IceBinders: artificial antifreeze proteins
The benefits
In short- Artificial proteins that prevent the growth of large ice crystals
- Thermostable
- Efficient production
- Patented technology
Some organisms are able to survive at sub-zero temperatures due to unique proteins that selectively bind to ice crystals. Wageningen University and Research and Eindhoven University of Technology designed artificial versions of such ice-binding proteins that prevent the growth of large ice crystals. We are looking for partners for valuable applications.
About our tech offer
Upon freezing and thawing, ice crystals can cause a lot of cellular damage to biological tissues. It has been proven in proof-of-concept studies that ice-binding proteins can protect cells against some forms of freezing damage. The ice-binding proteins collaboratively designed by Wageningen University and Research and Eindhoven University of Technology are thermostable and can be produced in bioreactors using suitable host microorganisms such as E. coli.
What makes our tech offer unique?
Computationally designed
We have computationally designed artificial ice-binding proteins.
Superb qualities
Our proteins have high thermal stability and high activity.
Efficient production
Our ice-binding proteins can be produced efficiently through a biotechnological process.
Important applications
Our artificial proteins can not only be used for food preservation, but also in healthcare (for example in organ transportation).
More information
- Organ and tissue transport and preservation
- Preservation of live cells (e.g. cell cultures for research, CarT cells, cells for IVF)
- Preventing freeze damage in frozen food
The technology is at TRL3/TRL 4 and protected by IP. The proteins have been produced at lab scale. Proof-of-concept cryopreservation studies have been performed using live cells. Wageningen University & Research and TU/e are actively taking steps to work on further product development.
- de Haas, R. J., de Vries, R., Tas, R., Voets, I. (2024). Improved ice-binding proteins based on twist constrained helices. (Patent No. WO2024076237A1).
- de Haas, R. J., Tas, R. P., van den Broek, D., Zheng, C., Nguyen, H., Kang, A., Bera, A. K., King, N. P., Voets, I. K., & de Vries, R. (2023). De novo designed ice-binding proteins from twist-constrained helices. Proceedings of the National Academy of Sciences of the United States of America, 120(27), Article e2220380120.
Interested?
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Technology licensing
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