ABSTRACT

This chapter describes the early history of enzyme kinetics. The goal of enzyme kinetics is to describe the catalytic mechanism of enzyme on the basis of kinetic data. Peroxidase contains heme as the prosthetic group, catalyzes the oxidation of a substance in the presence of hydrogen peroxide (H2O2), and shows a characteristic spectrum around 400 nm. The left-hand syringe contained peroxidase, and the right-hand syringe contained H2O2 and leuco-malachite green, an equal volume of both solutions was mixed by pushing the head of syringe. The usual stopped-flow apparatus is equipped with the detectors of absorbance and fluorescence. The inversion of sucrose to glucose and fructose was easily monitored by a polarimeter. The quantitative analysis of the enzymatic reaction was first reported by Henri. He studied the hydrolysis of sucrose by invertase, the hydrolysis of salicin by emulsin, and the hydrolysis of starch and dextrin by amylase.