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Updated: May 15, 2026

Recombinant Collagen I Peptide Microcarriers for Cell Expansion and Their Potential Use As Cell Delivery System in a Bioreactor Model
Published on: February 7, 2018
Human recombinant type I collagen produced in plants.
Oded Shoseyov1, Yehudit Posen, Frida Grynspan
1The Robert H. Smith Faculty of Agriculture, Food and Environment, The Robert H. Smith Institute of Plant Science and Genetics, The Hebrew University of Jerusalem, Rehovot, Israel. shoseyov@agri.huji.ac.il
Researchers developed a plant-based system to produce functional human collagen. This method offers a safe, scalable, and cost-effective alternative to traditional animal-derived collagen for medical and cosmetic applications.
Area of Science:
- Biotechnology
- Biochemistry
- Materials Science
Background:
- Collagen is a crucial extracellular matrix protein vital for tissue integrity and repair.
- Traditional collagen extraction from animal/human sources poses risks of contamination, allergenicity, and functional impairment.
- Recombinant collagen production is challenging due to complex post-translational modifications required for its bioactivity.
Purpose of the Study:
- To establish a reliable and safe method for producing functional human collagen.
- To overcome limitations associated with traditional collagen sourcing and recombinant expression.
- To explore the potential of plant-based expression systems for biopharmaceutical production.
Main Methods:
- Utilized a tobacco plant expression platform to express human collagen type I and essential modifying enzymes.
- Extracted and purified recombinant human collagen from the plant system.
- Characterized the structural and functional properties of the plant-derived collagen.
Main Results:
- Successfully produced recombinant human collagen type I in tobacco plants.
- The plant-derived collagen formed thermally stable helical structures and exhibited fibrillating properties.
- The recombinant collagen demonstrated bioactivity comparable to native collagen, indicating proper maturation and function.
Conclusions:
- Plant-based biofactories offer a viable strategy for mass, rapid, and low-cost production of recombinant proteins like collagen.
- This approach bypasses limitations of traditional sources and complex recombinant systems.
- The developed method yields structurally and functionally identical collagen, suitable for diverse medical and cosmetic applications.
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