Progress in the Expression, Purification, and Characterization of Recombinant Collagen

This review highlights the advancements in recombinant collagen production, emphasizing its benefits over traditional methods, such as higher bioactivity and low immunogenicity. Various expression systems, including E. coli, Pichia pastoris, and mammalian cells, are compared for efficiency and cost, with E. coli and Pichia pastoris being the most effective. Purification techniques like chromatography are crucial for high purity, while characterization methods ensure structural integrity and bioactivity. Recombinant collagen shows promise in wound healing and tissue engineering, but challenges remain in optimizing post-translational modifications and purification processes. Future research should focus on improving expression systems and exploring molecular mechanisms to enhance clinical applications.