How Does Denaturation Affect The Rate Of An Enzyme Catalyzed Reaction

Enzymes are globular proteins that are synthesized by the ribosomes in a cell. They act as catalysts during biological reactions; therefore, enzymes are able to speed up these reactions without undergoing a permanent change themselves. These proteins are able to do this by lowering the activation energy of a reaction. To add on, enzymes require specific conditions under which they can work best. Reactions occur at faster rates when the temperature is higher. However, the rate of an enzyme-catalyzed reaction is reduced or can be stopped if the temperature becomes too high. This is due to the fact that enzymes become denatured at high temperatures. Denaturation occurs when the shape of an enzyme is altered and so loses it ability to function.
Therefore, it can be said that enzymes have an optimum temperature that corresponds to maximum activity. In this experiment, the optimal temperature for each amylase activity was to be found. The enzyme amylase was used. Amylase was taken from two different types of organisms, a bacterium called Bacillus Licheniformis and a fungus called Aspergillus Oryzae. The reason for the experiment was to discover the optimal temperature for each amylase activity. The reaction between starch with the enzyme amylase was visually seen and recorded to see the effectiveness of the temperature. Amylase has an active site organized in subsites, each of which accommodated a glucose residue (Talamond, Noirot & de Kochko, 2005). This enzyme is responsible for hydrolyzing starch. The presence or absence of starch in the given solutions was tested by using iodine (I2). Iodine formed a blue-black color when added to starch. On the other hand, the iodine did not react with glucose. When added to a glucose solution, the iodine appeared to be yellow in color. Therefore, the faster the blue color of starch is lost, the faster the enzyme amylase is working. If the amylase is inactivated, it can no longer hydrolyze starch, so the blue color of the starch-iodine complex will persist. Multiple temperatures were tested on multiple time intervals to observe the stages of the reaction. It was concluded that with enough evidence, in which there was no relationship between temperature and enzymatic activity, the null hypothesis would be rejected. It would be concluded that there is a relationship between temperature and enzymatic activity.