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Updated: Jun 17, 2026

LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
Published on: February 4, 2013
An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast
Jong Kyu Lee1, Kyoung Sun Park, Seungil Park
1Division of Polar Biology and Ocean Sciences, Korea Polar Research Institute, Incheon, Republic of Korea.
Abstract:
A psychrophilic yeast was isolated from an Arctic pond and its culture supernatant showed ice-binding activity. This isolate, identified as Leucosporidium sp. based on an analysis of the D1/D2 and ITS regions of its ribosomal DNA, produced a secretory ice-binding protein (IBP). Yeast IBP was purified from the culture medium to near homogeneity by the ice affinity method and appeared to be glycosylated with a molecular mass of approximately 26 kDa. In addition, the yeast IBP was shown to have thermal hysteresis (TH) and recrystallization inhibition (RI) activities. The full-length cDNA for yeast IBP was determined and was found to encode a 261 amino acid protein with molecular weight of 26.8 kDa that includes an N-terminal signal peptide and one potential N-glycosylation site. The deduced protein showed high sequence identity with other IBPs and hypothetical IBPs from fungi, diatoms, and bacteria, clustering with a class of ice-active proteins.
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