Use este identificador para citar ou linkar para este item: http://repositorio.ufc.br/handle/riufc/62905
Tipo: Artigo de Periódico
Título: Alternative Heterologous Expression of l‑Arabinose Isomerase from Enterococcus faecium DBFIQ E36 By Residual Whey Lactose Induction
Autor(es): Souza, Ticiane C. de
Oliveira, Ravena Casemiro
Bezerra, Saulo Gonçalves Santiago
Manzo, Ricardo M
Mammarella, Enrique J
Hissa, Denise Cavalcante
Gonçalves, Luciana R. B
Palavras-chave: Cheese whey;l-Arabinose isomerase;· Escherichia coli expression;d-Tagatose;Auto-induction
Data do documento: 2021
Instituição/Editor/Publicador: Molecular Biotechnology
Citação: SOUZA, Ticiane C. de et al. Alternative Heterologous Expression of l‑Arabinose Isomerase from Enterococcus faecium DBFIQ E36 By Residual Whey Lactose Induction. Molecular Biotechnology,[s. l.], v. 1, n. 63, p. 289-304, 2021.
Abstract: This study reports an alternative strategy for the expression of a recombinant l-AI from Enterococcus faecium DBFIQ E36 by auto-induction using glucose and glycerol as carbon sources and residual whey lactose as inducer agent. Commercial lactose and isopropyl β-d-1-thiogalactopyranoside (IPTG) were also evaluated as inducers for comparison of enzyme expression levels. The enzymatic extracts were purifed by afnity chromatography, characterized, and applied in the bioconversion of d-galactose into d-tagatose. l-AI presented a catalytic activity of 1.67±0.14, 1.52±0.01, and 0.7±0.04 U/mL, when expressed using commercial lactose, lactose from whey, and IPTG, respectively. Higher activities could be obtained by changing the protocol of enzyme extraction and, for instance, the enzymatic extract produced with whey presented a catalytic activity of 3.8 U/mL. The specifc activity of the enzyme extracts produced using lactose (commercial or residual whey) after enzyme purifcation was also higher when compared to the enzyme expressed with IPTG. Best results were achieved when enzyme expression was conducted using 4 g/L of residual whey lactose for 11 h. These results proved the efcacy of an alternative and economic protocol for the efective expression of a recombinant l-AI aiming its high-scale production.
URI: http://www.repositorio.ufc.br/handle/riufc/62905
Tipo de Acesso: Acesso Aberto
Aparece nas coleções:DBIO - Artigos publicados em revista científica

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