Increasing salt rejection of polybenzimidazole nanofiltration membranes via the addition of immobilized and aligned aquaporins

Priyesh Wagh; Xinyi Zhang; Ryan Blood; Peter M. Kekenes-Huskey; Prasangi Rajapaksha; Yinan Wei; Isabel C. Escobar

doi:10.3390/pr7020076

Increasing salt rejection of polybenzimidazole nanofiltration membranes via the addition of immobilized and aligned aquaporins

Priyesh Wagh, Xinyi Zhang, Ryan Blood, Peter M. Kekenes-Huskey, Prasangi Rajapaksha, Yinan Wei, Isabel C. Escobar

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

Aquaporins are water channel proteins in cell membrane, highly specific for water molecules while restricting the passage of contaminants and small molecules, such as urea and boric acid. Cysteine functional groups were installed on aquaporin Z for covalent attachment to the polymer membrane matrix so that the proteins could be immobilized to the membranes and aligned in the direction of the flow. Depth profiling using x-ray photoelectron spectrometer (XPS) analysis showed the presence of functional groups corresponding to aquaporin Z modified with cysteine (Aqp-SH). Aqp-SH modified membranes showed a higher salt rejection as compared to unmodified membranes. For 2 M NaCl and CaCl ₂ solutions, the rejection obtained from Aqp-SH membranes was 49.3 ± 7.5% and 59.1 ± 5.1%. On the other hand, the rejections obtained for 2 M NaCl and CaCl ₂ solutions from unmodified membranes were 0.8 ± 0.4% and 1.3 ± 0.2% respectively. Furthermore, Aqp-SH membranes did not show a significant decrease in salt rejection with increasing feed concentrations, as was observed with other membranes. Through simulation studies, it was determined that there was approximately 24% capping of membrane pores by dispersed aquaporins.

Original language	English
Article number	76
Journal	Processes
Volume	7
Issue number	2
DOIs	https://doi.org/10.3390/pr7020076
State	Published - Feb 1 2019

Bibliographical note

Funding Information:
This material is based upon work supported by the National Science Foundation under Cooperative Agreement No.1355438, and by the NSF KY EPSCoR Program and in addition the author acknowledges Center of Membrane Sciences at University of Kentucky. Research reported in this publication, release was supported by the Maximizing Investigators' Research Award (MIRA) (R35) from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under grant number R35GM124977. We further acknowledge support from the American Chemical Society Petroleum Research Fund 58719-DN16. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. In addition, the authors want to acknowledge the sources of funding, NSF 1308095 and USGS 104(b): Ohio Water Development Authority GRT00028988/60040357 for funding this project. PBI Performance Products Inc. is thanked for supplying the PBI dope for the study.

Publisher Copyright:
© 2019 by the authors.

Keywords

Aquaporins
Biomimetic
Immobilization
Nanofiltration

ASJC Scopus subject areas

Bioengineering
Chemical Engineering (miscellaneous)
Process Chemistry and Technology

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10.3390/pr7020076

Cite this

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title = "Increasing salt rejection of polybenzimidazole nanofiltration membranes via the addition of immobilized and aligned aquaporins",

abstract = " Aquaporins are water channel proteins in cell membrane, highly specific for water molecules while restricting the passage of contaminants and small molecules, such as urea and boric acid. Cysteine functional groups were installed on aquaporin Z for covalent attachment to the polymer membrane matrix so that the proteins could be immobilized to the membranes and aligned in the direction of the flow. Depth profiling using x-ray photoelectron spectrometer (XPS) analysis showed the presence of functional groups corresponding to aquaporin Z modified with cysteine (Aqp-SH). Aqp-SH modified membranes showed a higher salt rejection as compared to unmodified membranes. For 2 M NaCl and CaCl 2 solutions, the rejection obtained from Aqp-SH membranes was 49.3 ± 7.5% and 59.1 ± 5.1%. On the other hand, the rejections obtained for 2 M NaCl and CaCl 2 solutions from unmodified membranes were 0.8 ± 0.4% and 1.3 ± 0.2% respectively. Furthermore, Aqp-SH membranes did not show a significant decrease in salt rejection with increasing feed concentrations, as was observed with other membranes. Through simulation studies, it was determined that there was approximately 24% capping of membrane pores by dispersed aquaporins.",

keywords = "Aquaporins, Biomimetic, Immobilization, Nanofiltration",

author = "Priyesh Wagh and Xinyi Zhang and Ryan Blood and Kekenes-Huskey, {Peter M.} and Prasangi Rajapaksha and Yinan Wei and Escobar, {Isabel C.}",

note = "Funding Information: This material is based upon work supported by the National Science Foundation under Cooperative Agreement No.1355438, and by the NSF KY EPSCoR Program and in addition the author acknowledges Center of Membrane Sciences at University of Kentucky. Research reported in this publication, release was supported by the Maximizing Investigators' Research Award (MIRA) (R35) from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under grant number R35GM124977. We further acknowledge support from the American Chemical Society Petroleum Research Fund 58719-DN16. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. In addition, the authors want to acknowledge the sources of funding, NSF 1308095 and USGS 104(b): Ohio Water Development Authority GRT00028988/60040357 for funding this project. PBI Performance Products Inc. is thanked for supplying the PBI dope for the study. Publisher Copyright: {\textcopyright} 2019 by the authors.",

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AU - Wagh, Priyesh

AU - Zhang, Xinyi

AU - Blood, Ryan

AU - Kekenes-Huskey, Peter M.

AU - Rajapaksha, Prasangi

AU - Wei, Yinan

AU - Escobar, Isabel C.

N1 - Funding Information: This material is based upon work supported by the National Science Foundation under Cooperative Agreement No.1355438, and by the NSF KY EPSCoR Program and in addition the author acknowledges Center of Membrane Sciences at University of Kentucky. Research reported in this publication, release was supported by the Maximizing Investigators' Research Award (MIRA) (R35) from the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) under grant number R35GM124977. We further acknowledge support from the American Chemical Society Petroleum Research Fund 58719-DN16. This work used the Extreme Science and Engineering Discovery Environment (XSEDE), which is supported by National Science Foundation grant number ACI-1548562. In addition, the authors want to acknowledge the sources of funding, NSF 1308095 and USGS 104(b): Ohio Water Development Authority GRT00028988/60040357 for funding this project. PBI Performance Products Inc. is thanked for supplying the PBI dope for the study. Publisher Copyright: © 2019 by the authors.

PY - 2019/2/1

Y1 - 2019/2/1

N2 - Aquaporins are water channel proteins in cell membrane, highly specific for water molecules while restricting the passage of contaminants and small molecules, such as urea and boric acid. Cysteine functional groups were installed on aquaporin Z for covalent attachment to the polymer membrane matrix so that the proteins could be immobilized to the membranes and aligned in the direction of the flow. Depth profiling using x-ray photoelectron spectrometer (XPS) analysis showed the presence of functional groups corresponding to aquaporin Z modified with cysteine (Aqp-SH). Aqp-SH modified membranes showed a higher salt rejection as compared to unmodified membranes. For 2 M NaCl and CaCl 2 solutions, the rejection obtained from Aqp-SH membranes was 49.3 ± 7.5% and 59.1 ± 5.1%. On the other hand, the rejections obtained for 2 M NaCl and CaCl 2 solutions from unmodified membranes were 0.8 ± 0.4% and 1.3 ± 0.2% respectively. Furthermore, Aqp-SH membranes did not show a significant decrease in salt rejection with increasing feed concentrations, as was observed with other membranes. Through simulation studies, it was determined that there was approximately 24% capping of membrane pores by dispersed aquaporins.

AB - Aquaporins are water channel proteins in cell membrane, highly specific for water molecules while restricting the passage of contaminants and small molecules, such as urea and boric acid. Cysteine functional groups were installed on aquaporin Z for covalent attachment to the polymer membrane matrix so that the proteins could be immobilized to the membranes and aligned in the direction of the flow. Depth profiling using x-ray photoelectron spectrometer (XPS) analysis showed the presence of functional groups corresponding to aquaporin Z modified with cysteine (Aqp-SH). Aqp-SH modified membranes showed a higher salt rejection as compared to unmodified membranes. For 2 M NaCl and CaCl 2 solutions, the rejection obtained from Aqp-SH membranes was 49.3 ± 7.5% and 59.1 ± 5.1%. On the other hand, the rejections obtained for 2 M NaCl and CaCl 2 solutions from unmodified membranes were 0.8 ± 0.4% and 1.3 ± 0.2% respectively. Furthermore, Aqp-SH membranes did not show a significant decrease in salt rejection with increasing feed concentrations, as was observed with other membranes. Through simulation studies, it was determined that there was approximately 24% capping of membrane pores by dispersed aquaporins.

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KW - Biomimetic

KW - Immobilization

KW - Nanofiltration

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Increasing salt rejection of polybenzimidazole nanofiltration membranes via the addition of immobilized and aligned aquaporins

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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