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  • Self-assembly of amyloid fibrils that display active enzymes

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    Author(s)
    Zhou, Xiao-Ming
    Entwistle, Aiman
    Zhang, Hong
    Jackson, Antony P
    Mason, Thomas O
    Shimanovich, Ulyana
    Knowles, Tuomas PJ
    Smith, Andrew T
    Sawyer, Elizabeth B
    Perrett, Sarah
    Griffith University Author(s)
    Smith, Andrew T.
    Year published
    2014
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    Abstract
    Enzyme immobilization is an important strategy to enhance the stability and recoverability of enzymes and to facilitate the separation of enzymes from reaction products. However, enzyme purification followed by separate chemical steps to allow immobilization on a solid support reduces the efficiency and yield of the active enzyme. Here we describe polypeptide constructs that self-assemble spontaneously into nanofibrils with fused active enzyme subunits displayed on the amyloid fibril surface. We measured the steady-state kinetic parameters for the appended enzymes in situ within fibrils and compare these with the identical ...
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    Enzyme immobilization is an important strategy to enhance the stability and recoverability of enzymes and to facilitate the separation of enzymes from reaction products. However, enzyme purification followed by separate chemical steps to allow immobilization on a solid support reduces the efficiency and yield of the active enzyme. Here we describe polypeptide constructs that self-assemble spontaneously into nanofibrils with fused active enzyme subunits displayed on the amyloid fibril surface. We measured the steady-state kinetic parameters for the appended enzymes in situ within fibrils and compare these with the identical protein constructs in solution. Finally, we demonstrated that the fibrils can be recycled and reused in functional assays both in conventional batch processes and in a continuous-flow microreactor.
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    Journal Title
    ChemCatChem
    Volume
    6
    Issue
    7
    DOI
    https://doi.org/10.1002/cctc.201402125
    Copyright Statement
    © 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
    Subject
    Inorganic Chemistry not elsewhere classified
    Inorganic Chemistry
    Physical Chemistry (incl. Structural)
    Chemical Engineering
    Publication URI
    http://hdl.handle.net/10072/171970
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    • Journal articles

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