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Production of recombinant human collagen in Physcomitrella

ABSTRACT: A hydrophilic region encompassing 334 amino acids from human type III collagen was produced in Physcomitrella bioreactors and analyzed with respect to prolyl-hydroxylation.

INSTRUMENT(S):

ORGANISM(S): Physcomitrella Patens Subsp. Patens (moss)

SUBMITTER: Sebastian Hoernstein

LAB HEAD: Ralf Reski

PROVIDER: PXD071319 | Pride | 2026-02-09

REPOSITORIES: Pride

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Publications

Secretion-based production of prolyl-hydroxylated human type III collagen in scalable Physcomitrella photobioreactors.

Bohlender Lennard L LL Parsons Juliana J Mitgau Antonia A Hoernstein Sebastian N W SNW Grigolon Giovanna G Henes Bernhard B Decker Eva L EL Reski Ralf R

Plant cell reports 20260128 2

<h4>Key message</h4>Scalable moss bioreactors enable the production of high-quality recombinant prolyl-hydroxylated human collagen without heterologous P4H expression, offering a sustainable and vegan alternative to conventional collagens derived from animals. Collagens are structural proteins of the extracellular matrix essential for skin elasticity and integrity. They are widely used in dietary supplements and cosmetics. Conventional collagens of animal origin raise concerns regarding ethics, ...[more]

PMID: 41604015

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