Amino acids are the basic “building blocks” that combine to form proteins and play an important physiological role in all life-forms. They can be used as models for the examination of the importance of intermolecular bonding in life processes. Dielectric spectroscopy severs to obtained information of the binary solutions on the macroscopic level regarding hydrogen bonding, molecular associations, charge transfer, dipole-dipole and dipole induced dipole interactions. In this paper two amino acids (DL-Alanine & L-Asparagines) with water have been studied by dielectric spectroscopy. The static dielectric constants, their excess dielectric properties, Kirkwood correlation factor and Bruggeman factor of the amino acids - water solutions for different temperatures have been calculated and reported. The static dielectric constants have been achieved by using a sensor which is based on frequency domain reflectometry technique. The behavior of excess dielectric permittivity and Bruggman factor suggest the presence of intermolecular interaction in the binary mixtures. The angular Kirkwood correlation factor confirms the parallel and antiparallel orientation of the electric dipoles in the mixtures.