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Effect of pH on the activity of ice-binding protein from Marinomonas primoryensis
Extremophiles ( IF 2.9 ) Pub Date : 2020-10-22 , DOI: 10.1007/s00792-020-01206-9
Elizabeth A. Delesky , Patrick E. Thomas , Marimikel Charrier , Jeffrey C. Cameron , Wil V. Srubar

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 ≤ 4 or pH ≥ 13. At 6 ≤ pH ≥ 12 MpIBP exhibited a reduction in grain size of ice crystals as compared to control solutions and demonstrated dynamic ice shaping at 6 ≤ pH ≥ 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.



中文翻译:

pH值对滨海边藜的冰结合蛋白活性的影响

在这项工作中,研究了滨海樱草Mp IBP)的冰结合蛋白(IBP)在非生理pH环境中影响冰晶生长和结构的能力。Mp IBP在压力环境条件下保持冰相互作用的能力是通过(1)改进的splat分析确定多晶冰的冰重结晶抑制(IRI)和(2)纳升渗透压法评估Mp IBP动态成型的能力来确定的单个冰晶的形态。使用圆二色性(CD)将Mp IBP的IRI和DIS活性与二级结构相关联。结果表明,MpIBP二级结构在pH 6和pH 10之间稳定。发现在pH≤4或pH≥13时,Mp IBP不与冰相互作用。在6≤pH≥12时,Mp IBP显示出冰晶的晶粒尺寸减小,因为与对照溶液比较,并证明在6≤pH≥10时具有动态冰成形。结果证实,Mp IBP在非中性pH环境中保留了一些二级结构和功能;因此,使其在非生理材料科学和工程应用中具有潜在的实用性。

更新日期:2020-10-30
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