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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The effect of Lead ions on amylase activity Aim What is the effect of Lead ions on the enzyme Amylase. And does it have an inhibitory effect‚ which causes the substrate‚ in this case starch to be blocked from the reaction process in the enzyme catalyst. Also is the effect reversible or irreversible‚ which is put on the amylase. Method Apparatus and substances required Test tube holder 2% starch solution 6 boiling tubes labelled 1 to 6 1% lead nitrate solution 6 test tubes labelled A to E‚
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but they themselves are not consumed or altered when doing so. These catalysts work best at optimum temperatures and pH’s. The temperature and pH at which the reaction occurs the quickest is the ideal condition for the enzymatic reaction. Alpha amylase converts starch into glucose and when starch is combined with I2KI indicator a dark purple solution forms. As the enzyme breaks down the starch the absorbency will decrease. The absorbency is measured through the spectrophotometer which reads the
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Abstract This experiment was carried out to monitor the ability of the Barley Amylase Enzyme to effectively break down starch in solutions that are increasing in neutral pH. To do this the experiment was carried out so that tubes containing a reaction solution of the Amylase enzyme and starch were simultaneously mixed. The reactions were then introduced to I2-KI‚ which stopped the reactions‚ at two minute intervals. Each of these trials was repeated three times to ensure proper accuracy. After
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and bacterial amylase‚ as well as the optimal temperature needed for the enzyme to correlate with the bacteria and fungi. The enzyme’s break down within the starch was observed through different temperatures and time periods. The Starch was placed in both the fungal and bacterial amylase where they were then placed on spot plates. Through the iodine test‚ it was concluded whether the breakdown of starch occurred or not. The experiment
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93-96 A STUDY OF THE OPTIMAL CONDITIONS FOR STARCH HYDROLYSIS THROUGH THERMOSTABLE α - AMYLASE T. Kolusheva‚ A. Marinova University of Chemical Technology and Metallurgy 8 Kl. Ohridski‚ 1756 Sofia‚ Bulgaria E-mail: e-mail: manahova@abv.bg. Received 10 July 2006 Accepted 12 November 2006 ABSTRACT The present work determines the optimal conditions for starch hydrolysis by thermostable α -amylase (EC 3.2.1.1) produced by Bac.subtilis strain XÊ-86. The hydrolysis reaction has the greatest
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Fungal Amylase and hydrolysis of Starch Abstract This experiment consisted of setting up a control group of starch in various temperature and then placing both fungal amylases and bacterial amylases in a mixture of starch and placing the solution of amylase and starch in various temperatures of water. After a certain amount of time- different amount of time needs to be used in order to have reliable results- iodine is added in a well on spot plates‚ then two drops of the mixture of amylase-starch
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Reaction of Enzyme Amylase Research Question: How will changing the percentage of sodium chloride concentration affect the rate of reaction of enzyme amylase‚ measured using the absorbance of starch and iodine with a spectrophotometer. Introduction: Amylase is an enzyme that is involved in the human digestive process. Found in both the human pancreas and the human saliva‚ amylase breaks down starch into sugar so that large molecules can be easily digested1. Like all enzymes‚ amylase must be kept
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Biochem. J. (1995) 305‚ 17-20 (Printed in Great Britain) 17 RESEARCH COMMUNICATION The effect of low temperatures Nicole MORE‚ Roy M. DANIEL* and Helen H. PETACH on enzyme activity Thermophile Research Unit‚ University of Waikato‚ Private Bag 3105‚ Hamilton 2001‚ New Zealand The stability of two enzymes from extreme thermophiles (glutamate dehydrogenase from Thermococcales strain ANI and f‚- enzymes‚ glucosidase from Caldocellum saccharolyticum expressed in Escherichia
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was to observe the effect of temperature and pH on the reaction of barley alpha-amylase enzyme with starch substrate and establish the optimum temperature and pH for this reaction. The optimum temperature and pH for the reaction of alpha-amylase and starch was predicted to be a temperature of 50°C and a pH of 5. The optimum temperature and pH for the reaction was determined by monitoring the reaction rate of alpha-amylase at different temperatures and pH’s by means of using a spectrophotometer to measure
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