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An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast

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Cited 72 time in scopus
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An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast
Lee, Jong Kyu
Kim, Hak Jun
Park, Kyoung Sun
Park, Seungil
Kang, Sung-Ho
Song, Young Hwan
Park, Hyun
Life Sciences & Biomedicine - Other Topics; Physiology
Psychrophilic yeast; Recrystallization inhibition; Thermal hysteresis; ice-binding proteins
Issue Date
Lee, Jong Kyu, et al. 2010. "An extracellular ice-binding glycoprotein from an Arctic psychrophilic yeast". Cryobiology, 60: 222-228.
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 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 iceactive proteins.
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