Enzyme Peroxidase Lab Report

Enzymes are catalysts which lower the activation energy of chemical reactions, thus making them occur more rapidly. Enzymes are in constant use because of their ability to increase the rate of the reaction without permanent alteration. Each enzyme has a different rate of reaction as well as a maximum speed; you can find this number by adding substrate into the concentration until the speed remains constant. The maximum velocity divided by two gives you the Km. In this experiment the efficacy of the enzyme peroxidase was tested. Using differing amounts of substrate in each reaction a spectrophotometer was utilized to observe how fast each reaction produced product. By observing the absorbance for the color change of the oxidized element we

Enzymes act as biological catalysts and are characterized by long chains of amino acids bound together by peptide bonds. Enzymes are seen in all living cells and the metabolic processes in which they convert nutrients into energy and new cells. They also assist in the breakdown of food materials. The reactants of enzyme catalyzed reactions are termed substrates. Each enzyme is quite specific in character, acting on specific substrates to produce specific products. The central approach for studying the mechanism of an enzyme-catalyzed reaction is to determine the rate of the reaction and its changes in response to the changes in parameters such as substrate concentration, enzyme concentration, pH, temperature all of this is known as enzyme kinetics. The substrate concentration, is one of the most important parameters that affects the rate of a reaction that catalyzed by an enzyme. To determine the effectiveness of a catalyst we use the Michaelis-Mentenconstant (Km). The Km is believed to provide a measure of the substrate concentration that is required for catalyst to occur(Berg, 2016). Km can indicate the efficiency of an enzyme, if the constant is low