biolab
ANALYSIS OF HOW INHIBITORY COMPOUNDS, ENZYME AND SUBSTRATE CONCENTRATION, pH, AND TEMPERATURE AFFECT THE REACTION RATE OF THE ENZYME ALKALINE PHOSPHATASE Abstract It is hypothesized that sodium molybdate, inorganic phosphate, and phenyl phosphonate are inhibitory compounds of the enzyme alkaline phosphatase. The higher the enzyme concentration or the higher the substrate concentration, the more pNP and inorganic phosphate will be formed. The hypothesized optimum for this enzyme is pH 6 to pH 8 and it is predicted that the higher the temperature, the more effective the alkaline phosphatase will be until an optimum is reached; at which point it will be less effective. Adding the supposed inhibitory compounds to the enzyme/substrate concentration slowed the rate of reaction, thus proving they inhibit the rate of reaction. By measuring the amounts of diluted enzyme in different ph concentrations and placing it at different temperatures, we find that the optimum pH for alkaline phosphatase is pH 8 to pH 10 and the optimum temperature is 37 degrees Celsius. Under these conditions, alkaline phosphatase is effective in catalyzing pNPP reactions, but it is not the cause of the reaction. Introduction Enzymes are important proteins that catalyze, or lower the activation energy of a chemical reaction. they are important in humans as well as other organisms because they speed up reactions and allow them to occur at a normal body temperature.