A complex composed of enzyme (horseradish peroxidase, HRP), layered titanate (TiOx), and magnetic beads (MB) was prepared, and the enzymatic activity of the complex and the repeatable use for the enzyme in the complex were investigated. The HRP/TiOx/MB complex was formed in acetate buffer (pH 4) by electrostatic interaction among the components where HRP and MB have positive charge, whereas TiOx is negatively charged. The resultant complex was sufficiently stable in an aqueous solution, and HRP immobilized on the layered titanate in the complex kept a certain enzymatic activity in which typical enzymatic relationship was observed between substrate concentration and initial reaction rate. By giving a magnetic field using commercial magnets, the HRP/TiOx/MB complex was easily and rapidly recovered, and the recovered complex was able to be used for the next enzymatic reactions. The enzyme/inorganic nanosheet/MB complex proposed in this study is expected to be applied as a new tool in the bioengineering and nanobiotechnological fields.