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Characterization of the Ice-Binding Protein from Arctic Yeast Leucosporidium sp. AY30

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Title
Characterization of the Ice-Binding Protein from Arctic Yeast Leucosporidium sp. AY30
Other Titles
북극 효모 (Leucosporidium sp. AY30) 유래 결빙방지단백질 (LeIBP) 의 특성 분석
Authors
Kyoung Sun Park
Kim, Hak Jun
Do, Hackwon
Eun jung Kim
Kang, Sung-Ho
Soon-Jong Kim
Seung Il Park
Lee, Jun Hyuck
Subject
Meteorology & Atmospheric Sciences
Keywords
Ice-binding protein; Leucosporidium sp.; N-linked glycosylation; Reversible dimer; Thermal hysteresis
Issue Date
2012
Publisher
Elsevier
Citation
Kyoung Sun Park, et al. 2012. "Characterization of the Ice-Binding Protein from Arctic Yeast Leucosporidium sp. AY30". Cryobiology, 64(3): 286-296.
Abstract
Previously, we reported the ice-binding protein (LeIBP) from the Arctic yeast Leucosporidium sp. AY30. In this study we provide physicochemical characterization of this IBP, which belongs to a class of IBPs that exhibited no significant similarity in primary structure to other known antifreeze proteins (AFPs). We compared native, glycosylated and non-glycosylated recombinant LeIBPs. Interestingly, size-exclusion chromatography and analytical ultracentrifugation revealed that LeIBP self-associates with a reversible dimer with Kd values in the range 3.45-7.24 × 10-6 M. Circular dichroism (CD) spectra showed that LeIBP, glycosylated or non-glycosylated, is predominantly composed of β-strand secondary structural elements (54.6%), similar to other β- helical antifreeze proteins (AFPs). In thermal hysteresis (TH) activity measurements, native LeIBP showed twice the activity (0.87 °C at 15 mg/ml) than that of the recombinant IBPs (0.43-0.42 °C at 10.8 mg/ml). This discrepancy is probably due to uncharacterized enhancing factors carried over during ice affinity purification, because glycosylated and non-glycosylated recombinant proteins displayed similarly low activity. Ice recrystallization inhibition (RI) activities of the native and recombinant LeIBPs were comparable. Measurements of CD, TH activity, and RI showed that glycosylation does not cause structural changes and is not required for fu similarity in primary structure to other known antifreeze proteins (AFPs). We compared native, glycosylated and non-glycosylated recombinant LeIBPs. Interestingly, size-exclusion chromatography and analytical ultracentrifugation revealed that LeIBP self-associates with a reversible dimer with Kd values in the range 3.45-7.24 × 10-6 M. Circular dichroism (CD) spectra showed that LeIBP, glycosylated or non-glycosylated, is predominantly composed of β-strand secondary structural elements (54.6%), similar to other β- helical antifreeze proteins
URI
http://repository.kopri.re.kr/handle/201206/6244
DOI
http://dx.doi.org/j.cryobiol.2012.02.014
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