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Open AccessCommentary
Molecules 2016, 21(7), 919;

Solid-State Metalloproteins—An Alternative to Immobilisation

Commonwealth Scientific and Industrial Research Organisation (CSIRO), Black Mountain, Canberra, ACT 2601, Australia
Academic Editor: Roberto Fernandez-Lafuente
Received: 12 May 2016 / Revised: 7 July 2016 / Accepted: 8 July 2016 / Published: 14 July 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
Full-Text   |   PDF [729 KB, uploaded 14 July 2016]   |  


This commentary outlines a protein engineering approach as an alternative to immobilisation developed in our laboratory. We use a recombinant silk protein into which metal active sites can be incorporated to produce solid-state metalloprotein materials. The silk protein directly coordinates to the metal centres providing control over their reactivity akin to that seen in naturally occurring metalloproteins. These solid-state materials are remarkably stable at a range of temperatures and different solvent conditions. I discuss the genesis of this approach and highlight areas where such solid-state materials could find application. View Full-Text
Keywords: biocatalysis; industrial biotechnology; silk; biosensors; de novo engineering biocatalysis; industrial biotechnology; silk; biosensors; de novo engineering

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Rapson, T.D. Solid-State Metalloproteins—An Alternative to Immobilisation. Molecules 2016, 21, 919.

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