The pharmaceutical production of the key therapeutic protein erythropoietin is largely dependent on the establishment of a successful heterologous expression system. This study reports the successful expression of the recombinant human erythropoietin in the methylotrophic yeast Hansenula polymorpha at a significantly high level (265 mg/l). Although erythropoietin was previously expressed in a wide variety of mammalian, bacterial and fungal-based systems, this is the first time this key hormone is expressed in the industrially important H. polymorpha. The significantly high expression level and the convenience of this organism for the industrial production of recombinant proteins make the development of a stable H. polymorpha erythropoietin transformants an essential improvement, in the exploitation of this key protein by the pharmaceutical industry. The expressed protein was successfully purified and characterized; confirming its structural and functional properties, while an industrial scale development of the system is under development.
EPO, Erythropoietin, H. polymorpha, Recombinant proteins, Glycosylated