Efficient secretory expression of type III recombinant human collagen with triple-helical structure in Komagataella phaffii.

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

SUBMITTER: Ma Y 

PROVIDER: S-EPMC12408790 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature