amylase enzyme

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Introduction

Name Simon Henry Opio-Emuna Module: TEP061N Date: 29th. October 2008. Title: The experiment to determine the effect of temperature on the activity of amylase enzyme. Abstract: The rate of reaction was found to increase as the temperature of the environment was raised. As the temperature was raised from incrementally to 4°C, 22°C, 37°C and finally 80°C the rate of reaction followed this trend and also increased. However as predicted in the hypothesis of this experiment when the temperature was raised too high the enzyme would denature. In this experiment the value which the enzyme denatured at was 80°C. To summarize, the temperature of the environment was increased the reaction rate increased until the enzyme denatured. Introduction: Amylase is an enzyme found in the human body and is an important metabolic enzyme. Its function is to catalyze the hydrolysis of starch into glucose. This particular enzyme, which is found in all mammals, speeds up specific digestive processes which take place along the digestive track running from the mouth to the small intestines. Most enzymes are specific, meaning that they only work on a particular reaction or class of reactions.

Middle

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Conclusion

Archives of Oral Biology 49.12 (2004): 963. Cowen, Robert. "Study of Life's Origins May Improve Everyday Life Today." Christian Science Monitor 87.84 (1995):11. Cold temperature is similar to what cold blooded animals face in winter every year. The amylase cells which could not handle the cold died. Conversely the boiling presented conditions which amylase was not prepared to deal with. that the enzyme is denatured at high temperatures.. . At temperatures above the optimum, the denaturation reaction is dominant, and a rise in temperature within this range further depletes the system of active native enzyme and hence apparently slows the enzyme-substrate reaction. Denaturation of a protein involves breaking of chemical bonds within the molecular structure of the protein. Chemical groupings such as SH and OH which, in the native protein are held in tight combination and are not reactive to any great extent with externally added agents, after denaturation become free at the molecular surface and may be detected by chemical means. The catalytic activity, a function of the peculiarly individual structure of the protein molecule, is generally lost. In addition, the denaturation process is characterized by a very large heat of activation, that is, 50,000 calories or more, as would be expected if a number of chemical bonds were broken in the process. 1

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