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Molecules 2016, 21(11), 1577; doi:10.3390/molecules21111577

Agarose and Its Derivatives as Supports for Enzyme Immobilization

1
Dipartimento di Scienze Biomediche, Università di Cagliari, 09042 Monserrato (CA), Italy
2
Departamento de Biocatalisis, ICP-CSIC; C/Marie Curie 2, Campus UAM-CSIC, Madrid 28049, Spain
*
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 27 September 2016 / Revised: 12 November 2016 / Accepted: 16 November 2016 / Published: 19 November 2016
(This article belongs to the Special Issue Enzyme Immobilization 2016)
View Full-Text   |   Download PDF [2984 KB, uploaded 19 November 2016]   |  

Abstract

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. View Full-Text
Keywords: enzymes; immobilization; stabilization; agar-agar; agarose; cross-linking; functionalization enzymes; immobilization; stabilization; agar-agar; agarose; cross-linking; functionalization
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Zucca, P.; Fernandez-Lafuente, R.; Sanjust, E. Agarose and Its Derivatives as Supports for Enzyme Immobilization. Molecules 2016, 21, 1577.

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