10 different Escherichia coli strains were evaluated for the host of recombinant proteins with non-canonical amino acids. For the incorporation of non-canonical amino acids, genetic code expansion was performed using a green fluorescent protein, which was mutated to have an amber codon at 204th amino acid. The expression level of green fluorescence proteins and the amber suppression of amino-acyl tRNA synthetase were compared among 10 different E. coli strains. As a result of comparison, E. coli W, DH10B, and EPI300 were shown to be efficient hosts for the expression of recombinant fluorescent protein incorporated with noncanonical amino acids. The results of this study can be utilized not only for selecting a host for the production of recombinant therapeutic proteins with non-canoncial amino acids, but also for the development and improvement of aminoacyltRNA synthetase capable of incorporating new non-canonical amino acids.