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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...

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Detalles Bibliográficos
Autores principales: Ni, Kefeng, Zhou, Xu, Zhao, Li, Wang, Hualei, Ren, Yuhong, Wei, Dongzhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
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.
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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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