Selective protein extraction from chicken egg albumen using polyelectrolyte complexes
Selectively extracts proteins from chicken egg albumen using polyelectrolyte complexes (PECs) that mimic the membrane-less organelles cells use to take up specific molecules. Lysozyme has been extracted from freeze-dried egg white powder while retaining its biological activity. Selectivity can be tuned by varying the polyelectrolyte ratio or pH, enabling adaptation to other proteins.
Overview
Egg white (chicken albumen) is a multi-protein mixture containing valuable proteins with a wide range of commercial applications. Polyelectrolyte complexes (PECs) — structures formed by oppositely charged polymers — can mimic the droplet-like, membrane-less organelles that cells use to compartmentalize and selectively capture specific molecules. This research applies that principle to protein separation: a PEC-based extraction method that selectively removes individual proteins from a multi-protein mixture, such as egg white, without destroying their biological activity.
The key benefit is a gentle, tunable extraction technique with demonstrated selectivity. Lysozyme has been selectively extracted from freeze-dried egg white powder and remained biologically active. Because the uptake of a protein depends on the PEC composition and pH, the same platform can be adapted to target other egg white proteins, offering a route to a selective isolation and purification of valuable proteins from complex natural sources.
Technical specifications
- PECs are formed from oppositely charged polyelectrolytes, with their composition controlling which proteins are taken up.
- The approach replicates the selective uptake behavior of membrane-less organelles, allowing individual proteins to be separated from a multi-protein mixture.
- Demonstrated example: lysozyme extracted from freeze-dried egg white powder with retained biological activity.
- Selectivity is tuned through the ratio of oppositely charged polyelectrolytes and pH, and can be adjusted for other proteins of interest.
- The process runs in a liquid environment and the same approach is anticipated to suit different egg white proteins by modifying the operating conditions.
- Scale-up of an lysozyme extraction route can be discussed with an industrial production facility.
Technology readiness level
The method is at the laboratory / proof-of-concept stage, with published results demonstrating selective lysozyme extraction from freeze-dried egg white powder while preserving biological activity. Validation of performance for other egg white proteins still requires development and will depend on the target protein and product requirements. For lysozyme, the process is ready to be scaled up, and discussions on industrial integration can already be initiated.
About University of Twente
The University of Twente is a mid-sized public technical university in Enschede with an engineering-driven, entrepreneurial culture. Industry collaborates through co-located labs and shared facilities, including open-access nanofabrication, prototyping spaces, and campus living labs. A research and technology park adjacent to campus connects companies to faculty and student talent, while a dedicated technology transfer office supports IP, licensing, and startup formation. The university’s integration with regional hospitals enables clinical translation, and its Dutch–German border location offers direct access to the Eastern Netherlands high‑tech systems cluster and North Rhine–Westphalia’s manufacturing base. Research is backed by competitive funding from the Dutch Research Council and ministries, alongside European programs such as Horizon Europe and the ERC.
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