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    Complexes of Magnetic Nanoparticles with Cellulose Nanocrystals as Regenerable, Highly Efficient, and Selective Platform for Protein Separation
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    † Department of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, FI-00076 Aalto, Finland
    ‡ Alabama Center for Paper and Bioresource Engineering, Department of Chemical Engineering, Auburn University, Auburn, Alabama 36849-5127, United States
    ∥ Department of Applied Physics, School of Science, Aalto University, FI-00076 Aalto, Finland
    ⊥ Departments of Forest Biomaterials and Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695, United States
    *E-mail: [email protected]
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    Biomacromolecules

    Cite this: Biomacromolecules 2017, 18, 3, 898–905
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    https://doi.org/10.1021/acs.biomac.6b01778
    Published February 15, 2017
    Copyright © 2017 American Chemical Society
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    Abstract

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    We present an efficient approach to develop cellulose nanocrystal (CNC) hybrids with magnetically responsive Fe3O4 nanoparticles that were synthesized using the (Fe3+/Fe2+) coprecipitation. After 2,2,6,6-tetramethylpiperidine-1-oxyl radical (TEMPO)-catalyzed oxidation of CNC, carbodiimide (EDC/NHS) was used for coupling amine-containing iron oxide nanoparticles that were achieved by dopamine ligand exchange (NH2–Fe3O4 NPs). The as-prepared hybrids (Fe3O4@CNC) were further complexed with Cu(II) ions to produce specific protein binding sites. The performance of magnetically responsive Cu–Fe3O4@CNC hybrids was assessed by selectively separating lysozyme from aqueous media. The hybrid system displayed a remarkable binding capacity with lysozyme of 860.6 ± 14.6 mg/g while near full protein recovery (∼98%) was achieved by simple elution. Moreover, the regeneration of Fe3O4@CNC hybrids and efficient reutilization for protein separation was demonstrated. Finally, lysozyme separation from matrices containing egg white was achieved, thus revealing the specificity and potential of the presented method.

    Copyright © 2017 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.biomac.6b01778.

    • Video of lysozyme separation with the assistance of magnet (AVI)

    • Experimental procedures of protein concentration analysis, SDS page analysis. TEM image of TEMPO-oxidation cellulose nanocrystals (TEMPO-CNC). Calculation method of degree of oxidation of TEMPO-CNC. The calibration curve for copper ions concentration. Zeta potential of NH2–Fe3O4 NPs. Stability test of Fe3O4 NPs (PDF)

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    Biomacromolecules

    Cite this: Biomacromolecules 2017, 18, 3, 898–905
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.biomac.6b01778
    Published February 15, 2017
    Copyright © 2017 American Chemical Society
    Request reuse permissions

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