Por favor, use este identificador para citar o enlazar este ítem: http://repositorio.ufc.br/handle/riufc/62917
Tipo: Artigo de Periódico
Título : One-step immobilization and stabilization of a recombinant Enterococcus faecium DBFIQ E36 L-Arabinose isomerase for D-Tagatose synthesis
Autor : Sousa, Marylane de
Melo, Vânia M. M.
Hissa, Denise Cavalcante
Manzo, Ricardo M.
Mammarella, Enrique J.
Antunes, André Saraiva Leão Marcelo
García, José L.
Pessela, Benevides C.
Gonçalves, Luciana R. B.
Palabras clave : L-Arabinose isomerase;Chelate-agarose;D-Tagatose;Enterococcus faecium;Immobilization;Enzyme activity
Fecha de publicación : 2018
Editorial : Applied Biochemistry and Biotechnology
Citación : SOUSA, Marylane de et al. One-step immobilization and stabilization of a recombinant Enterococcus faecium DBFIQ E36 L-Arabinose isomerase for D-Tagatose synthesis. Applied Biochemistry and Biotechnology, [s. l.], n. 188, p. 310-325.
Abstract: 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.
URI : http://www.repositorio.ufc.br/handle/riufc/62917
Derechos de acceso: Acesso Aberto
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