Effect of pH on the activity of ice-binding protein from Marinomonas primoryensis
Effect of pH on the activity of ice-binding protein from Marinomonas primoryensis
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DOI：
10.1007/s00792-020-01206-9
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发表时间：
2020-10-22
期刊：
影响因子：
2.9
通讯作者：
Srubar, Wil V., III
中科院分区：
文献类型：
--
作者：
Delesky, Elizabeth A.;Thomas, Patrick E.;Srubar, Wil V., III
研究了在非生理pH环境中，来自原海单胞菌的冰结合蛋白（MpIBP）对冰晶生长和结构的影响。MpIBP在应激环境条件下保持冰相互作用的能力通过（1）测定多晶冰的冰重结晶抑制（IRI）的改良的splat测定和（2）评价MpIBP动态地塑造单个冰晶形态的能力的纳升渗透压测定来测定。用圆二色性（CD）分析了MpIBP的IRI和DIS活性与二级结构的关系。结果表明，MpIBP二级结构在pH 6和pH 10之间稳定。结果发现，MpIBP在pH = 13时不与冰相互作用。在δ = 12时，MpIBP与对照溶液相比表现出冰晶粒度的减小，并在δ = 10时表现出动态冰成形。结果证实MpIBP在非中性pH环境中保留了一些二级结构和功能，从而使其在非生理材料科学和工程应用中具有潜在的实用性。
The ability of an ice-binding protein (IBP) from Marinomonas primoryensis (MpIBP) to influence ice crystal growth and structure in nonphysiological pH environments was investigated in this work. The ability for MpIBP to retain ice interactivity under stressed environmental conditions was determined via (1) a modified splat assay to determine ice recrystallization inhibition (IRI) of polycrystalline ice and (2) nanoliter osmometry to evaluate the ability of MpIBP to dynamically shape the morphology of a single ice crystal. Circular dichroism (CD) was used to relate the IRI and DIS activity of MpIBP to secondary structure. The results illustrate that MpIBP secondary structure was stable between pH 6 and pH 10. It was found that MpIBP did not interact with ice at pH = 13. At 6 = 12 MpIBP exhibited a reduction in grain size of ice crystals as compared to control solutions and demonstrated dynamic ice shaping at 6 = 10. The results substantiate that MpIBP retains some secondary structure and function in non-neutral pH environments; thereby, enabling its potential utility in nonphysiological materials science and engineering applications.