ArticleApplied microbiology and biotechnology2026
Enhanced biosynthesis of full-length triple-helical human type III collagen in engineered Komagataella phaffii.
Article in Applied microbiology and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Fibrillar type III collagen, characterized by a distinct triple helix structure, is a critical structural component of the mammalian extracellular matrix (ECM). Its unique mechanical properties and biological functions make it a highly valuable biomaterial for medical applications. However, the limited availability of natural human type III collagen (hCOL3) and the defects of animal-derived sources necessitate sustainable alternatives. Here, we developed an integrated molecular engineering strategy for the efficient production of full-length recombinant human type III collagen (rhCOL3) in Komagataella phaffii. The N- and C-terminal propeptides of the rhCOL3α1 chain were rationally redesigned to preserve its intrinsic capability for triple helix formation. Synergistic co-expression of human P4Hαβ and Bacillus anthracis-derived BaP4H achieved a proline hydroxylation level of 52.88%, enabling the stable assembly of rhCOL3 procollagen homotrimers (> 300 kDa). Subsequent optimization, including high-copy-number strain screening, signal sequence substitution (with Ost1 identified as optimal), and co-expression of the molecular chaperones (e.g., BCY1 and ERO1), significantly enhanced productivity. The engineered strain achieved a rhCOL3 procollagen yield of 430 mg/L in a 5-L fed-batch bioreactor. The purified rhCOL3 exhibited a stable triple helix conformation, a melting temperature of 38.87 °C, and the ability to self-assemble into fibrils with a characteristic D-banding pattern. Biological assays confirmed that the rhCOL3 promotes cell proliferation, adhesion, and migration at levels comparable to those of natural collagen. This study establishes a promising platform for the industrial-scale production of bioactive, triple-helical human collagen. KEY POINTS: • Synergistic P4Hαβ and BaP4H co-expression achieves 52.88% Hyp level and Tm 38.87 °C. • Ost1 and Bcy1 co-expression elevated rhCOL3 yield to 430 mg/L in a 5-L bioreactor. • Purified rhCOL3 self-assembles into D-banded fibrils resembling native collagen.
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