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

Basic human fibroblast growth factor FGF-2 plays a major role in wound healing. Thus, its regenerative potential attracts both researchers and commercial drug manufacturers, including cell therapy developers. This research aims to optimize purification method to obtain high purity rhFGF-2 expressed in methylotrophic yeast Pichia pastoris. Suggested method allows purification of rhFGF-2 with purity of >98% as determined by SDS-PAGE. The effective proliferative dose of rhFGF-2 determined by WST-1 proliferative assay on 3T3 mouse fibroblast cell culture is 5.73 ± 2.16 ng/ml. The presented optimized technique may be attractive for the development of an industrial technology for rhFGF-2 production.