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dc.contributor.author
Nicolás, Paula
dc.contributor.author
Lassalle, Verónica Leticia
dc.contributor.author
Ferreira, María Luján
dc.date.available
2018-08-22T14:09:41Z
dc.date.issued
2017-10-13
dc.identifier.citation
Nicolás, Paula; Lassalle, Verónica Leticia; Ferreira, María Luján; Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol; Springer; Bioprocess And Biosystems Engineering; 41; 2; 13-10-2017; 171-184
dc.identifier.issn
1615-7591
dc.identifier.uri
http://hdl.handle.net/11336/56516
dc.description.abstract
Magnetic biocatalysts offer enormous advantages over traditional ones. Their ability to be isolated by means of a magnet, in combination with their extensive reuse possibilities, makes them highly attractive and competitive from the commercial point of view. In this work, magnetic biocatalysts were prepared by immobilization of Candida antarctica Lipase B (E.C. 3.1.1.3, CALB) on magnetite–lysine nanoparticles. Two methodologies were explored tending to find the optimal biocatalyst in terms of its practical implementation: I—physical adsorption of CALB followed by cross-linking, and II—covalent coupling of the lipase on the nanoparticles surface. Both procedures involved the use of glutaraldehyde (GLUT) as cross-linker or coupling agent, respectively. A range of GLUT concentrations was evaluated in method I and the optimum one, in terms of efficiency and operational stability, was chosen to induce the covalent linkage CALB-support in method II. The chosen test reaction was solvent-free ethyl oleate synthesis. Method I produced operationally unstable catalysts that deactivated totally in four to six cycles. On the other hand, covalently attached CALB (method II) preserved 60% of its initial activity after eight cycles and also retained 90% of its initial activity along 6 weeks in storage. CALB immobilization by covalent linkage using controlled GLUT concentration appears as the optimum methodology to asses efficient and stable biocatalysts. The materials prepared within this work may be competitive with commercially available biocatalysts.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Calb
dc.subject
Glutaraldehyde
dc.subject
Immobilized Calb
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Magnetic Nanoparticles
dc.subject.classification
Biotecnología Industrial
dc.subject.classification
Biotecnología Industrial
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
Immobilization of CALB on lysine-modified magnetic nanoparticles: influence of the immobilization protocol
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-08-21T13:04:21Z
dc.identifier.eissn
1615-7605
dc.journal.volume
41
dc.journal.number
2
dc.journal.pagination
171-184
dc.journal.pais
Alemania
dc.journal.ciudad
Berlín
dc.description.fil
Fil: Nicolás, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
dc.description.fil
Fil: Lassalle, Verónica Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
dc.description.fil
Fil: Ferreira, María Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Planta Piloto de Ingeniería Química. Universidad Nacional del Sur. Planta Piloto de Ingeniería Química; Argentina
dc.journal.title
Bioprocess And Biosystems Engineering
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs00449-017-1855-2
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s00449-017-1855-2


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