A hydrogel-based enzyme-loaded polymersome reactor

In this study we report the immobilization of enzyme-containing polymersomes into a macromolecular hydrogel. Whereas free enzyme shows progressive leakage from the hydrogel in a period of days, leakage of the polymersome-protected enzyme is virtually absent. The preparation of the hydrogel occurs un...

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Published in:Nanoscale
Main Authors: De Hoog, Hans-Peter M., Arends, Isabel W. C. E., Rowan, Alan E., Cornelissen, Jeroen J. L. M., Nolte, Roeland J. M.
Format: Article in Journal/Newspaper
Language:English
Published: Royal Society of Chemistry 2010
Subjects:
Online Access:https://espace.library.uq.edu.au/view/UQ:596255
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spelling ftunivqespace:oai:espace.library.uq.edu.au:UQ:596255 2023-05-15T13:59:53+02:00 A hydrogel-based enzyme-loaded polymersome reactor De Hoog, Hans-Peter M. Arends, Isabel W. C. E. Rowan, Alan E. Cornelissen, Jeroen J. L. M. Nolte, Roeland J. M. 2010-05-01 https://espace.library.uq.edu.au/view/UQ:596255 eng eng Royal Society of Chemistry doi:10.1039/b9nr00325h issn:2040-3364 issn:2040-3372 orcid:0000-0003-0728-3851 Chemistry Multidisciplinary Nanoscience & Nanotechnology Materials Science Physics Applied Science & Technology - Other Topics 2500 Materials Science Journal Article 2010 ftunivqespace https://doi.org/10.1039/b9nr00325h 2020-10-27T03:53:45Z In this study we report the immobilization of enzyme-containing polymersomes into a macromolecular hydrogel. Whereas free enzyme shows progressive leakage from the hydrogel in a period of days, leakage of the polymersome-protected enzyme is virtually absent. The preparation of the hydrogel occurs under mild conditions and does not inhibit the activity of the encapsulated enzymes nor does it affect the structure of the polymersomes. The stability of the polymersome hydrogel architecture is demonstrated by the facile recycling of the polymersomes and their use in repeated reaction cycles. A 'continuous-flow polymersome reactor' is constructed in which substrate is added to the top of the reactor and product is collected at the bottom. This set-up allows the use of different enzymes and the processing of multiple substrates, as is demonstrated by the conversion of 2-methoxyphenyl acetate to tetraguaiacol in a reactor loaded with polymersome hydrogels containing the enzymes Candida antarctica lipase B (CALB) and glucose oxidase (GOx). Article in Journal/Newspaper Antarc* Antarctica The University of Queensland: UQ eSpace Nanoscale 2 5 709
institution Open Polar
collection The University of Queensland: UQ eSpace
op_collection_id ftunivqespace
language English
topic Chemistry
Multidisciplinary
Nanoscience & Nanotechnology
Materials Science
Physics
Applied
Science & Technology - Other Topics
2500 Materials Science
spellingShingle Chemistry
Multidisciplinary
Nanoscience & Nanotechnology
Materials Science
Physics
Applied
Science & Technology - Other Topics
2500 Materials Science
De Hoog, Hans-Peter M.
Arends, Isabel W. C. E.
Rowan, Alan E.
Cornelissen, Jeroen J. L. M.
Nolte, Roeland J. M.
A hydrogel-based enzyme-loaded polymersome reactor
topic_facet Chemistry
Multidisciplinary
Nanoscience & Nanotechnology
Materials Science
Physics
Applied
Science & Technology - Other Topics
2500 Materials Science
description In this study we report the immobilization of enzyme-containing polymersomes into a macromolecular hydrogel. Whereas free enzyme shows progressive leakage from the hydrogel in a period of days, leakage of the polymersome-protected enzyme is virtually absent. The preparation of the hydrogel occurs under mild conditions and does not inhibit the activity of the encapsulated enzymes nor does it affect the structure of the polymersomes. The stability of the polymersome hydrogel architecture is demonstrated by the facile recycling of the polymersomes and their use in repeated reaction cycles. A 'continuous-flow polymersome reactor' is constructed in which substrate is added to the top of the reactor and product is collected at the bottom. This set-up allows the use of different enzymes and the processing of multiple substrates, as is demonstrated by the conversion of 2-methoxyphenyl acetate to tetraguaiacol in a reactor loaded with polymersome hydrogels containing the enzymes Candida antarctica lipase B (CALB) and glucose oxidase (GOx).
format Article in Journal/Newspaper
author De Hoog, Hans-Peter M.
Arends, Isabel W. C. E.
Rowan, Alan E.
Cornelissen, Jeroen J. L. M.
Nolte, Roeland J. M.
author_facet De Hoog, Hans-Peter M.
Arends, Isabel W. C. E.
Rowan, Alan E.
Cornelissen, Jeroen J. L. M.
Nolte, Roeland J. M.
author_sort De Hoog, Hans-Peter M.
title A hydrogel-based enzyme-loaded polymersome reactor
title_short A hydrogel-based enzyme-loaded polymersome reactor
title_full A hydrogel-based enzyme-loaded polymersome reactor
title_fullStr A hydrogel-based enzyme-loaded polymersome reactor
title_full_unstemmed A hydrogel-based enzyme-loaded polymersome reactor
title_sort hydrogel-based enzyme-loaded polymersome reactor
publisher Royal Society of Chemistry
publishDate 2010
url https://espace.library.uq.edu.au/view/UQ:596255
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_relation doi:10.1039/b9nr00325h
issn:2040-3364
issn:2040-3372
orcid:0000-0003-0728-3851
op_doi https://doi.org/10.1039/b9nr00325h
container_title Nanoscale
container_volume 2
container_issue 5
container_start_page 709
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