The activity of the enzyme invertase in breaking down sucrose into glucose and fructose is highly dependent on the pH of the environment. Invertase, like other enzymes, has an optimal pH range in which it exhibits maximum activity. This optimal pH range is typically between 4.5 and 5.5 for invertase.Enzymes are proteins that act as biological catalysts, and their structure is crucial for their function. The pH of the environment can affect the ionization state of amino acid residues in the enzyme, which in turn can alter the enzyme's conformation and its ability to bind to the substrate in this case, sucrose .At pH values below the optimal range, the enzyme's activity decreases due to protonation of specific amino acid residues, leading to changes in the enzyme's conformation and reduced substrate binding. On the other hand, at pH values above the optimal range, the enzyme's activity also decreases due to deprotonation of specific amino acid residues, again leading to conformational changes and reduced substrate binding.In summary, the effect of pH on the activity of the enzyme invertase in breaking down sucrose into glucose and fructose is significant. The enzyme exhibits maximum activity in a narrow pH range 4.5-5.5 , and its activity decreases at pH values outside this range due to conformational changes caused by altered ionization states of amino acid residues.