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Updated: Jul 11, 2025
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
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Identifying Ice-Binding Proteins in Nature.
1Department of Evolution, Behavior and Ecology, University of Illinois, Urbana Champaign, Urbana, IL, USA. adevries@illinois.edu.
Methods in Molecular Biology (Clifton, N.J.)
|November 9, 2023
Summary
Organisms in freezing environments use ice-binding proteins (IBPs) to survive. New techniques detect these antifreeze proteins in fish, insects, microbes, and plants, aiding cold adaptation research.
Area of Science:
- Cryobiology
- Molecular Biology
- Biochemistry
Background:
- Organisms in freezing environments possess adaptations to survive sub-freezing temperatures.
- Ice-binding proteins (IBPs) are key adaptations, conferring antifreeze properties in some species and ice recrystallization inhibition (IRI) in others.
Purpose of the Study:
- To describe techniques for detecting IBPs across diverse organisms.
- To differentiate between antifreeze and IRI functions of IBPs.
Main Methods:
- Blood and hemolymph collection from fish and insects to test for hysteresis (antifreeze property).
- Analysis of microbial spent growth media for ice basal plane pitting (IRI).
- Isolation of plant apoplastic fluid via vacuum infiltration and centrifugation, followed by ice basal plane pitting assay.
Main Results:
- Hysteresis indicates antifreeze IBPs in fish and insects.
- Microbial IBPs and plant apoplastic IBPs demonstrate potent IRI, with minimal hysteresis.
- Ice basal plane pitting effectively verifies IBP presence in microbes and plants.
Conclusions:
- Effective methods are established for identifying IBPs and their functions in various organisms.
- These techniques advance the study of cold adaptation mechanisms in nature.
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