Puede utilizar el filtro de búsqueda del panel izquierdo para acotar los resultados
Filtro
Tipo de publicación
Todos Libros Revistas
Título
Autor
Palabras clave
ISBN
Acceso DOI
Acceso digital CSIC
Buscar
Datos técnicos
RevistaCatalysts
Año2017
Volumen7
Páginas250
Internacional

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

Autores:Roberto Fernandez-Lafuente
Grupos de investigación: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.

Palabras clave:Enzyme stabilization, Enzyme immobilization, glutaraldehyde, Enzyme inactivation
logo de CSIC