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dc.contributor.author
Manzo, Ricardo Martín
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dc.contributor.author
Antunes, André Saraiva Leão Marcelo
dc.contributor.author
de Sousa Mendes, Jocélia
dc.contributor.author
Hissa, Denise Cavalcante
dc.contributor.author
Goncalves, Luciana Rocha Barros
dc.contributor.author
Mammarella, Enrique José
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dc.date.available
2020-06-23T13:18:16Z
dc.date.issued
2019-06
dc.identifier.citation
Manzo, Ricardo Martín; Antunes, André Saraiva Leão Marcelo; de Sousa Mendes, Jocélia; Hissa, Denise Cavalcante; Goncalves, Luciana Rocha Barros; et al.; Biochemical characterization of heat-tolerant recombinant L-arabinose isomerase from Enterococcus faecium DBFIQ E36 strain with feasible applications in D-tagatose production; Humana Press; Molecular Biotechnology; 61; 6; 6-2019; 385-399
dc.identifier.issn
1073-6085
dc.identifier.uri
http://hdl.handle.net/11336/107895
dc.description.abstract
D-Tagatose is a ketohexose, which presents unique properties as a low-calorie functional sweetener possessing a sweet flavor profile similar to D-sucrose and having no aftertaste. Considered a generally recognized as safe (GRAS) substance by FAO/WHO, D-tagatose can be used as an intermediate for the synthesis of other optically active compounds as well as an additive in detergent, cosmetic, and pharmaceutical formulations. This study reports important features for L-arabinose isomerase (EC 5.3.1.4) (L-AI) use in industry. We describe arabinose (araA) gene virulence analysis, gene isolation, sequencing, cloning, and heterologous overexpression of L-AI from the food-grade GRAS bacterium Enterococcus faecium DBFIQ E36 in Escherichia coli and assess biochemical properties of this recombinant enzyme. Recombinant L-AI (rL-AI) was one-step purified to homogeneity by Ni2+-agarose resin affinity chromatography and biochemical characterization revealed low identity with both thermophilic and mesophilic L-AIs but high degree of conservation in residues involved in substrate recognition. Optimal conditions for rL-AI activity were 50 °C, pH 5.5, and 0.3 mM Mn2+, exhibiting a low cofactor concentration requirement and an acidic optimum pH. Half-life at 45 °C and 50 °C were 1427 h and 11 h, respectively, and 21.5 h and 39.5 h at pH 4.5 and 5.6, respectively, showing the high stability of the enzyme in the presence of a metallic cofactor. Bioconversion yield for D-tagatose biosynthesis was 45% at 50 °C after 48 h. These properties highlight the technological potential of E. faecium rL-AI as biocatalyst for D-tagatose production.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Humana Press
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dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
L-ARABINOSE ISOMERASE
dc.subject
D-TAGATOSE
dc.subject
ENTEROCOCCUS FAECIUM
dc.subject
FOOD-GRADE MICROORGANISMS
dc.subject
D-GALACTOSE
dc.subject
BIOCHEMICAL PROPERTIES
dc.subject.classification
Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
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dc.subject.classification
Biotecnología Industrial
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dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
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dc.title
Biochemical characterization of heat-tolerant recombinant L-arabinose isomerase from Enterococcus faecium DBFIQ E36 strain with feasible applications in D-tagatose production
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-06-16T13:40:53Z
dc.journal.volume
61
dc.journal.number
6
dc.journal.pagination
385-399
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
New York
dc.description.fil
Fil: Manzo, Ricardo Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
dc.description.fil
Fil: Antunes, André Saraiva Leão Marcelo. King's College London;
dc.description.fil
Fil: de Sousa Mendes, Jocélia. Universidade Estadual do Ceará; Brasil
dc.description.fil
Fil: Hissa, Denise Cavalcante. Universidade Estadual do Ceará; Brasil
dc.description.fil
Fil: Goncalves, Luciana Rocha Barros. Universidade Estadual do Ceará; Brasil
dc.description.fil
Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
dc.journal.title
Molecular Biotechnology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12033-019-00161-x
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