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[Producing human lactoferrin by high-density fermentation recombinant Pichia pastoris]
Ge Ying1, Shu-hua Wu, Jing Wang
1Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention, Beijing 100052, China.
Summary
High-density fermentation of recombinant Pichia pastoris successfully expressed human lactoferrin, achieving 115 mg/L. This method maintained the protein
Area of Science:
- Biotechnology
- Molecular Biology
- Microbial Fermentation
Context:
- Human lactoferrin is a crucial protein with antimicrobial and immune-modulating properties.
- Recombinant protein expression in Pichia pastoris offers a scalable production system.
- Maintaining biological activity during heterologous expression is essential for therapeutic applications.
Purpose:
- To optimize the high-density fermentation process for human lactoferrin expression in Pichia pastoris.
- To ensure the biological activity of the expressed human lactoferrin.
- To achieve high yields of functional human lactoferrin.
Summary:
- Human lactoferrin cDNA was cloned and expressed in Pichia pastoris.
- High-producing transformants were screened and subjected to fed-batch high-density fermentation.
- The process yielded 115 mg/L of human lactoferrin, a significant increase over shake flask methods, while preserving biological activity.
Impact:
- Demonstrates a robust method for large-scale production of biologically active human lactoferrin.
- Provides a foundation for further optimization of recombinant protein expression in Pichia pastoris.
- Potential for cost-effective manufacturing of human lactoferrin for therapeutic and industrial uses.