Ice-Binding Protein from Shewanella frigidimarinas Inhibits Ice Crystal Growth in Highly Alkaline Solutions
Ice-Binding Protein from Shewanella frigidimarinas Inhibits Ice Crystal Growth in Highly Alkaline Solutions
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DOI：
10.3390/polym11020299
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发表时间：
2019-02-01
期刊：
影响因子：
5
通讯作者：
Srubar, Wil V., III
中科院分区：
文献类型：
--
作者：
Delesky, Elizabeth A.;Frazier, Shane D.;Srubar, Wil V., III
研究了一种天然冰结合蛋白在高碱性溶液中抑制冰晶生长的能力。首先通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）和具有紫外检测器的尺寸排阻色谱（SEC-UV）确认分离的SfIBP的纯度。使用圆二色谱法、SEC-UV和SDS-PAGE评价蛋白质在碱性溶液中的稳定性。SfIBP冰重结晶抑制（IRI）活性，冰晶生长抑制的量度，使用改良的splat测定法进行评估。结果的统计分析证实，尽管SfIBP部分变性和错误折叠，但在碱性溶液（pH = 0.16 mol/L）中限制冰晶生长。SfIBP在具有pH值的溶液中的IRI活性
The ability of a natural ice-binding protein from Shewanella frigidimarina (SfIBP) to inhibit ice crystal growth in highly alkaline solutions with increasing pH and ionic strength was investigated in this work. The purity of isolated SfIBP was first confirmed via sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and size-exclusion chromatography with an ultraviolet detector (SEC-UV). Protein stability was evaluated in the alkaline solutions using circular dichroism spectroscopy, SEC-UV, and SDS-PAGE. SfIBP ice recrystallization inhibition (IRI) activity, a measure of ice crystal growth inhibition, was assessed using a modified splat assay. Statistical analysis of results substantiated that, despite partial denaturation and misfolding, SfIBP limited ice crystal growth in alkaline solutions (pH = 0.16 mol/L. IRI activity of SfIBP in solutions with pH