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PublicationCatalysts
Year2017
Volume7
Pages250
International

Exploiting the Versatility of Aminated Supports Activated with Glutaraldehyde to Immobilize β-galactosidase from Aspergillus oryzae

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Hadjer Zaak 1,2,3, Sara Peirce 1,4, Tiago L. de Albuquerque 1,5, Mohamed Sassi *,3 and Roberto Fernandez-Lafuente 1,*
1   Departamento de Biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid, Spain; rfl@icp.csic.es, (RFL)
2   Food Biotechnology Division, Biotechnology Research Center (CRBt), Algeria; hadjer.zaak@yahoo.fr, (HZ)
3   Nature and life Science Faculty, Ibn Khaldoun University, Algeria; mo_sassi@yahoo.fr, (MS)
4   Dipartimento di Ingegneria Chimica, dei Materiali e della Produzione Industriale – Università degli Studi di Napoli Federico II, P.le V. Tecchio 80, 80125 Napoli (Italy); sara.peirce@unina.it, (SP)
5   Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, CEP 60455-760, Fortaleza, CE, Brazil; tiagotla1@gmail.com, (TLA)


.The enzyme β-galactosidase from Aspergillus oryzae has been immobilized in aminated (MANAE)-agarose beads via glutaraldehyde chemistry using different strategies. The immobilization on MANAE-supports was first assayed at different pH values (this gave different stabilities to the immobilized enzymes) and further modified with glutaraldehyde. Dramatic drops in activity were found, even using 0.1% (v/v) glutaraldehyde. The use of a support with lower activation permitted to get a final activity of 30%, but stability was almost identical to that of the just adsorbed enzyme. Next, the immobilization on pre-activated glutaraldehyde beads was assayed at pH 5, 7 and 9. At pH 7 full, rapid immobilization and a high expressed enzyme activity were accomplished. At pH 9 some decrease in enzyme activity was observed. Direct covalent immobilization of the enzyme was very slow, even reducing the volume of enzyme /support ratio the yield was not complete after 24 h. The stability of the biocatalyst using pre-activated supports was about 4-6 folds more stable than that of the enzyme immobilized via ion exchange at pH 5, with small differences among them. Thus the immobilization of the enzyme at pH 7 at low ionic strength on pre-activated glutaraldehyde supports seems to be the most adequate in terms of activity, stability and immobilization rate.

Keywords:Enzyme stabilization, Enzyme immobilization, glutaraldehyde, Enzyme inactivation
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