Aim: The aim of this practical is to use three different techniques to investigate the effect of different concentrations of the enzyme catalase on the rate of breakdown of hydrogen peroxide.
Background information
Catalase is an enzyme which is found in all living organisms. This enzyme catalases the decomposition of hydrogen peroxide into water and oxygen. Cells continually produce a poisonous by-product of metabolising, called hydrogen peroxide.
This is very damaging to cells and is broken down as soon as it is formed in the cytoplasm into water and oxygen by the action of the enzyme catalase. Catalase occurs in all cells, especially those that are very active or in organs specialised to break down unwanted materials. Purified catalase or tissues containing catalase are used in practical investigations as a source of the enzyme. Enzymes that are reacting with the catalase will need to have a very specific shape and a very specific shaped active site. In order to work, the substrate will need to properly fit into the enzymes active site. Once this happens, the reaction occurs. Once the substrate has entered the active site and a reaction has occurred, the substrate will leave the active site as a product, and a new substrate will enter the enzyme. Catalase is a biological enzyme and because of this its optimum functioning temperature would be 37 degrees, at this temperature the enzyme can function properly. At much higher or lower temperatures, the enzymes will not work. This is because at higher temperatures, the active site of the enzyme is way too high and the shape for the substrate to fit into will become disfigured and denatured, having its shape to one which will not react with the substrate. At too low of a temperature, the substrates do have enough kinetic energy to move around on its way and in the active site, meaning that no reaction will take place. If inside a host, the danger of having such a high