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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(es): | 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. |
Palavras-chave: | L-Arabinose isomerase;Chelate-agarose;D-Tagatose;Enterococcus faecium;Immobilization;Enzyme activity |
Data do documento: | 2018 |
Instituição/Editor/Publicador: | Applied Biochemistry and Biotechnology |
Citação: | 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 |
Tipo de Acesso: | Acesso Aberto |
Aparece nas coleções: | DBIO - Artigos publicados em revista científica |
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2018_art_msousa.pdf | 684,42 kB | Adobe PDF | Visualizar/Abrir |
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