Falling water ice affinity purification of ice-binding proteins
Chen Adar1, Vera Sirotinskaya1, Maya Bar Dolev1
1The Hebrew University of Jerusalem, Robert H. Smith Faculty of Agriculture, Food and Environment, Institute of Biochemistry, Food Science and Nutrition, Rehovot, 7610001, Israel.
Scientific Reports
|July 25, 2018
Summary
A novel falling water ice affinity purification (FWIP) method efficiently purifies ice-binding proteins (IBPs) without tags. This technique yields high-purity IBPs suitable for various industrial applications.
Area of Science:
- Biochemistry
- Materials Science
Background:
- Ice-binding proteins (IBPs) enable organisms to survive in icy environments.
- IBPs' ice-modulating properties offer potential in food preservation, cryopreservation, and anti-icing technologies.
- Scalable and efficient purification methods are crucial for the commercialization of IBPs.
Purpose of the Study:
- To develop and validate a novel, tag-free purification method for ice-binding proteins.
- To assess the efficiency and scalability of the proposed purification technique.
Main Methods:
- Falling water ice affinity purification (FWIP) utilizing a standard ice machine.
- IBPs selectively bind to ice crystals formed on a chilled surface, while other solutes remain in solution.
- Tangential flow filtration for concentrating the purified protein solution.
Main Results:
- FWIP achieves high purity (>95%) for IBPs in just two purification rounds.
- Up to 35 mg of IBP can be incorporated per 1 kg of ice.
- A single ice machine can purify approximately 1 gram of IBP per day, demonstrating scalability.
Conclusions:
- FWIP is an effective, tag-free method for purifying large quantities of ice-binding proteins.
- The method's scalability makes it suitable for producing grams of IBPs for research and industrial applications.
- This purification strategy facilitates the broader use of IBPs in cryopreservation, food science, and anti-icing applications.
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