Glucose oxidase was immobilized in polypyrrole by electrosynthesis. The enzyme had an influence on the redox properties of a complex enzyme electrode. In the cyclic voltammograms of the enazyme electrode new peaks were appeared at the potential around 0.7V vs. Ag/AgCl in additional to the typical peaks for polypyrrole. The more immobilized the stronger the peaks became. During the cycling the pH of electrolyte solution was decreased to about 4.4 The reason for that is to be the proton released from the carboxyl in the glucose oxidase in order to keep on a charge neutrality of the oxidized enzyme. This fact suggests that the new peaks in the voltammograms are caused by the redox of glucose oxidase. In the AC impedance spectrum analysis of the electrode the diffusion of electrolyte anion was limited because of chained structure of the enzyme. The faradic impedance was large since the glucose oxidase is an insulator. Therefore when glucose oxidase is entrapped the enzyme should be limited in amount. Because the growth of the polypyrrole is accompanied both charge transfer and mass transport. For the traditional electrosynthesis that means amount of enzyme present in the electrode is limited to as much as film growable.