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Related Experiment Video

Updated: Jul 11, 2025

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

Published on: May 5, 2017

Identifying Ice-Binding Proteins in Nature.

Arthur L DeVries¹

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.

Keywords:

Antifreeze proteins Fish Freeze avoidance Freezing tolerance Ice pitting assay Ice-binding proteins Inhibition of recrystallization Insects Nucleation Supercooling Thermal hysteresis (TH)

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Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity

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Published on: January 15, 2014

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.