EXPRESSION OF SOLUBLE AND ACTIVE INTERFERON αΑ IN PERIPLASM OF <i>Escherichia coli </i>BY FUSION WITH THERMOSTABLE LICHENASE USING THE DOMAIN INSERTION APPROACH
A recombinant DNA that the sequence of the interferon oA gene is integrated into the loop region of the gene coding for the thermostable lichenase was constructed. It is demonstrated that the approach of insertion fusion with thermostable lichenase can be advantageous in terms of increasing the solubility, stability, and production of the fusion partner in soluble form in general and in the periplasm of bacterial cells in particular. Thus, the insertion of interferon oA into the loop (53 a.a.) of thermostable lichenase from C. thermocellum resulted in the effective expression of the soluble form of the recombinant protein in the periplasm of E. coli without any compromises in the biological activity of the interferon oA, while the thermostable lichenase retained its ability for functional folding, without dramatic loss of its basic properties - activity and thermostability.