Activation Energy of Enzyme and Non-Enzyme Catalyzed Reactions

Abstract

The goal of this research was to compare the activation energy and rate constants of an enzyme catalyzed and a non-enzyme catalyzed hydrolysis reaction at different temperatures. NaOH was used as the non-enzyme catalyst and esterase was used as the enzyme catalyst. Using UV-Vis Spectroscopy, the catalyzed transformation from p-nitrophenylacetate to p-nitrophenol was observed. It was found through curve-fit analysis that the rate constants for both were temperature dependent. Arrhenius analysis utilizing these constants determined activation energies of 57.53 kJ/mol for the esterase and 58.02 kJ/mol for NaOH. These results suggest enzyme catalyzed reactions have a lower activation energy and therefore a faster rate of reaction than non-enzyme catalyzed reactions.