‚ substrate concentration and enzymatic activity. Dependent: the reaction rate Control variable: temperature and amount of substrates and enzymes added. Materials: Phosphate Buffers Beaker Catechol Potato Juice Parafilm Test Tubes Procedure: To study the effect of temperature: 1. Three different test tubes where filled with 3mL of phosphate. 2. They were set in three different temperature settings. First tube was placed in an ice-water
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were created in 2 mL microcentrifuge tubes using a two-fold serial dilution. The catechol concentration of the samples ranged from 8.00 mM to 0.065 mM. Eight uninhibited samples were prepared by mixing 10 μL of extracted enzyme
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Dihydroxybenzenes Industry Overview 6 1.5 Dihydroxybenzenes Industry History 7 1.6 Dihydroxybenzenes Industry Competitive Landscape 8 1.7 Dihydroxybenzenes Industry International and China Development Comparison 10 Chapter Two Dihydroxybenzenes(Catechol‚Resorcinol‚Hydroquinone) Market Data Analysis
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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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then added 0.5 mL of substrate (catechol) into each test tube. In the instructions it says to apply your 0.5 mL of tyrosinase (potato extract) as well but you have to blank the spectrophotometer before. The results from this experiment confirms that our hypothesis of a neutral pH displaying a stronger impact on tyrosinase is true. According to our results the pH levels at a more neutral state showed a greater reaction compared to pH levels
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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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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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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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