The aim of this study was to investigate the optimal temperature for α-Amylase to catalyse the hydrolysis of starch. After the implementation of the experiment, it was established that the hypothesis, that the ability of α-Amylase to act upon large linear carbohydrate polymers in starch will prove most effective at 37°C (the optimum human body temperature), was supported by the observed data. The hypothesis was justified based on the observation that the overall average of average colour grades representing the presence of starch molecules in the test solution was the highest at 37°C as 7.2 units, proving that maximum level of maltose and glucose production by α-amylase occurred at this temperature. This was 7.77%, 17.77%, 4.44%, and
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This result was not promoted by past theoretical studies which addressed that even though α-Amylase is considered to still be active at temperatures slightly lower or higher than 37°C, the rate of this enzymatic reaction under this condition is still inhibited in some extent and hence inactivated, due to changes in the moving speed of molecules, the rate at which intermolecular collisions between enzyme’s active sites and their complementary substrates occur, and the amount of energy available for the reaction. The reaction rate of any enzymes, including α-Amylase, is directly proportional to the temperature before it reaches a certain limit. As the temperature reaches this limit (which was observed to be 37°C in this experiment) , causing the reaction to also be the speed up the most, it is high enough to denature the protein composition of the enzyme, resulting in the enzyme losing its initial shape and therefore the ability to bind securely to a specific substrate molecule, which is starch in this experiment, to degrade carbohydrate molecules contained in starch to small glucose-containing polymers such as maltose, maltotriose, α-1,4 linked maltooligosacharides, and α-limit dextrins. This was exemplified by the result as the temperature of the water bath was increased to 47°C, the overall average colour grades instantly dropped by 1.28 units from 7.2 to 5.92 units (Table
This result was not promoted by past theoretical studies which addressed that even though α-Amylase is considered to still be active at temperatures slightly lower or higher than 37°C, the rate of this enzymatic reaction under this condition is still inhibited in some extent and hence inactivated, due to changes in the moving speed of molecules, the rate at which intermolecular collisions between enzyme’s active sites and their complementary substrates occur, and the amount of energy available for the reaction. The reaction rate of any enzymes, including α-Amylase, is directly proportional to the temperature before it reaches a certain limit. As the temperature reaches this limit (which was observed to be 37°C in this experiment) , causing the reaction to also be the speed up the most, it is high enough to denature the protein composition of the enzyme, resulting in the enzyme losing its initial shape and therefore the ability to bind securely to a specific substrate molecule, which is starch in this experiment, to degrade carbohydrate molecules contained in starch to small glucose-containing polymers such as maltose, maltotriose, α-1,4 linked maltooligosacharides, and α-limit dextrins. This was exemplified by the result as the temperature of the water bath was increased to 47°C, the overall average colour grades instantly dropped by 1.28 units from 7.2 to 5.92 units (Table