Abstract
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.
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Acknowledgments
This research was made possible by the Department of Civil, Environmental, and Architectural Engineering, the College of Engineering and Applied Sciences, and the Living Materials Lab at the University of Colorado Boulder. Thanks to Peter Davies at Queen's University for the gift of the Marinomonas primoryensus clones used in this study. A special thanks is given to Dr. Annette Erbse and the Biochemistry Shared Instruments Pool for assistance with CD Spectrometry.
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This research was funded by the United States (US) National Science Foundation (Award No. CMMI-1727788), the National Science Foundation Graduate Research Fellowship Program, the National Highway’s Cooperative Research Program (NCHRP) (Award No. NCHRP-204), and the NIH/CU Molecular Biophysics Training Program (P.E.T.). This work represents the views of the authors and not necessarily those of the sponsors.
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Data curation: [EAD]; formal analysis: [EAD], [PET], and [MC]; funding acquisition: [WVSIII]; investigation: [EAD] and [PET]; methodology: [EAD], [PET], [JCC], and [WVSIII]; supervision: [JCC] and [WVSIII]; writing–original draft, [EAD]; writing–review and editing, [PET], [MC], [JCC] and [WVSIII]. All authors have read and agreed to the published version of the manuscript.
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Delesky, E.A., Thomas, P.E., Charrier, M. et al. Effect of pH on the activity of ice-binding protein from Marinomonas primoryensis. Extremophiles 25, 1–13 (2021). https://doi.org/10.1007/s00792-020-01206-9
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DOI: https://doi.org/10.1007/s00792-020-01206-9