Abstract: The present invention provides a method of producing polypeptide utilizing a fusion protein of A-B type in the following formula (I), by culturing transformed microorganism comprising DNA sequence encoding the desirable polypeptide; A-B (I). In the above formula (I), A is a fusion partner of 25 or more amino acid residues where aspartic and glutamic acid residues are incorporated to have a net negative charge of 30% or more, and B is the target protein to be produced. The target protein can be isolated from the fusion protein by employing enzymatic cleavage site etc. at the carboxyl-terminus of the fusion partner.

Abstract: The present invention relates to a method for producing a recombinant protein capable of increasing expression rate of a target protein and also improving solubility and folding of the expressed target protein using a modified protein disulfide isomerase (PDI) as a fusion partner, and an expression vector containing the modified PDI gene as a fusion partner. The method for preparing a recombinant protein using a modified PDI as a fusion partner according to the present invention may solve the problems concerning a low yield and solubility and folding that conventional fusion partners have, and be widely used for protein drug and industrial protein production.

Abstract: The present invention relates to a method for producing a recombinant protein capable of increasing expression rate of a target protein and also improving solubility and folding of the expressed target protein using a modified protein disulfide isomerase (PDI) as a fusion partner, and an expression vector containing the modified PDI gene as a fusion partner. The method for preparing a recombinant protein using a modified PDI as a fusion partner according to the present invention may solve the problems concerning a low yield and solubility and folding that conventional fusion partners have, and be widely used for protein drug and industrial protein production.