The effect of pH on the reaction rate of the hydrolysis of sucrose using invertase enzyme at 37C can be explained by understanding the optimal pH range for the enzyme's activity. Invertase, also known as beta-fructofuranosidase, is an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose.The activity of invertase, like most enzymes, is influenced by the pH of the surrounding environment. Enzymes have an optimal pH range in which they exhibit maximum activity. For invertase, the optimal pH range is typically between 4.5 and 5.5. Within this range, the enzyme's structure and active site are most conducive to binding with the substrate sucrose and catalyzing the hydrolysis reaction.When the pH is outside of this optimal range, the enzyme's activity decreases. At extremely acidic or alkaline pH values, the enzyme may become denatured, meaning its structure is altered, and the active site is no longer able to bind with the substrate effectively. This results in a reduced reaction rate for the hydrolysis of sucrose.In summary, the effect of pH on the reaction rate of the hydrolysis of sucrose using invertase enzyme at 37C is that the reaction rate is highest within the optimal pH range of 4.5 to 5.5. Outside of this range, the enzyme's activity decreases, leading to a reduced reaction rate.