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Coating titania nanoparticles with epoxy-containing catechol polymers via Cu(0)-living radical polymerization as intelligent enzyme carriers
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Wang, Donghao, Ding, Wenyi, Zhou, Kaiyue, Guo, Shutong, Zhang, Qiang and Haddleton, David M. (2018) Coating titania nanoparticles with epoxy-containing catechol polymers via Cu(0)-living radical polymerization as intelligent enzyme carriers. Biomacromolecules, 19 (7). pp. 2979-2990. doi:10.1021/acs.biomac.8b00544
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WRAP-coating-titania-nanoparticles-epoxy-containing-catechol-polymers-Haddleton-2018.pdf - Accepted Version - Requires a PDF viewer. Download (1095Kb) | Preview |
Official URL: https://doi.org/10.1021/acs.biomac.8b00544
Abstract
Immobilization of enzyme could offer the biocatalyst with increased stability and important recoverability, which plays a vital role in the enzyme’s industrial applications. In this study, we present a new strategy to build an intelligent enzyme carrier by coating titania nanoparticles with thermoresponsive epoxy-functionalized polymers. Zero-valent copper-mediated living radical polymerization (Cu(0)-LRP) was utilized herein to copolymerize N-isopropylacrylamide (NIPAM) and glycidyl acrylate (GA) directly from an unprotected dopamine-functionalized initiator to obtain an epoxy-containing polymer with terminal anchor for the “grafting to” or “one-pot” modification of titania nanoparticles. A rhodamine B-labeled laccase has been subsequently used as a model enzyme for successful immobilization to yield an intelligent titania/laccase hybrid bifunctional catalyst. The immobilized laccase has shown excellent thermal stability under ambient or even relatively high temperature above the lower critical solution temperature (LCST) at which temperature the hybrid particles could be facilely recovered for reuse. The enzyme activity could be maintained during the repeated use after recovery and enzymatic degradation of bisphenol A was proven to be efficient. The photocatalytic ability of titania was also investigated by fast degradation of rhodamine B under the excitation of simulated sunlight. Therefore, this study has provided a facile strategy for the immobilization of metal oxide catalysts with enzymes, which constructs a novel bifunctional catalyst that will be promising for the “one-pot” degradation of different organic pollutants.
| Item Type: | Journal Article | |||||||||||||||
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| Subjects: | Q Science > QP Physiology R Medicine > RS Pharmacy and materia medica |
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| Divisions: | Faculty of Science > Chemistry | |||||||||||||||
| SWORD Depositor: | Library Publications Router | |||||||||||||||
| Library of Congress Subject Headings (LCSH): | Enzymes -- Industrial applications, Polymers, Nanoparticles, Titanium dioxide | |||||||||||||||
| Journal or Publication Title: | Biomacromolecules | |||||||||||||||
| Publisher: | American Chemical Society (ACS) | |||||||||||||||
| ISSN: | 1526-4602 | |||||||||||||||
| Official Date: | 9 July 2018 | |||||||||||||||
| Dates: |
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| Date of first compliant deposit: | 29 November 2018 | |||||||||||||||
| Volume: | 19 | |||||||||||||||
| Number: | 7 | |||||||||||||||
| Page Range: | pp. 2979-2990 | |||||||||||||||
| DOI: | 10.1021/acs.biomac.8b00544 | |||||||||||||||
| Status: | Peer Reviewed | |||||||||||||||
| Publication Status: | Published | |||||||||||||||
| Publisher Statement: | “This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biomacromolecules, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see ACS Articles on Request author-directed link to Published Work, see http://pubs.acs.org/page/policy/articlesonrequest/index.html].” | |||||||||||||||
| Access rights to Published version: | Restricted or Subscription Access | |||||||||||||||
| RIOXX Funder/Project Grant: |
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