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Title: Confocal Raman Microscopy for the Determination of Protein and Quaternary Ammonium Ion Loadings in Biocatalytic Membranes for Electrochemical Energy Conversion and Storage

Abstract

Here, the need to immobilize active enzyme, while ensuring high rates of substrate turnover and electronic charge transfer with an electrode, is a centrally important challenge in the field of bioelectrocatalysis. In this work, we demonstrate the use of confocal Raman microscopy as a tool for quantitation and molecular-scale structural characterization of ionomers and proteins within biocatalytic membranes to aid in the development of energy efficient biofuel cells. A set of recently available short side chain Aquivion ionomers spanning a range of equivalent weight (EW) suitable for enzyme immobilization was investigated. Aquivion ionomers (790 EW, 830 EW and 980 EW) received in the proton-exchanged (SO3H) form were treated with tetra-n-butylammonium bromide (TBAB) to neutralize the ionomer and expand the size of ionic domains for enzyme incorporation. Through the use of confocal Raman microscopy, membrane TBA+ ion content was predicted in calibration studies to within a few percent of the conventional titrimetric method across the full range of TBA+ : SO3- ratios of practical interest (0.1 to 1.7). Protein incorporation into membranes was quantified at the levels expected in biofuel cell electrodes. Furthermore, features associated with the catalytically active, enzyme-coordinated copper center were evident between 400 cm-1 - 500 cm-1 inmore » spectra of laccase catalytic membranes, demonstrating the potential to interrogate mechanistic chemistry at the enzyme active site of biocathodes under fuel cell reaction conditions. When benchmarked against the 1100 EW Nafion ionomer in glucose/air enzymatic fuel cells (EFCs), EFCs with laccase air-breathing cathodes prepared from TBA+ modified Aquivion ionomers were able to reach maximum power densities (Pmax) up to 1.5 times higher than EFCs constructed with cathodes prepared from TBA+ modified Nafion. The improved performance of EFCs containing the short side chain Aquivion ionomers relative to Nafion is traced to effects of ionomer ion-exchange capacity (IEC, where IEC = EW-1), where the greater density of SO3- moieties in the Aquivion materials produces an environment more favourable to mass transport and higher TBA+ concentrations.« less

Authors:
 [1];  [1];  [1];  [1];  [1];  [1];  [2]
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  1. Univ. of Utah, Salt Lake City, UT (United States)
  2. Univ. of Utah, Salt Lake City, UT (United States); Texas Tech Univ., Lubbock, TX (United States)
Publication Date:
Research Org.:
Univ. of Utah, Salt Lake City, UT (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Contributing Org.:
Texas Tech University, Lubbock, TX 79416
OSTI Identifier:
1408778
Grant/Contract Number:  
FG03-93ER14333
Resource Type:
Accepted Manuscript
Journal Name:
Analytical Chemistry
Additional Journal Information:
Journal Volume: 89; Journal Issue: 24; Journal ID: ISSN 0003-2700
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
77 NANOSCIENCE AND NANOTECHNOLOGY; 36 MATERIALS SCIENCE; membrane separations; fuel cells; biocatalysis

Citation Formats

Cai, Rong, Abdellaoui, Sofiene, Kitt, Jay P., Irvine, Cullen, Harris, Joel M., Minteer, Shelley D., and Korzeniewski, Carol. Confocal Raman Microscopy for the Determination of Protein and Quaternary Ammonium Ion Loadings in Biocatalytic Membranes for Electrochemical Energy Conversion and Storage. United States: N. p., 2017. Web. doi:10.1021/acs.analchem.7b03380.
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Cai, Rong, Abdellaoui, Sofiene, Kitt, Jay P., Irvine, Cullen, Harris, Joel M., Minteer, Shelley D., & Korzeniewski, Carol. Confocal Raman Microscopy for the Determination of Protein and Quaternary Ammonium Ion Loadings in Biocatalytic Membranes for Electrochemical Energy Conversion and Storage. United States. https://doi.org/10.1021/acs.analchem.7b03380
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Cai, Rong, Abdellaoui, Sofiene, Kitt, Jay P., Irvine, Cullen, Harris, Joel M., Minteer, Shelley D., and Korzeniewski, Carol. Tue . "Confocal Raman Microscopy for the Determination of Protein and Quaternary Ammonium Ion Loadings in Biocatalytic Membranes for Electrochemical Energy Conversion and Storage". United States. https://doi.org/10.1021/acs.analchem.7b03380. https://www.osti.gov/servlets/purl/1408778.
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@article{osti_1408778,
title = {Confocal Raman Microscopy for the Determination of Protein and Quaternary Ammonium Ion Loadings in Biocatalytic Membranes for Electrochemical Energy Conversion and Storage},
author = {Cai, Rong and Abdellaoui, Sofiene and Kitt, Jay P. and Irvine, Cullen and Harris, Joel M. and Minteer, Shelley D. and Korzeniewski, Carol},
abstractNote = {Here, the need to immobilize active enzyme, while ensuring high rates of substrate turnover and electronic charge transfer with an electrode, is a centrally important challenge in the field of bioelectrocatalysis. In this work, we demonstrate the use of confocal Raman microscopy as a tool for quantitation and molecular-scale structural characterization of ionomers and proteins within biocatalytic membranes to aid in the development of energy efficient biofuel cells. A set of recently available short side chain Aquivion ionomers spanning a range of equivalent weight (EW) suitable for enzyme immobilization was investigated. Aquivion ionomers (790 EW, 830 EW and 980 EW) received in the proton-exchanged (SO3H) form were treated with tetra-n-butylammonium bromide (TBAB) to neutralize the ionomer and expand the size of ionic domains for enzyme incorporation. Through the use of confocal Raman microscopy, membrane TBA+ ion content was predicted in calibration studies to within a few percent of the conventional titrimetric method across the full range of TBA+ : SO3- ratios of practical interest (0.1 to 1.7). Protein incorporation into membranes was quantified at the levels expected in biofuel cell electrodes. Furthermore, features associated with the catalytically active, enzyme-coordinated copper center were evident between 400 cm-1 - 500 cm-1 in spectra of laccase catalytic membranes, demonstrating the potential to interrogate mechanistic chemistry at the enzyme active site of biocathodes under fuel cell reaction conditions. When benchmarked against the 1100 EW Nafion ionomer in glucose/air enzymatic fuel cells (EFCs), EFCs with laccase air-breathing cathodes prepared from TBA+ modified Aquivion ionomers were able to reach maximum power densities (Pmax) up to 1.5 times higher than EFCs constructed with cathodes prepared from TBA+ modified Nafion. The improved performance of EFCs containing the short side chain Aquivion ionomers relative to Nafion is traced to effects of ionomer ion-exchange capacity (IEC, where IEC = EW-1), where the greater density of SO3- moieties in the Aquivion materials produces an environment more favourable to mass transport and higher TBA+ concentrations.},
doi = {10.1021/acs.analchem.7b03380},
journal = {Analytical Chemistry},
number = 24,
volume = 89,
place = {United States},
year = {Tue Nov 14 00:00:00 EST 2017},
month = {Tue Nov 14 00:00:00 EST 2017}
}
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    Infrared Microscopy as a Probe of Composition within a Model Biofuel Cell Electrode Prepared from Trametes versicolor Laccase
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