Objective: To explore the feasibility of applying molecular chaperones to the soluble expression of e23sFv/His fusion proteins.
Methods: The molecular chaperone plasmid pGro7 or pKJE7 was transformed into BL21 (DE3) competent cells together with the prokaryotic expression vector harboring His-tagged e23sFv. The soluble expression of e23sFv/His proteins was induced at 16 °C. The yield and antigen-binding activity of the soluble products were compared with those of the insoluble products conventionally purified from inclusion bodies.
Results: Both the overall yield and the purification ratio of soluble e23sFv/His proteins were relatively lower. The binding affinity of the soluble products to immobilized HER2 was not superior to that of the insoluble products from inclusion bodies.
Conclusion: The molecular chaperone plasmids pGro7 and pKJE7 partially facilitate the soluble expression of e23sFv/His proteins, but both the yield and the purification ratio are still limited.