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dc.contributor.author
Mendes, Adriano
dc.contributor.author
Castro, Heizir
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Rodrigues, Dasciana
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Adriano, Wellington
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Tardioli, Paulo
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Mammarella, Enrique José
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Giordano, Roberto
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Giordano, Raquel
dc.date.available
2017-02-16T15:39:28Z
dc.date.issued
2011-10
dc.identifier.citation
Mendes, Adriano; Castro, Heizir; Rodrigues, Dasciana; Adriano, Wellington; Tardioli, Paulo; et al.; Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts; Springer Heidelberg; Journal Of Industrial Microbiology; 38; 8; 10-2011; 1055-1066
dc.identifier.issn
1367-5435
dc.identifier.uri
http://hdl.handle.net/11336/13098
dc.description.abstract
This work aimed at the production of stabilized derivatives of Thermomyces lanuginosus lipase (TLL) by multipoint covalent immobilization of the enzyme on chitosan-based matrices. The resulting biocatalysts were tested for synthesis of biodiesel by ethanolysis of palm oil. Different hydrogels were prepared: chitosan alone and in polyelectrolyte complexes (PEC) with kappa-carrageenan, gelatin, alginate, and polyvinyl alcohol (PVA). The obtained supports were chemically modified with 2,4,6-trinitrobenzene sulfonic acid (TNBS) to increase support hydrophobicity, followed by activation with different agents such as glycidol (GLY), epichlorohydrin (EPI), and glutaraldehyde (GLU). The chitosan-alginate hydrogel, chemically modified with TNBS, provided derivatives with higher apparent hydrolytic activity (HA(app)) and thermal stability, being up to 45-fold more stable than soluble lipase. The maximum load of immobilized enzyme was 17.5 mg g(-1) of gel for GLU, 7.76 mg g(-1) of gel for GLY, and 7.65 mg g(-1) of gel for EPI derivatives, the latter presenting the maximum apparent hydrolytic activity (364.8 IU g(-1) of gel). The three derivatives catalyzed conversion of palm oil to biodiesel, but chitosan-alginate-TNBS activated via GLY and EPI led to higher recovered activities of the enzyme. Thus, this is a more attractive option for both hydrolysis and transesterification of vegetable oils using immobilized TLL, although industrial application of this biocatalyst still demands further improvements in its half-life to make the enzymatic process economically attractive.
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application/pdf
dc.language.iso
eng
dc.publisher
Springer Heidelberg
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Multipoint Covalent Immobilization
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Thermomyces Lanuginosus Lipase
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Chitosan
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Polyelectrolyte Complexes
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Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
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Biotecnología Industrial
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-02-09T13:51:29Z
dc.journal.volume
38
dc.journal.number
8
dc.journal.pagination
1055-1066
dc.journal.pais
Alemania
dc.journal.ciudad
Heidelberg
dc.description.fil
Fil: Mendes, Adriano. Universidade Federal do Sao Carlos; Brasil
dc.description.fil
Fil: Castro, Heizir. Universidade Federal do Sao Carlos; Brasil
dc.description.fil
Fil: Rodrigues, Dasciana. Universidade Federal do Sao Carlos; Brasil
dc.description.fil
Fil: Adriano, Wellington. Universidade Federal do Sao Carlos; Brasil
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Fil: Tardioli, Paulo. Universidade Federal do Sao Carlos; Brasil
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Fil: Mammarella, Enrique José. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
dc.description.fil
Fil: Giordano, Roberto. Universidade Federal do Sao Carlos; Brasil
dc.description.fil
Fil: Giordano, Raquel. Universidade Federal do Sao Carlos; Brasil
dc.journal.title
Journal Of Industrial Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10295-010-0880-9
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs10295-010-0880-9
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