Lab report April 14‚ 2013 Abstract: In this article‚ we will experiment on the significant in strength of the enzyme by using three different test tubes and measuring the amount of product they give off. To determine this we are going to test the amount of color absorbance by using a special tool to help us understand our results. We will see how our end results show the effect of the amount of concentration we apply to each test tube. The results would be shown by the support of two graphs
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LAB 1: What temperature does the enzyme actually work properly in? (Hypothesis) If the temperature is below 40 but above 20‚ then the liver will show bubbles. If the temperature is raised higher than the optimum temperature‚ then an extreme decline in enzyme activity would occur following by the quick denaturing of the enzyme‚ rendering it is permanently useless. Also about 37°C is body temperature. The liver that was at 25°C had a huge amount of bubbles (a 4 on the scale) and the 0°C
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Abstract The main goal of the enzyme kinetics experiment was to see how the phosphatase-catalyzed hydrolysis of p-nitrophenyl produced p-nitrophenol in the presence of phosphate and fluoride ion inhibitors of various concentrations. The calculated Km constant was found to be 0.22 for all reactions. The Vmax values for each inhibition ion were 0.00986 for the phosphate ion and 0.00436 for the fluoride ion. The inhibitor constant‚ Ki‚ was determined to be 0.0967 for the phosphate ion. The inhibitor
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BIO 5 Lab Report: Lactase Enzymes Enzymes are biological catalysts or assistants. Enzymes consist of various types of proteins that work to drive the chemical reaction required for a specific action or nutrient. Enzymes can either launch a reaction or speed it up. The chemicals that are transformed with the help of enzymes are called substrates. In the absence of enzymes‚ these chemicals are called reactants. Enzymes are thought to have an area with a very particular shape. When a molecule of
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1. Prepare a lactase enzyme solution by dissolving one lactase enzyme tablet in 200 ml of water in a clean 250 ml beaker. Stir until the tablet has dissolved. Use labeling tape to label the beaker: “Lactase Enzyme Solution.” 2. Prepare a “denatured” enzyme solution by pouring 20 ml of your enzyme solution into a heat resistant tube. The test tube must have the words “Kimax” or “Pyrex” on it. If it does not‚ it is not heat resistant and may break! Use labeling tape to label the test tube: “Denatured
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Enzymes are catalytic proteins which speed up the rate of reactions. Every enzyme has a specific function – meaning‚ they can only bind to certain substrates. Because these enzymes are proteins‚ they can be denatured. Enzymes can be denatured by many factors‚ such as pH and temperature. This lab was divided into three parts which examined the effects of pH‚ enzyme concentration and temperature on the rate of which enzymes catalyze. The pH is an index of hydrogen ions. In acidic conditions‚ where
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In this lab the peroxidase enzyme is tested in a dormant avocado seed as well as an avocado seed undergoing the process of germination. A gas pressure will be used to test the seeds and see if the peroxidase enzyme is present in either of the seeds. A catalyst is very similar to track spikes. Spikes increase a runner’s speed‚ as a catalyst speeds up the chemical reaction time in a plant. Neither the catalyst nor shoes are changed in these actions. Enzymes are macromolecules that act like catalysts
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An experiment was run to determine which enzyme (pectinase‚ and cellulase or combinations of the two enzymes) maximizes juice production and would be most cost effective. The proposed hypothesis was if the enzyme‚ pectinase‚ is added to apple juice‚ then the more juice will be extracted than if cellulase were added because pectinase holds the cell wall together and if it is separated apart from each other‚ then the more juice would be able to flow out. The experimental data show that during the ten
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Effect of pH on Enzyme Activity A piece of Solanum tuberosum (potato) was removed and mixed with distilled water in a blender. The resulting solution was filtered through multiple layers of cheese cloth to filter out the liquid by eliminating any large pieces in the solution. The solution created was catechol. Five different solutions were prepared as blanks with each test tube containing 6.0mL of a different pH (pH 4‚ pH6‚ pH7‚ pH8‚ pH10) of phosphate buffer‚ 1.0mL of the enzyme and 1.0mL of water
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Enzymes Reactions to Changes in Substrate and Inhibitors Benjamin J. Mora Coronado University of Texas Rio Grande Valley at Edinburgh Abstract Purpose for the experiments was to test the enzymes in various scenarios and see how changing this would affect the rate of reaction. The enzyme source used in the experiments was Turnip Extract. Concentrations of Turnip extract for activity 1 where o.5ml‚ 1.0ml‚ and 2.0 ml as for the rest of the activities 2 Through 4 stayed at a consistent concentration
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