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Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization
We report on the synthesis and application of a new hydrogel based on a methacrylate substituted polyphosphazene. Through ring-opening polymerization and nucleophilic substitution, poly[bis(methacrylate)phosphazene] (PBMAP) was successfully synthesized from hexachlorocyclotriphosphazene. By adding P...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270993/ https://www.ncbi.nlm.nih.gov/pubmed/25006790 http://dx.doi.org/10.3390/molecules19079850 |
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author | Qian, Yue-Cheng Chen, Peng-Cheng He, Gui-Jin Huang, Xiao-Jun Xu, Zhi-Kang |
author_facet | Qian, Yue-Cheng Chen, Peng-Cheng He, Gui-Jin Huang, Xiao-Jun Xu, Zhi-Kang |
author_sort | Qian, Yue-Cheng |
collection | PubMed |
description | We report on the synthesis and application of a new hydrogel based on a methacrylate substituted polyphosphazene. Through ring-opening polymerization and nucleophilic substitution, poly[bis(methacrylate)phosphazene] (PBMAP) was successfully synthesized from hexachlorocyclotriphosphazene. By adding PBMAP to methacrylic acid solution and then treating with UV light, we could obtain a cross-linked polyphosphazene network, which showed an ultra-high absorbency for distilled water. Lipase from Candida rugosa was used as the model lipase for entrapment immobilization in the hydrogel. The influence of methacrylic acid concentration on immobilization efficiency was studied. Results showed that enzyme loading reached a maximum of 24.02 mg/g with an activity retention of 67.25% when the methacrylic acid concentration was 20% (w/w). |
format | Online Article Text |
id | pubmed-6270993 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62709932018-12-21 Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization Qian, Yue-Cheng Chen, Peng-Cheng He, Gui-Jin Huang, Xiao-Jun Xu, Zhi-Kang Molecules Article We report on the synthesis and application of a new hydrogel based on a methacrylate substituted polyphosphazene. Through ring-opening polymerization and nucleophilic substitution, poly[bis(methacrylate)phosphazene] (PBMAP) was successfully synthesized from hexachlorocyclotriphosphazene. By adding PBMAP to methacrylic acid solution and then treating with UV light, we could obtain a cross-linked polyphosphazene network, which showed an ultra-high absorbency for distilled water. Lipase from Candida rugosa was used as the model lipase for entrapment immobilization in the hydrogel. The influence of methacrylic acid concentration on immobilization efficiency was studied. Results showed that enzyme loading reached a maximum of 24.02 mg/g with an activity retention of 67.25% when the methacrylic acid concentration was 20% (w/w). MDPI 2014-07-08 /pmc/articles/PMC6270993/ /pubmed/25006790 http://dx.doi.org/10.3390/molecules19079850 Text en © 2014 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Qian, Yue-Cheng Chen, Peng-Cheng He, Gui-Jin Huang, Xiao-Jun Xu, Zhi-Kang Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization |
title | Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization |
title_full | Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization |
title_fullStr | Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization |
title_full_unstemmed | Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization |
title_short | Preparation of Polyphosphazene Hydrogels for Enzyme Immobilization |
title_sort | preparation of polyphosphazene hydrogels for enzyme immobilization |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270993/ https://www.ncbi.nlm.nih.gov/pubmed/25006790 http://dx.doi.org/10.3390/molecules19079850 |
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