because they contain starch. The optimum pH for pancreatic amylase is the pH of 7. In the experiment I have used buffer solutions with the pHs of 2.8‚ 4 and 6.5. I have also used iodine and starch. Normally‚ iodine is orange-yellow‚ however when you add starch to it‚ the solution will turn blue-black. Aim: The aim for this experiment is to investigate how the different buffer solutions work on the enzyme amylase. This will be investigated by using iodine and by timing the experiment using the
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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 to neutral. When pH was acidic or basic‚ the
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Joanne Kathleen Saori T. Suzuki‚ Laurent Santos‚ Val Justin D.M. Tongco* College of Science‚ University of Santo Tomas‚ Manila Philippines Abstract Salivary amylase‚ found in humans‚ is enzyme that catalyzes the hydrolysis of starch into simpler compounds. Its enzymatic activity is affected by several factors‚ such as temperature and pH. The rates of enzymatic activity of salivary amylase in different temperatures and pH were measured and resulted to be very near 50 C and 7 respectively. However
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Experiment 1: "A cis to trans conversion" Saturday‚ June 25‚ 2005 4:19 PM Notes on Theory • Alkenes o They are hydrocarbons with a C=C double bond • Double bonds are stronger and more reactive than single bonds o Hydrocarbons with double bonds used to be known as "olefins"‚ because they had an oily appearance • "Oleum" means oil • "Ficare" means make • Isomers o Geometric isomers have the same molecular formula‚ but a different geometric arrangement • They also have different physical properties
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required to work some of the problems in this chapter. 1. In which one of the following solutions will acetic acid have the greatest percent ionization? A. B. C. D. 2. Which one of the following is a buffer solution? A. B. C. D. E. 3. 0.40 M HCN and 0.10 KCN 0.20 M CH3COOH 1.0 M HNO3 and 1.0 M NaNO3 0.10 M KCN 0.50 M HCl and 0.10 NaCl Which one of the following combinations cannot function as a buffer solution? A. B. C. D. E. 4. 0.1 M CH3COOH 0.1 M CH3COOH dissolved in 1.0 M HCl 0.1 M CH3COOH
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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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react with cell organelles Due to the density and size of sucrose molecules‚ it is able to suspend pellets for configuration while providing a solution where the centrifugation can be better balanced Sucrose offers a liquid medium in which less dense fractions can be poured off as supernatant at the end of each centrifugation step. 0.25M sucrose solution is isotonic and therefore inhibits the premature lysis of the mitochondria membranes during the fractionation process (centrifugation) 2) List
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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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