Austin Peay State University Department of Chemistry CHEM 1021 BREAKING DOWN STARCH USING SALIVARY AMYLASE Caution: You will be using a Bunsen burner and glassware to create your own constant water bath. Appropriate caution should be exercised when dealing with the Bunsen burner‚ hot water‚ and glassware. Purpose: Many plants store their energy in the form of starch‚ a polysaccharide made from repeating units of the monosaccharide glucose. Our bodie
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HINTS ON WRITING YOUR REPORT Title: Enzyme activity Objective: To investigate the effect of temperature on amylase activity Design principle Background: Amylase activity products? (show the equation) Which factors will affect enzyme activity? How to study the rate of reaction? (e.g. rate of disappearance of substrates or rate of formation of products) Independent variable: temperature of reaction mixture or at which the enzymatic reaction occurs. It can be varied by setting water bath at
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pH Affecting on Amylase Enzyme Is there a difference in the concentration of pH in the amylase enzyme activity? The null hypothesis would be that there will be no difference in the concentration of pH and alternative hypothesis would be that there will be a difference in the concentration of pH. The predication if that there will be a difference in the concentration of pH. The pH affects on enzyme activities‚ one of the enzyme that was used in the process was amylase. When a serial dilution was
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are amylases? Amylases are enzymes that break down starch or glycogen. Amylases are produced by a variety of living organisms‚ ranging from bacteria to plants and humans. Bacteria and fungi secrete amylases to the outside of their cells to carry out extracellular digestion. When they have broken down the insoluble starch‚ the soluble end products such as (glucose or maltose) are absorbed into their cells. Amylases are classified based on how they break down starch molecules i. α-amylase (alpha-amylase)
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sugars were found and not starch‚ is because saliva contains an enzyme known as salivary amylase which catalyses the breakdown of starch to produce sugars such as maltose (Sherwood‚ 2013). When testing the effect of the salivary amylase concentration‚ we observed that the solution containing the most saliva (3ml)‚ become colourless faster than the solution which contained the least saliva (1ml). This proves that an increase in enzyme concentration (increase in saliva)‚ will cause an increase in the
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3 SUBJECT: Biology TITLE: Enzymes AIM: To investigate the effect of substrate concentration on the enzyme amylase INTRODUCTION: Enzymes are perhaps one of the most important proteins of the human body. Enzymes such as amylase‚ an enzyme that breaks down carbohydrates‚ work by means of surface catalysis. In other words‚ the surface of the enzyme enables other molecules to react in a manner they would not be able to without the surface of the enzyme present. Enzymes achieve this by lowering the
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Enzymes are a type of protein. They are catalysts meaning they speed up the rate of the reaction. Enzymes activity depends on the concentration of the substrate‚ temperature and the pH. The more concentrated the substrate is the more reactive the enzyme is. The optimal pH for an enzyme is 7.5 and the optimal temperature for an enzyme is 53 Celsius. Extremes in the temperature and the pH of an enzyme can denature therefore destroy it. The enzyme that is in this experiment is Amylase. Amylase is found
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Abstract: Enzymes are specific-type proteins that act as a catalyst by lowering the activation energy of a reaction. Each enzyme binds closely to the substrate; this greatly increases the reaction rate of the bounded substrate. Amylase enzyme‚ just like any other enzyme‚ has an optimum PH and temperature range in which it is most active‚ and in which the substrate binds most easily. The purpose of this experiment was to determine (1) the reaction rate of an amylase enzyme in starch and (2)
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of pH on amylase activity This practical allows you to: * discover how pH affects the rate of an enzyme controlled reaction * evaluate the experimental procedure Procedure SAFETY: Follow 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
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iodine can be measured by using a spectrophotometer. α-amylases are found in saliva‚ pancreatic juice‚ human breast milk‚ serum and certain tissues such as the liver. This enzyme catalyzes the hydrolysis of α (1-4) linkages in starch by breaking it down to maltose and some glucose. As the starch is broken down‚ the coiled structure of α-amylase is unfolded. Therefore‚ iodine will no longer be able to form the blue complex with the α-amylase. It can be assumed that the decrease in color (absorbance)
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