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Determining the Optimal Temperature and Ph of Barley Amylase

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Determining the Optimal Temperature and Ph of Barley Amylase
Determining the Optimal Temperature and PH of Barley Amylase

Abstract
The purpose of this experiment was to find the optimal temperature and pH of barley alpha-amylase. I hypothesize that the optimal temperature would be 55 degrees Celsius and the optimal pH would be 5.5. In this experiment, the starch is used as a substrate to examine the optimum temperature and pH for the reaction of alpha amylase. It is known that the measuring of disappearance (absorbance) of the substrate starch with iodine using spectrophotometer will show the concentration of the substrate which will also reflect on the reaction rate. Once the reaction rates are figured out, the optimal temperature and pH can be determined. The result concluded that the optimal temperature was at 50 degrees Celsius and the optimal pH was at 5.0. I have evaluated that my hypothesis was not supported through this experiment however, it has been clarified that the optimal temperature and pH of barley alpha-amylase turns out to be around 50-55degrees Celsius, and the pH of 5.0-5.5 based on the research of MacGregor in 1978.

Introduction
The purpose of this experiment is to determine the optimal temperature and pH of barley amylase with starch using the absorbance rate of alpha-amylase. When reactants undergo a reaction, enzymes, proteins that serve as chemical agents without being consumed by the reaction, are used to speed up the reaction. (Campbell, Reece, 2005) Every enzyme has its own optimal temperature and pH which they can be most efficiently active.
Thus, in order for an enzyme to be most efficiently active, the environmental factors, such as temperature and pH, must support the reaction. The increase in temperature instantaneously increases the rate of enzymatic reaction by causing the molecules to move rapidly which alludes the substrates to collide with active sites more frequently. However, because the substrate binds to the active site by weak interactions, such as



Cited: Campbell, N.A. and J.B Reece. 2005.Biology 7th edition. San Francisco. Benjamin Cummings. MacGregor, A.W. 1978. Alpha-Amylase I from Malted Barley---Physical Properties and Action Pattern on Amylose. Journal of Cereal Chemistry 55: 754 - 765. Vliet, Kent A. 2008.A Lab Manual For Integrated Principles of Biology Part One-BSC2010L third edition. Pearson Custom Publishing. United States of America

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