Trypsin was immobilized to alumina by adsorption from its aqueous solutions. The activity of trypsin was increased by immobilization for peptide synthesis. With these immobilized enzymes Bz-Arg-Leu-NH2 dipeptide synthesis was carried out. Iso amylalcohol, tetrahydrofuran and acetonitrile were used as solvents giving the highest yield in the peptide formation reaction. The yield of the peptide was strongly dependent on water content in the reaction medium. The stability of alumina-immobilized trypsin is described.