Artículo
One-Step Immobilization and Stabilization of a Recombinant Enterococcus faecium DBFIQ E36 l-Arabinose Isomerase for d-Tagatose Synthesis
de Sousa, Marylane; Melo, Vânia M. M.; Hissa, Denise C.; Manzo, Ricardo Martín
; Mammarella, Enrique José
; Antunes, André Saraiva Leão Marcelo; García, José L.; Pessela, Benevides C.; Gonçalves, Luciana R. B.
![Icon](/themes/CONICETDigital/images/conicet.png)
![Icon](/themes/CONICETDigital/images/conicet.png)
Fecha de publicación:
04/2019
Editorial:
Humana Press
Revista:
Applied Biochemistry And Biotechnology
ISSN:
0273-2289
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
A recombinant l-arabinose isomerase from Enterococcus faecium DBFIQ E36 was immobilized onto multifunctional epoxide supports by chemical adsorption and onto a chelate-activated support via polyhistidine-tag, located on the N-terminal (N-His-L-AI) or on the C-terminal (C-His-L-AI) sequence, followed by covalent bonding between the enzyme and the support. The results were compared to reversible L-AI immobilization by adsorption onto charged agarose supports with improved stability. All the derivatives presented immobilization yields of above 75%. The ionic interaction established between agarose gels containing monoaminoethyl-N-aminoethyl structures (MANAE) and the enzyme was the most suitable strategy for L-AI immobilization in comparison to the chelate-activated agarose. In addition, the immobilized biocatalysts by ionic interaction in MANAE showed to be the most stable, retaining up to 100% of enzyme activity for 60 min at 60 °C and with Km values of 28 and 218 mM for MANAE-N-His-L-AI and MANAE-C-His-L-AI, respectively.
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Articulos(INTEC)
Articulos de INST.DE DES.TECNOL.PARA LA IND.QUIMICA (I)
Articulos de INST.DE DES.TECNOL.PARA LA IND.QUIMICA (I)
Citación
de Sousa, Marylane; Melo, Vânia M. M.; Hissa, Denise C.; Manzo, Ricardo Martín; Mammarella, Enrique José; et al.; One-Step Immobilization and Stabilization of a Recombinant Enterococcus faecium DBFIQ E36 l-Arabinose Isomerase for d-Tagatose Synthesis; Humana Press; Applied Biochemistry And Biotechnology; 188; 4-2019; 310-325
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