ArticleApplied microbiology and biotechnology2025
Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.
Article in Applied microbiology and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Advances in Key Genetic Elements and Strategies for High-Yield Heterologous Protein Expression inJournal of fungi (Basel, Switzerland) · 2026Review
- Strategies for Optimizing the Yield and Function of Recombinant Collagen in Different Expression Systems: A Review.International journal of molecular sciences · 2026Review
- Progress in the Expression, Purification, and Characterization of Recombinant Collagen.Bioengineering (Basel, Switzerland) · 2026Review
- Recombinant collagen in regenerative medicine: Expression strategies, structural design, and translational applications.Materials today. Bio · 2025Review
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Authors and funding
8 authors.
Funding
Abstract
Recombinant human collagen (rhCol) holds broad potential in biomedical and industrial applications due to its high purity and low immunogenicity. However, large-scale production of structurally stable and functionally active rhCol remains challenging. A novel strategy integrating collagen sequence optimization and microbial prolyl-4-hydroxylase (P4H) screening was developed to enable efficient production of triple-helical rhCol in Komagataella phaffii. Five Type III collagen variants (ColP1 ~ ColP5) were rationally designed based on interchain salt-bridge engineering to improve structural stability and biological activity, with ColP2 showing superior expression and functionality. A systematic evaluation of four microbial P4Hs identified Bacillus megaterium P4H (BmP4H) as the most effective catalyst for proline hydroxylation, enabling stable triple-helix formation. Combined with strain optimization, promoter and signal peptide screening, and 5-L scale fermentation, this approach achieved a high rhCol yield of 2.54 g/L with confirmed triple-helical structure. These results demonstrate an integrated and scalable platform for high-level production of functional recombinant collagen, providing a promising foundation for its industrial and clinical applications. Key Points • Co-expression of BmP4H enables stable triple-helical collagen in yeast. • Strain X-33, promoter P
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