Method for producing polypeptide from recombinant fusion protein and use thereof

Abstract

The present invention relates to a method for producing a polypeptide from a recombinant fusion protein, and disclosed are a method for producing a polypeptide by means of serially combining multiple protease cleavage sites and polypeptide sequences in a specific order under the assistance of protein chaperones, and the use thereof. The high-tandem number recombinant engineering bacteria constructed in the present invention can efficiently express soluble recombinant proteins without forming inclusion bodies and with less impurity proteins. The fusion protein captured after high-pressure crushing can be quickly digested by an enzyme within 1-2 h to obtain a target polypeptide monomer. The expression system can be used to produce various polypeptides having 10-60 amino acids and/or an isoelectric point range of 2-10. Compared with a single serial connection, the yield of the target polypeptide is greatly improved. The method is more suitable for industrial large-scale production.

Dependencies are inferred from the claim text.