Optimization of Purification Method of Recombinant Basic Human Fibroblast Growth Factor rhFGF-2 Obtained in Methylotrophic Yeast Pichia pastoris

Basic fibroblast growth factor (FGF-2) is an important regulator of wound healing in humans, which makes it a focus of research in drug and cell therapy development. In this study methods of production, isolation and purification of recombinant human FGF-2 (rhFGF-2) are evaluated and an optimized protocol of rhFGF-2 purification is proposed. Using a Pichia pastoris methylotrophic yeast expression system yield of rhFGF-2 with >98% purity (SDS-PAGE) and high proliferative activity (5.73 ± 2.16 ng/mL) was achieved. The developed approach is suitable for scaling up industrial rhFGF-2 production.