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Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase
The magnetic chitosan nanocomposites have been studied intensively and been used practically in various biomedical and biological applications including enzyme immobilization. However, the loading capacity and the remained activity of immobilized enzyme based on existing approaches are not satisfied...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3398885/ https://www.ncbi.nlm.nih.gov/pubmed/22815930 http://dx.doi.org/10.1371/journal.pone.0041101 |
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author | Ni, Kefeng Zhou, Xu Zhao, Li Wang, Hualei Ren, Yuhong Wei, Dongzhi |
author_facet | Ni, Kefeng Zhou, Xu Zhao, Li Wang, Hualei Ren, Yuhong Wei, Dongzhi |
author_sort | Ni, Kefeng |
collection | PubMed |
description | The magnetic chitosan nanocomposites have been studied intensively and been used practically in various biomedical and biological applications including enzyme immobilization. However, the loading capacity and the remained activity of immobilized enzyme based on existing approaches are not satisfied. Simpler and more effective immobilization strategies are needed. Here we report a simple catechol modified protocol for preparing a novel catechol-chitosan (CCS) - iron oxide nanoparticles (IONPs) composites carrying adhesive moieties with strong surface affinity. The ω-transaminase (ω-TA) was immobilized onto this magnetic composite via nucleophilic reactions between catechol and ω-TA. Under optimal conditions, 87.5% of the available ω-TA was immobilized on the composite, yielding an enzyme loading capacity as high as 681.7 mg/g. Furthermore, the valuation of enzyme activity showed that ω-TA immobilized on CCS-IONPs displayed enhanced pH and thermal stability compared to free enzyme. Importantly, the immobilized ω-TA retained more than 50% of its initial activity after 15 repeated reaction cycles using magnetic separation and 61.5% of its initial activity after storage at 4°C in phosphate buffered saline (PBS) for 15 days. The results suggested that such adhesive magnetic composites may provide an improved platform technology for bio-macromolecules immobilized. |
format | Online Article Text |
id | pubmed-3398885 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33988852012-07-19 Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase Ni, Kefeng Zhou, Xu Zhao, Li Wang, Hualei Ren, Yuhong Wei, Dongzhi PLoS One Research Article The magnetic chitosan nanocomposites have been studied intensively and been used practically in various biomedical and biological applications including enzyme immobilization. However, the loading capacity and the remained activity of immobilized enzyme based on existing approaches are not satisfied. Simpler and more effective immobilization strategies are needed. Here we report a simple catechol modified protocol for preparing a novel catechol-chitosan (CCS) - iron oxide nanoparticles (IONPs) composites carrying adhesive moieties with strong surface affinity. The ω-transaminase (ω-TA) was immobilized onto this magnetic composite via nucleophilic reactions between catechol and ω-TA. Under optimal conditions, 87.5% of the available ω-TA was immobilized on the composite, yielding an enzyme loading capacity as high as 681.7 mg/g. Furthermore, the valuation of enzyme activity showed that ω-TA immobilized on CCS-IONPs displayed enhanced pH and thermal stability compared to free enzyme. Importantly, the immobilized ω-TA retained more than 50% of its initial activity after 15 repeated reaction cycles using magnetic separation and 61.5% of its initial activity after storage at 4°C in phosphate buffered saline (PBS) for 15 days. The results suggested that such adhesive magnetic composites may provide an improved platform technology for bio-macromolecules immobilized. Public Library of Science 2012-07-17 /pmc/articles/PMC3398885/ /pubmed/22815930 http://dx.doi.org/10.1371/journal.pone.0041101 Text en Ni et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ni, Kefeng Zhou, Xu Zhao, Li Wang, Hualei Ren, Yuhong Wei, Dongzhi Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase |
title | Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase |
title_full | Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase |
title_fullStr | Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase |
title_full_unstemmed | Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase |
title_short | Magnetic Catechol-Chitosan with Bioinspired Adhesive Surface: Preparation and Immobilization of ω-Transaminase |
title_sort | magnetic catechol-chitosan with bioinspired adhesive surface: preparation and immobilization of ω-transaminase |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3398885/ https://www.ncbi.nlm.nih.gov/pubmed/22815930 http://dx.doi.org/10.1371/journal.pone.0041101 |
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