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Catalysts 2017, 7(9), 250; doi:10.3390/catal7090250

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

1
Departamento de Biocatálisis, Instituto de Catálisis-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain
2
Food Biotechnology Division, Biotechnology Research Center (CRBt), Ali Mendjeli 91735, Algeria
3
Nature and Life Science Faculty, Ibn Khaldoun University, Tiaret 14000, Algeria
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
5
Departamento de Engenharia Química, Universidade Federal do Ceará, Campus do Pici, Fortaleza 60455-760, Brazil
*
Authors to whom correspondence should be addressed.
Received: 1 August 2017 / Revised: 16 August 2017 / Accepted: 18 August 2017 / Published: 25 August 2017
(This article belongs to the Special Issue Biocatalysis and Biotransformations)
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Abstract

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. View Full-Text
Keywords: glutaraldehyde; enzyme immobilization; enzyme stabilization; enzyme inactivation glutaraldehyde; enzyme immobilization; enzyme stabilization; enzyme inactivation
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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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MDPI and ACS Style

Zaak, H.; Peirce, S.; de Albuquerque, T.L.; Sassi, M.; Fernandez-Lafuente, R. Exploiting the Versatility of Aminated Supports Activated with Glutaraldehyde to Immobilize β-galactosidase from Aspergillus oryzae. Catalysts 2017, 7, 250.

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