Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/94036
Title: A hydrogel-based enzyme-loaded polymersome reactor
Authors: De Hoog, Hans-Peter M.
Arends, Isabel W. C. E.
Rowan, Alan E.
Cornelissen, Jeroen J. L. M.
Nolte, Roeland J. M.
Keywords: DRNTU::Engineering::Materials::Biomaterials
Issue Date: 2010
Source: De Hoog, H. P. M., Arends, I. W. C. E., Rowan, A. E., Cornelissen, J. J. L. M., & Nolte, R. J. M. (2010). A hydrogel-based enzyme-loaded polymersome reactor. Nanoscale, 2, 709-716.
Series/Report no.: Nanoscale
Abstract: 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 antarcticalipase B (CALB) and glucose oxidase (GOx).
URI: https://hdl.handle.net/10356/94036
http://hdl.handle.net/10220/6970
ISSN: 2040-3364
DOI: 10.1039/b9nr00325h
Rights: © 2010 The Royal Society of Chemistry. This is the author created version of a work that has been peer reviewed and accepted for publication by Nanoscale, The Royal Society of Chemistry.  It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at: [DOI: http://dx.doi.org/10.1039/b9nr00325h].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:MSE Journal Articles

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