Scientists have discovered that an ice-binding protein fcIBP from the sea ice microalga does not fit in the conventional classification of ice-binding proteins, suggesting unknown mechanisms behind its antifreeze property. This finding could lead to a broader application of the antifreeze protein in food and medical industries. Organisms living in cold zones produce ice-binding antifreeze proteins to prevent themselves from freezing to death. Such proteins have been classified in two groups; the hyperactive type attaches to the hexagonal basal faces of ice crystals to inhibit ice crystal growth and lowers the freezing temperature by up to six degrees C while the moderate type does not attach to the basal faces and lowers the freezing temperature by not more than 1 degree C. The morphology of ice crystals to which fclBP had attached was observed under microscopes and their growth rates were precisely measured.
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