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Related Concept Videos

Upstream Processing01:27

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Upstream processing represents a critical phase in biomanufacturing, wherein biological systems such as microorganisms, mammalian cells, or insect cells are cultivated to produce therapeutic proteins, vaccines, enzymes, or other biologically derived products. This phase encompasses all steps from the selection and genetic manipulation of the production organism to the cultivation of cells in bioreactors under tightly controlled environmental conditions.Host Selection and Genetic OptimizationThe...
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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under...
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Related Experiment Video

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Surface Passivation for Single-molecule Protein Studies
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Integrated process for high conversion and high yield protein PEGylation.

David Pfister1, Massimo Morbidelli2

  • 1Institute for Chemical and Bioengineering, ETH, Vladimir-Prelog-Weg 1, Zurich, 8093, Switzerland.

Biotechnology and Bioengineering
|January 13, 2016
PubMed
Summary
This summary is machine-generated.

This study integrates chromatography into PEGylation to enhance mono-PEGylated protein production. Recycling unreacted protein boosts overall conversion and yield, improving therapeutic protein manufacturing.

Keywords:
PEGylationion-exchange chromatographyprocess integrationprotein purification

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Area of Science:

  • Biotechnology
  • Chemical Engineering
  • Protein Chemistry

Background:

  • PEGylation is crucial for extending therapeutic protein half-life.
  • Improving PEGylation selectivity and yield is vital for cost-effective protein drug development.

Purpose of the Study:

  • To intensify the PEGylation process by integrating chromatography.
  • To enhance yield and conversion for mono-PEGylated protein production.
  • To demonstrate the feasibility using lysozyme as a model protein.

Main Methods:

  • Integrated reaction/separation process using chromatography for fractionation.
  • Isolation and recycling of unreacted protein.
  • Minimizing multi-PEGylated by-products through controlled reaction times.

Main Results:

  • Achieved high yield of mono-PEGylated protein by stopping the reaction early.
  • Demonstrated successful recycling of unreacted protein to drive overall conversion.
  • Showcased the potential for improved yields in processes limited by product over-reaction.

Conclusions:

  • The integrated chromatographic approach significantly improves mono-PEGylation yield.
  • Recycling unreacted protein enables high overall conversion.
  • This method offers a promising strategy for efficient therapeutic protein modification.