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Hydrophobic and Bulk Polymerizable Protein-Based Elastomers Compatibilized with Surfactants

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    Research Article

    Hydrophobic and Bulk Polymerizable Protein-Based Elastomers Compatibilized with Surfactants
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    • W. Y. Chan
      W. Y. Chan
      Department of Chemical Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States
      More by W. Y. Chan
    • E. J. King
      E. J. King
      Wellesley College, 106 Central Sreet, Wellesley, Massachusetts 02481, United States
      More by E. J. King
    • B. D. Olsen*
      B. D. Olsen
      Department of Chemical Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States
      *E-mail: [email protected]
      More by B. D. Olsen
      Orcidhttp://orcid.org/0000-0002-7272-7140
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    ACS Sustainable Chemistry & Engineering

    Cite this: ACS Sustainable Chem. Eng. 2019, 7, 10, 9103–9111
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    https://doi.org/10.1021/acssuschemeng.8b03557
    Published April 29, 2019
    Copyright © 2019 American Chemical Society
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    Abstract

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    Proteins have great potential as biomass-derived feedstocks for material synthesis and can form strong materials due to their highly hydrogen-bonded nature. Elastomers comprised of proteins and a synthetic rubbery polymer were prepared by copolymerizing a methacrylated protein and a vinyl monomer, where proteins function as macro-cross-linkers and reinforcing fillers. Selecting a hydrophobic synthetic polymer block partially mitigates the moisture absorption of protein-based materials while maintaining desirable levels of mechanical properties. The use of a hydrophobic monomer is enabled by the use of surfactants that function as compatibilizers, since proteins are generally insoluble in organic solvents and vinyl monomers. Surfactants also lower the softening temperature of proteins, allowing materials to be fabricated solvent free using thermoplastic processing techniques. The preparation of a polyacrylate network toughened through incorporation of protein cross-linking domains is demonstrated using whey protein, the cationic surfactant benzalkonium chloride, and the hydrophobic monomer n-butyl acrylate. The resulting materials are amorphous and disordered but have microphase-separated protein-rich and polyacrylate-rich domains. All materials soften with increasing relative humidity, but the presence of a hydrophobic polyacrylate decreases the material’s moisture absorption at high humidity levels when compared to pure protein and networks comprised of a hydrophilic polyacrylate.

    Copyright © 2019 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/acssuschemeng.8b03557.

    • Reaction scheme for protein methacrylation and copolymerization; mechanical properties of materials polymerized at different molding pressures; thermogravimetric analysis of protein–surfactant–polyacrylate copolymer equilibrated at various humidity levels; comparison of small-angle X-ray scattering curves between cross-linked protein–surfactant–polyacrylate at various relative humidity levels and between blends and materials with different cross-linking densities; surfactant peak positions in wide-angle X-ray scattering curves; images of a protein–surfactant complex and a protein–surfactant–polyacrylate under a cross polarizer at 0% and 50% strain; small-angle X-ray scattering curve for the protein–surfactant complex; comparison of mechanical properties between a cross-linked protein–surfactant–polyacrylate, protein–surfactant complex, and a cross-linked polyacrylate homopolymer control; swelling ratio of blend and copolymers with various cross-linking densities (PDF)

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    This article is cited by 6 publications.

    1. Yiping Cao, Bradley D. Olsen. Strengthening and Toughening of Protein-Based Thermosets via Intermolecular Self-Assembly. Biomacromolecules 2022, 23 (8) , 3286-3295. https://doi.org/10.1021/acs.biomac.2c00372
    2. Masih Karimi Alavijeh, Anne S. Meyer, Sally L. Gras, Sandra E. Kentish. Improving β-Galactosidase-Catalyzed Transglycosylation Yields by Cross-Linked Layer-by-Layer Enzyme Immobilization. ACS Sustainable Chemistry & Engineering 2020, 8 (43) , 16205-16216. https://doi.org/10.1021/acssuschemeng.0c05186
    3. Wui Yarn Chan. Proteins in the design of sustainable plastics alternatives. MRS Communications 2023, 13 (6) , 1009-1024. https://doi.org/10.1557/s43579-023-00481-9
    4. Jhenifer Stefani Lopes, Marina Fernandes Cosate de Andrade, Ana Rita Morales. Effect of Cetylpyridinium Chloride Surfactant and Polyethylene Glycol on the Process and Properties of Whey Protein Isolate Modification. Journal of Polymers and the Environment 2023, 31 (11) , 4703-4713. https://doi.org/10.1007/s10924-023-02894-y
    5. Emil Andersen, Wui Yarn Chan, Sarah Av-Ron, Hursh V. Sureka, Bradley D. Olsen. Tuning compatibility and water uptake by protein charge modification in melt-polymerizable protein-based thermosets. Materials Advances 2022, 3 (4) , 2158-2169. https://doi.org/10.1039/D1MA00485A
    6. Marina P. Chang, Winnie Huang, Danielle J. Mai. Monomer‐scale design of functional protein polymers using consensus repeat sequences. Journal of Polymer Science 2021, 59 (22) , 2644-2664. https://doi.org/10.1002/pol.20210506
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    ACS Sustainable Chemistry & Engineering

    Cite this: ACS Sustainable Chem. Eng. 2019, 7, 10, 9103–9111
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acssuschemeng.8b03557
    Published April 29, 2019
    Copyright © 2019 American Chemical Society
    Request reuse permissions

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