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September 10, 2025Applied Microbiology and BiotechnologyOpen Access

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

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Co-expression of BmP4H enables stable triple-helical collagen in yeast.
Strain X-33, promoter PAOX1, and a-factor leader optimize collagen secretion.
Scale-up in 5L bioreactor achieves 2.54 g/L rhCol production.
Collagen sequence optimization and microbial screening enhance production efficiency.

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Implication

This novel approach improves yield and stability of recombinant human collagen using microbial prolyl-4-hydroxylase screening and strain optimization.

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Ma et al. (2025) studied this question.

synapsesocial.com/papers/68c187269b7b07f3a0611419 https://doi.org/10.1007/s00253-025-13566-3

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Implication

This novel approach improves yield and stability of recombinant human collagen using microbial prolyl-4-hydroxylase screening and strain optimization.

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

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Discussion

Implication

Cite This Study

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

Key Points

Discussion

Implication

Cite This Study

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