An The main objective of this lab is to

An enzyme is a protein catalysts, in light of the fact that they are made up of amino acids, and they act as a biological catalyst for the biochemicals reactions in living organisms. A catalyst is a substance that triggers a biochemical reactions (endothermic and exothermic), without enzymes, these reactions would not occur fast enough. Enzymes are affected by various factors, temperature, PH, and substrate concentration are all examples of said factors.The substrate concentration in a given reaction is the limiting factor this experiment will focus on.  Increasing substrate concentration will increase the rate of reactions, as substrate-active site collisions will take place more frequently.  In other words, during biochemical reactions, kinetic energy increases as well as the rate of the reaction, nevertheless, it should be considered that the rate of the reaction will inevitably become constant, this is known as the maximum velocity (Vmax). This occurs as the active site of an enzyme is occupied and unavailable to other substrates molecules until products have been formed and released. Active sites become more and more occupied when the substrate concentration is increased, thereby, the substrate-active site collisions are blocked and the rate in which enzymes catalyse reactions gets smaller and smaller. The main objective of this lab is to find the maximum capacity of substrates an enzyme can catalyse without a decrease in enzyme activity rate. In addition to analyzing the rate of the enzymes, a comparison between the rate of enzyme activity with different substrate concentrations will take place. Hydrogen peroxide will be used as the substrates, in order to see how much is needed for the catalase enzyme activity to significantly slow down due to the maximum substrate concentration being reached. As a group, we believe that the more hydrogen peroxide added, the more the catalase enzyme activity will increase. Nevertheless only for a short period of time as the active site of the catalase enzymes will  become so occupied that the catalase activity will stop increasing, even if more hydrogen peroxide is added. We believe this because Leonor Michaelis and Maud Menten, were the ones who first discovered that the rate limiting step in enzymatic reactions is the breakdown of the ES complex to free enzyme and product,

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