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Agarose and its derivatives as supports for enzyme immobilization

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos

Paolo Zucca 1, Roberto Fernandez-Lafuente 2, and Enrico Sanjust 1,*

1   Dipartimento di Scienze Biomediche, Università di Cagliari, Monserrato, Italy; pzucca@unica.it (P. Z.); sanjust@unica.it (E. S.)

2   Departamento de Biocatalisis, ICP-CSIC; C/ Marie Curie 2, Campus UAM-CSIC, Madrid 28049, Spain; rfl@icp.csic.es (R. F.-L.)


Agarose is a polysaccharide, coming from some seaweeds, with a quite particular structure allowing 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 from 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.

Palabras clave:enzymes; immobilization; stabilization; agar-agar; agarose; cross-linking; functionalization
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