Abstract

Cultured meat is an emerging technology with the potential to meet future protein demands while addressing the challenges associated with traditional livestock farming. The production of cultured meat requires efficient, animal component-free in vitro systems for muscle stem cell (MuSC) expansion. Fibroblast growth factor 1 (FGF1) is a critical growth factor that regulates the MuSC function. In this study, we established an efficient method for the soluble expression and purification of recombinant porcine FGF1 (rpFGF1) in Escherichia coli, achieving a yield of 48 mg of purified protein per liter of culture. Treatment with rpFGF1 significantly enhanced the proliferation of porcine MuSC under serum-free conditions. Furthermore, rpFGF1 induced mitochondrial fission and mitophagy by activating the ERK-dependent phosphorylation of DRP1 at Ser616, resulting in improved mitochondrial function and proliferation capacity in porcine MuSC. These findings highlight the potential of rpFGF1 in the development of serum-free media for scalable and sustainable cultured meat production.