Abstract:

Pseudomonas fluorescens, as an emerging protein expression system, has demonstrated significant application potential in the fields of biotechnology and biopharmaceuticals, due to its diverse and unique secretion systems. While traditional protein expression systems such as Escherichia coli, Saccharomyces cerevisiae, and insect cell systems have achieved considerable success in many research and industrial applications, they still exhibit limitations in protein folding mechanisms and post-translational modifications. In contrast, P. fluorescens has rapidly gained attention as a research hotspot for its ability to efficiently process and secrete large, complex proteins. This review summarizes recent advances in P. fluorescens as a protein expression system, covering areas such as efficient host strains, cloning vectors, regulatory elements, and protein secretion systems. The paper provides a detailed analysis of P. fluorescens's performance in key steps like protein folding, secretion, and glycosylation, while also exploring the application of various signal peptides in optimizing protein secretion efficiency. These findings not only significantly enhance the solubility and expression levels of target proteins but also offer new insights into improving protein production processes. Furthermore, the application of P. fluorescens in vaccine, therapeutic protein, and antibody production has shown promising potential. Despite significant progress in recent years, challenges remain in expressing certain high-molecular-weight proteins. Future research should focus on genome editing technologies, optimization of protein secretion regulation, and improvements in industrial production processes to further enhance the flexibility and efficiency of P. fluorescens as a protein expression platform, providing a powerful tool for protein engineering and synthetic biology.

Key words: Pseudomonas fluorescens, protein expression system, secretion system