Wednesday, February 12, 2020
Enzymes activity Lab Report Example | Topics and Well Written Essays - 1750 words
Enzymes activity - Lab Report Example The three sets of reactions were prepared by adding varying amounts of 0.25M sucrose and distilled water. In one set, 0.2 ml of 75mM of magnesium chloride was added, and in another set, an equal amount of 4M Urea was added as inhibitors to the reaction. Reactions in living organisms are slow, enzymes speed up the reactions so as to maintain life. The enzymes control the reactions by ensuring that every reaction is catalyzed by a specific enzyme and at a particular point in a cell. They have a tertiary structure and are folded in a conformation that many intramolecular interactions of amino acids that make up the molecule. They are not used up in the reactions therefore can be used in several reactions. They are substrate specific that is they fold in a shape assisted by chaperone proteins that will determine which substrate the enzyme will act upon. Coenzymes and cofactors aid enzymes in their functions. Enzymes can be denatured by extremes in temperature and pH. Competitive inhibitors, noncompetitive inhibitors and allosteric inhibitors regulate enzyme activity. The enzymes do not change the reactionsââ¬â¢ equilibrium since the free energies of the reactants or products are not changed. Enzymes are catalysts that are protein in nature that increase the rate of a chemical reaction by providing an alternative reaction pathway with a lower free energy of activation. The reaction is usually expressed as In enzyme kinetics, the Michaelis Menten reaction relates the reaction rate (à ½) to [S] which is the concentration of a substrate. The Km and the Vmax of an enzyme can be determined from determination of the initial rates of the enzyme catalyzed reactions over the concentration of the substrate. The maximum rate achieved is Vmax while Km is the Michaelis constant, is the substrate concentration at which the reaction rate is half of Vmax. Km varies from one enzyme to another but is
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