Digestive processes in both plants and animals convert starch to glucose‚ a source of energy. Starch is one of the major nutrients in the human died. Its presence in foods and other substances can be detected by the blue-black color produced when iodine solution is added to a sample of the material to be tested [5]. Starch + I2 blue-black color Amylase enzyme Proteins which catalyze the chemical reactions are called enzymes. Non-biological catalysts work at wide ranges of temperature and pH‚
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the buffer was prepared by using the formula as follows: Figure 1: Calculation for prepare 0.1 M potassium phosphate buffer at pH 6 3.4007g of potassium phosphate was weighed and placed in 300 mL beaker. Then‚ 125 mL of water was added into the beaker that contained potassium phosphate. The mixture was dissolved using the stirring rod‚ and then the magnetic stirring bar was placed in the beaker for further dissolve when measuring the pH. The pH meter was used to measure the solution‚ and
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at a carbon fiber microdisk electrode(CFE) was developed for the determination of nicotine. Effects of detection potential‚ concentration and pH value of the phosphate buffer‚ and injection time as well as separation voltage were investigated. Under the optimized conditions: a detection potential of 1.20 V‚ 40 mmol/L phosphate buffer(pH 2.0)‚ a sample injection time of 10 s at 10 kV and a separation voltage of 16 kV‚ the linear range obtained was from 5.0×10–7 mol/L to 1.0×10–4 mol/L with a correlation
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salivary amylase‚ 1ml saliva‚ 9ml distilled water and 30ml of 0.5% NaCl made up the enzyme solution. One percent starch in phosphate buffer pH 6.7 was the buffered starch. The experiment was comprised of two parts. For the first part (effect of temperature)‚ 2 ml of the enzyme solution was placed in a large test tube and labelled as 4℃. In a separate large test tube‚ 2 ml of the buffered starch solution was added. Both test tubes were incubated for 10 minutes in an ice bath with a temperature
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equilibrium to the left This causes the pH to be higher than the pH of the acid solution 9lowering the H3O+ ion concentration 2 Dr. Ali Jabalameli Copyright © 2011 Pearson Education‚ Inc. 1 Chemistry102 5/7/2013 Common Ion Effect Copyright © 2011 Pearson Education‚ Inc. 3 The Common-Ion Effect • Consider a solution of acetic acid: CH3COOH(aq) + H2O(l) H3O+(aq) + CH3COO−(aq) • If acetate ion is added to the solution‚ Le Châtelier says the equilibrium will shift to the left. Aqueous Equilibria
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Research Question How will the addition of different pH buffers to amylase affect the rate of starch digestion measured using starch and iodine? Introduction Amylase is an enzyme found in human saliva and pancreas. It is the digestive enzyme that is needed to breakdown starch molecules. Amylase must be kept at certain conditions to function at its optimum level. This experiment will explore the effect of pH (1‚ 4‚ 7‚ 10‚ and 14) on the function of amylase by using starch and iodine. Usually
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your teacher’s instructions for handling the solutions. Wear eye protection when handling the iodine solution. Investigation * Place single drops of iodine solution in rows on the tile. * Label a test tube with the pH to be tested. * Use the syringe to place 2 cm3 of amylase into the test tube. * Add 1 cm3 of buffer solution to the test tube using a syringe. * Use another syringe to add 2 cm3 of starch to the amylase/ buffer solution. Start the stop clock and leave it on throughout
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| Buffer A | Buffer B | Mass of NaC2H3O2 used to prepare buffer (grams) | | | Volume of buffer prepared (mL) | 100.0 | 100.0 | Molar concentration of HC2H3O2 in buffer (M) | 0.1 | 1.0 | Initial pH of buffer | | | Volume of 0.5 M NaOH to raise pH by 2 units (mL) | | | Volume of 0.5 M HCl to lower pH by 2 units (mL) | | | Volume of 0.5 M NaOH at equivalence point (mL) | | | Data Analysis 1. Write reaction equations to explain how your acetic acid-acetate buffer reacts
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performed to precipitate out LDH and other proteins. Components such as nucleic acids and sugars‚ which are more soluble‚ remained in the supernatant. In this step 0.13g of ammonium sulfate salt was slowly added per each ml of the 40% supernatant as the solution was stirring. Enzyme assay and protein assay were performed. The results indicated 4600±100 unit enzyme activity concentration and 75±2 mg of protein in the 60% pellet (Raw Data tables 1-A‚2). The enzyme assay was performed on the 60% sup as well
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LEE ET AL.: JOURNAL OF AOAC INTERNATIONAL VOL. 88‚ NO. 5‚ 2005 1269 DIETARY SUPPLEMENTS Determination of Total Monomeric Anthocyanin Pigment Content of Fruit Juices‚ Beverages‚ Natural Colorants‚ and Wines by the pH Differential Method: Collaborative Study JUNGMIN LEE U.S. Department of Agriculture‚ Agricultural Research Service‚ Pacific West Area (PWA)‚ Horticultural Crops Research Laboratory Worksite‚ 29603 University of Idaho Ln‚ Parma‚ ID 83660 ROBERT W. DURST and RONALD E. WROLSTAD Oregon
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