Determining_The_Effects_Of_PH,_Temperature,_Enzyme_Concentra

Determining The Effects Of PH, Temperature, Enzyme Concentration, And Substrate Concentration On The Activity Of Catacholase In Solanum Tuberosum Abstract: In this experiment, the effect of varying pH, temperature, and enzyme and substrate concentration on the activity of the enzyme catecholase was investigated. The activity of the enzyme was measured by testing the absorbance, which is a measure of the formation of benzoquinone. When the temperature was varied, an optimal level was found at 30 degrees celcius and the optimal pH level was found at pH 7. When the enzyme and substrate concentrations were varied it was found that an increase in either would increase the enzyme activity. From these observations, it was determined that the enzymatic activity of catecholase is dependent on temperature, pH, and enzyme and substrate concentration. Introduction: There are millions of living organisms that have important uses for enzymes as catalytic proteins. Enzymes increase reaction rate by lowering the activation energy of the reaction, however they are not consumed. An enzyme is present as both a reactant and a product in a reaction. Substrates are the reactants for an enzyme and since enzymes have such a high specificity, only specific substrates will fit on certain enzymes. These substrates bind to the active site of an enzyme and form enzyme-substrate complexes. Weak interactions such as hydrogen bonds and ionic ph, enzyme, tubes, substrate, absorbance, activity, rate, concentration, benzoquinone, catechol, added, temperature, reaction, optimal, increasing, experiment, catecholase, tube, phosphate, minutes, each, 1ml, product, increase, four, buffer, recorded, mixed, minute, enzymatic, water, potato, graphs, formed, , until