Activity from pH and Concentration Abstract Enzymes are the key to many of the chemical reactions that our bodies depend on to live. Without enzymes‚ we would not exist. These biological catalysts speed up the reactions as well as reduce the amount of activation energy needed to complete the process. Knowing how important enzymes are to us‚ it is important to realize what they require to function. They need select conditions and rates to work right. These conditions can range from what level of pH to use
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phosphate solution using a pH meter and construct a titration curve of an amino acid to determine the pka values of its ionisable groups to identitfy an unknown amino acid. Method: The ratio of [HPO42-] to [H2PO4-] required to produce buffer solutions at pH values 5.9‚ 6.9 and 7.9 were calculated. 0.1M of H2PO4- and 0.1M HPO42- were used to mix appropriate volumes to 25mL of each of the buffer solutions. The calibrated pH meter was used to measure and record the pH of each buffer solution and
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100M Tris buffer‚ the calculated amount of ingredients brought the solution to a pH of 7.0‚ but the desired pH was 7.50. Discrepancies between the theoretically calculated amounts and the actual measured amounts of ingredients are likely to be the biggest source of error. Dilution affected our 0.0100M Tris buffer by decreasing its pH. The buffer was originally set to a pH of 7.48‚ but the pH gradually moved down by a pH unit of about 0.1 after each dilution. This is agrees very well with what we expected
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Tutorial 1 1. pK = 3.4 DH = ASA Plasma pH = 7.3 Stomach pH = 1.5 = 10pH – pK = 10pH – pK = 107.3 – 3.4 = 101.5 – 3.4 = 7943.2823 = 0.01259 [Total Drug] = [D-] + [DH] [Total Drug] = [D-] + [DH] = 7943.2823 + 1 = 0.0126 + 1 = 7944.2823 = 1.0126 [Total Drug] in stomach relative to plasma = 7944.2823/1.0126 = 7845.43 Conclusion: High absorption of ASA from the stomach lumen. Absorption from stomach is 7845.43 times
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and NaOH and monitoring the pH change of the various solutions. The data collected shows that the buffer systems made with sodium acetate and acetic acid were effect when titrated with the strong acid and the strong base. Comparison of all the solutions shows that the concepts of buffers holds true for the results from the experimentation. Introduction The main objective of this lab was to test the ability of buffered and unbuffered solutions to resist changes in pH with the addition of strong
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! Affect of pH on Porcine Pancreatic Alpha-Amylase Activity Introduction Proteins function in a variety of different ways‚ and one of their fundamental tasks is to act as enzymes. Enzymes are extremely important in controlling reaction speed (by initiating and regulating biological activity)‚ cell communication‚ and growth. One particularly significant enzyme is amylase‚ which catalyzes the hydrolysis of alpha glycosidic linkages of amylose‚ starch components‚ and other oligosaccharides (Qian
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reactions there are enzymes‚ biological catalysts‚ which help speed up metabolic reactions by lowering the energy barriers without being used up or altered in the reaction. (Campball‚ 2008) Every enzyme has an optimum pH at which it is most active. An increase or decrease in the pH of the solution will cause the enzyme to have a change in its three dimensional shape. If an enzyme is placed in an environment that is to basic or acidic the reaction will take longer to digest the starch because the
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In this lab‚ the pH of flat sprite and a fresh sprite are compared two ways: one way was to record the pH directly with a digital pH probe and the other was to calculate the concentration through titration. Because the reaction is a neutralization reaction‚ the concentration of can be calculated if the concentration of is known. At the end of the titration‚ the moles of will equal the moles of and the pH is expected to be greater than 7 because the found in sprite is weak and is a strong
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studied by steady shear and dynamic oscillatory viscoelasticity‚ intrinsic viscosity measurements and microscopic observation. The pH of cornstarch dispersion was adjusted between 6.0 and 3.0. The viscosity of the pastes was increased by lowering the pH (between 5.5 and 3.6)‚ while the viscosity of samples with pH below 3.5 decreased further than that of the control (pH ) 6.3). Citric acid promoted the collapse of starch granules; however‚ adding excessive citric acid led to the hydrolysis of glucose
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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
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