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Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations

Enzymes are attractive, “green” alternatives to chemical catalysts within the industrial sector, but their robustness to environmental conditions needs optimizing. Here, an enzyme is tagged chemically and recombinantly with a self-assembling peptide that allows the conjugate to spontaneously assembl...

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Detalles Bibliográficos
Autores principales: Hickling, Christopher, Toogood, Helen S, Saiani, Alberto, Scrutton, Nigel S, Miller, Aline F
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BlackWell Publishing Ltd 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4316184/
https://www.ncbi.nlm.nih.gov/pubmed/24604676
http://dx.doi.org/10.1002/marc.201400027
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author Hickling, Christopher
Toogood, Helen S
Saiani, Alberto
Scrutton, Nigel S
Miller, Aline F
author_facet Hickling, Christopher
Toogood, Helen S
Saiani, Alberto
Scrutton, Nigel S
Miller, Aline F
author_sort Hickling, Christopher
collection PubMed
description Enzymes are attractive, “green” alternatives to chemical catalysts within the industrial sector, but their robustness to environmental conditions needs optimizing. Here, an enzyme is tagged chemically and recombinantly with a self-assembling peptide that allows the conjugate to spontaneously assemble with pure peptide to form β-sheet-rich nanofibers decorated with tethered enzyme. Above a critical concentration, these fibers entangle and form a 3D hydrogel. The immobilized enzyme catalyzes chemical transformations and critically its stability is increased significantly where it retains activity after exposure to high temperatures (90 °C) and long storage times (up to 12 months).
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spelling pubmed-43161842015-02-11 Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations Hickling, Christopher Toogood, Helen S Saiani, Alberto Scrutton, Nigel S Miller, Aline F Macromol Rapid Commun Communications Enzymes are attractive, “green” alternatives to chemical catalysts within the industrial sector, but their robustness to environmental conditions needs optimizing. Here, an enzyme is tagged chemically and recombinantly with a self-assembling peptide that allows the conjugate to spontaneously assemble with pure peptide to form β-sheet-rich nanofibers decorated with tethered enzyme. Above a critical concentration, these fibers entangle and form a 3D hydrogel. The immobilized enzyme catalyzes chemical transformations and critically its stability is increased significantly where it retains activity after exposure to high temperatures (90 °C) and long storage times (up to 12 months). BlackWell Publishing Ltd 2014-05 2014-03-07 /pmc/articles/PMC4316184/ /pubmed/24604676 http://dx.doi.org/10.1002/marc.201400027 Text en © 2014 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim http://creativecommons.org/licenses/by/3.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Hickling, Christopher
Toogood, Helen S
Saiani, Alberto
Scrutton, Nigel S
Miller, Aline F
Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations
title Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations
title_full Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations
title_fullStr Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations
title_full_unstemmed Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations
title_short Nanofibrillar Peptide Hydrogels for the Immobilization of Biocatalysts for Chemical Transformations
title_sort nanofibrillar peptide hydrogels for the immobilization of biocatalysts for chemical transformations
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4316184/
https://www.ncbi.nlm.nih.gov/pubmed/24604676
http://dx.doi.org/10.1002/marc.201400027
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