Acid Phosphatase Lab

Most enzymes are catalytic proteins made up of amino acids and are a key part of the breakdown and synthesis of virtually every biological catalysis reaction mechanism. The primary function of a catalytic enzyme is to increase the rate of reaction by helping the enzyme overcome the activation energy barrier without the reaction consuming or changing the enzyme. In enzymatic reactions, the substrate binds to the highly specific enzyme active site (the substrate-binding domain) and forms an enzyme-substrate complex. The substrate begins to convert into the product and the intact enzyme releases from the complex and is able to bind to another substrate to start the process over. The enzyme binding to the substrate is a crucial step in the reaction because the more enzyme-substrate complexes, (up until reaching saturation), the more product the reaction is generating.
The enzyme of interest in this experiment is acid phosphatase, a digestive-enzyme that is ubiquitous in nature and while it is found in the blood, kidneys, liver etc. of …show more content…
The experimental results were obtained from the use of a standard curve for a known concentration of nitrophenol and an experimental reaction to test the velocity of the pure and extracted acid phosphatase. Also, the rate at which the nitrophenol formed at different substrate concentrations was tested and a Michaelis Menten and Lineweaver-Burk plot was made to determine the Vmax and Km. Based on previous research, it was expected that the velocity for the extracted enzyme would have a higher rate of reaction than the pure enzyme. Also, it was expected that as the concentration of substrate increased, the Michaelis Menten and the Lineweaver-Burk plot would show an increased