Describe The Relationship Between Enzyme And Hydrolyse

Amylase is a very important enzyme located in the saliva and pancreatic juices that hydrolyses (break down) starch and glycogen into more simple and readily digestible forms of sugar. Enzymes are biological catalysts that increase the rate of biological reactions. Enzymes are produced in living cells and are involved in speeding up biochemical reactions. They have an active site to which specific substrate binds. They increase the rate of reactions by decreasing the amount of activation energy meaning that the barrier to a reaction is lower when an enzyme is being used. The combination of enzyme and substrate creates a new energy outline hence causing a decrease in the amount of activation energy.(Lesson 6.5 A Catalyst and the Rate of Reaction). Once a product has been formed, they leave the active site of the enzyme hence more reactions can occur. There are
Enzyme inhibitors reduce the rate of a catalysed reaction. They do this by interfering with the enzyme when combining with the substrate. There are two types of known inhibitors. Competitive inhibitors are known to prevent the formation of Enzyme-Substrate Complex due to the fact that they have a similar shape to the substrate of the molecule (Day). The inhibitor competes for the same active site as the substrate molecules. No reaction takes place due to its role to prevent any substrate molecules from reacting with the enzyme. However, non-competitive inhibitors are substances that do not interact with the active site of the enzyme. They react very closely to the active site, thus their intention is to change the shape of the enzyme so that the substrate can no longer interact with the enzyme (Enzyme Inhibitors). Non-competitive inhibitors are usually reversible. In this experiment, Copper Sulphate will be used as an inhibitor to determine the efficiency of the enzyme Amylase. Starch will be used as the substrate for Amylase to break down into