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Agarose and Its Derivatives as Supports for Enzyme Immobilization
Agarose is a polysaccharide obtained from some seaweeds, with a quite particular structure that allows spontaneous gelation. Agarose-based beads are highly porous, mechanically resistant, chemically and physically inert, and sharply hydrophilic. These features—that could be further improved by means...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6273708/ https://www.ncbi.nlm.nih.gov/pubmed/27869778 http://dx.doi.org/10.3390/molecules21111577 |
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author | Zucca, Paolo Fernandez-Lafuente, Roberto Sanjust, Enrico |
author_facet | Zucca, Paolo Fernandez-Lafuente, Roberto Sanjust, Enrico |
author_sort | Zucca, Paolo |
collection | PubMed |
description | Agarose is a polysaccharide obtained from some seaweeds, with a quite particular structure that allows spontaneous gelation. Agarose-based beads are highly porous, mechanically resistant, chemically and physically inert, and sharply hydrophilic. These features—that could be further improved by means of covalent cross-linking—render them particularly suitable for enzyme immobilization with a wide range of derivatization methods taking advantage of chemical modification of a fraction of the polymer hydroxyls. The main properties of the polymer are described here, followed by a review of cross-linking and derivatization methods. Some recent, innovative procedures to optimize the catalytic activity and operational stability of the obtained preparations are also described, together with multi-enzyme immobilized systems and the main guidelines to exploit their performances. |
format | Online Article Text |
id | pubmed-6273708 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62737082018-12-28 Agarose and Its Derivatives as Supports for Enzyme Immobilization Zucca, Paolo Fernandez-Lafuente, Roberto Sanjust, Enrico Molecules Review Agarose is a polysaccharide obtained from some seaweeds, with a quite particular structure that allows spontaneous gelation. Agarose-based beads are highly porous, mechanically resistant, chemically and physically inert, and sharply hydrophilic. These features—that could be further improved by means of covalent cross-linking—render them particularly suitable for enzyme immobilization with a wide range of derivatization methods taking advantage of chemical modification of a fraction of the polymer hydroxyls. The main properties of the polymer are described here, followed by a review of cross-linking and derivatization methods. Some recent, innovative procedures to optimize the catalytic activity and operational stability of the obtained preparations are also described, together with multi-enzyme immobilized systems and the main guidelines to exploit their performances. MDPI 2016-11-19 /pmc/articles/PMC6273708/ /pubmed/27869778 http://dx.doi.org/10.3390/molecules21111577 Text en © 2016 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 (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Zucca, Paolo Fernandez-Lafuente, Roberto Sanjust, Enrico Agarose and Its Derivatives as Supports for Enzyme Immobilization |
title | Agarose and Its Derivatives as Supports for Enzyme Immobilization |
title_full | Agarose and Its Derivatives as Supports for Enzyme Immobilization |
title_fullStr | Agarose and Its Derivatives as Supports for Enzyme Immobilization |
title_full_unstemmed | Agarose and Its Derivatives as Supports for Enzyme Immobilization |
title_short | Agarose and Its Derivatives as Supports for Enzyme Immobilization |
title_sort | agarose and its derivatives as supports for enzyme immobilization |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6273708/ https://www.ncbi.nlm.nih.gov/pubmed/27869778 http://dx.doi.org/10.3390/molecules21111577 |
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