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Updated: Jun 16, 2026
09:43
Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
8.7K
Extended Temperature Range of the Ice-Binding Protein Activity
Vera Sirotinskaya1, Maya Bar Dolev1,2, Victor Yashunsky1,3
1Institute of Biochemistry, Food Science, and Nutrition, Robert H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Rehovot 7610001, Israel.
Langmuir : the ACS Journal of Surfaces and Colloids
|March 25, 2024
Summary
Antifreeze proteins (AFPs) prevent ice damage in organisms. This study shows AFPs inhibit ice formation and growth even at -80°C, enhancing cryopreservation potential.
Area of Science:
- Cryobiology
- Biochemistry
- Materials Science
Background:
- Ice-binding proteins (IBPs) protect organisms from freezing.
- IBPs inhibit ice growth, recrystallization, nucleation, and shaping.
- Limited data exists on IBPs' functionality under cryogenic conditions.
Purpose of the Study:
- Investigate the impact of fish type III AFP and Tenebrio molitor AFP on vitrified solutions.
- Assess AFP efficacy in depressing devitrification and ice recrystallization at cryogenic temperatures.
Main Methods:
- Tested fish type III AFP and Tenebrio molitor AFP in vitrified dimethylsulfoxide (DMSO) solutions.
- Observed AFP effects on ice formation and recrystallization at -80 °C.
Main Results:
- Both AFPs successfully depressed devitrification at -80 °C.
- AFPs inhibited ice recrystallization during warming phases.
- Demonstrated AFP activity below the homogeneous nucleation temperature regime.
Conclusions:
- AFPs are active and effective at cryogenic temperatures (-80 °C).
- AFPs show potential for enhancing cryopreservation by minimizing ice-related damage.
- Further research into AFPs can advance cryopreservation techniques.
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