The activity of the enzyme -amylase in breaking down starch into maltose is significantly affected by temperature. Enzymes, including -amylase, are proteins that act as biological catalysts, speeding up chemical reactions in living organisms. They have an optimal temperature at which they function most efficiently.As the temperature increases, the kinetic energy of the enzyme and substrate molecules also increases. This results in more frequent collisions between the enzyme and substrate, leading to an increased rate of reaction. However, this increase in activity is only observed up to a certain point, known as the optimal temperature.The optimal temperature for -amylase varies depending on its source. For example, human -amylase has an optimal temperature of around 37C 98.6F , while the -amylase from the bacterium Bacillus licheniformis has an optimal temperature of around 90C 194F .Beyond the optimal temperature, the enzyme's activity starts to decline. This is because high temperatures can cause the enzyme's structure to denature, or unfold. The enzyme loses its specific three-dimensional shape, which is crucial for its function. Once denatured, the enzyme can no longer bind to the substrate effectively, and the reaction rate decreases.In summary, the activity of -amylase in breaking down starch into maltose is affected by temperature in the following way:1. At low temperatures, the enzyme activity is low due to reduced molecular movement and fewer collisions between the enzyme and substrate.2. As the temperature increases, the enzyme activity increases due to increased molecular movement and more frequent enzyme-substrate collisions.3. At the optimal temperature, the enzyme functions most efficiently, resulting in the highest reaction rate.4. Beyond the optimal temperature, the enzyme activity decreases due to denaturation and loss of its specific shape, which is essential for its function.