Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach
- Autores
- Manzo, Ricardo Martín; de Sousa, Marylane; Fenoglio, Cecilia Lorena; Gonçalves, Luciana Rocha Barro; Mammarella, Enrique José
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.
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
Fil: de Sousa, Marylane. Universidade Estadual do Ceará; Brasil
Fil: Fenoglio, Cecilia Lorena. Universidad Nacional del Litoral; Argentina
Fil: Gonçalves, Luciana Rocha Barro. Universidade Estadual do Ceará; Brasil
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 - Materia
-
Chitosan
D-Galactose
D-Tagatose
Immobilization
L-Arabinose Isomerase
Multipoint Covalent Attachment - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/73016
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/73016 |
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CONICET Digital (CONICET) |
spelling |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approachManzo, Ricardo Martínde Sousa, MarylaneFenoglio, Cecilia LorenaGonçalves, Luciana Rocha BarroMammarella, Enrique JoséChitosanD-GalactoseD-TagatoseImmobilizationL-Arabinose IsomeraseMultipoint Covalent Attachmenthttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.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; ArgentinaFil: de Sousa, Marylane. Universidade Estadual do Ceará; BrasilFil: Fenoglio, Cecilia Lorena. Universidad Nacional del Litoral; ArgentinaFil: Gonçalves, Luciana Rocha Barro. Universidade Estadual do Ceará; BrasilFil: 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; ArgentinaSpringer Heidelberg2015-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/73016Manzo, Ricardo Martín; de Sousa, Marylane; Fenoglio, Cecilia Lorena; Gonçalves, Luciana Rocha Barro; Mammarella, Enrique José; Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach; Springer Heidelberg; Journal of Industrial Microbiology & Biotechnology; 42; 10; 10-2015; 1325-13401367-5435CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs10295-015-1662-1info:eu-repo/semantics/altIdentifier/doi/10.1007/s10295-015-1662-1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:13:24Zoai:ri.conicet.gov.ar:11336/73016instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:13:25.291CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
title |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
spellingShingle |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach Manzo, Ricardo Martín Chitosan D-Galactose D-Tagatose Immobilization L-Arabinose Isomerase Multipoint Covalent Attachment |
title_short |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
title_full |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
title_fullStr |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
title_full_unstemmed |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
title_sort |
Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach |
dc.creator.none.fl_str_mv |
Manzo, Ricardo Martín de Sousa, Marylane Fenoglio, Cecilia Lorena Gonçalves, Luciana Rocha Barro Mammarella, Enrique José |
author |
Manzo, Ricardo Martín |
author_facet |
Manzo, Ricardo Martín de Sousa, Marylane Fenoglio, Cecilia Lorena Gonçalves, Luciana Rocha Barro Mammarella, Enrique José |
author_role |
author |
author2 |
de Sousa, Marylane Fenoglio, Cecilia Lorena Gonçalves, Luciana Rocha Barro Mammarella, Enrique José |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Chitosan D-Galactose D-Tagatose Immobilization L-Arabinose Isomerase Multipoint Covalent Attachment |
topic |
Chitosan D-Galactose D-Tagatose Immobilization L-Arabinose Isomerase Multipoint Covalent Attachment |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.9 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives. 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 Fil: de Sousa, Marylane. Universidade Estadual do Ceará; Brasil Fil: Fenoglio, Cecilia Lorena. Universidad Nacional del Litoral; Argentina Fil: Gonçalves, Luciana Rocha Barro. Universidade Estadual do Ceará; Brasil 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 |
description |
d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives.d-tagatose is produced from d-galactose by the enzyme l-arabinose isomerase (L-AI) in a commercially viable bioprocess. An active and stable biocatalyst was obtained by modifying chitosan gel structure through reaction with TNBS, d-fructose or DMF, among others. This led to a significant improvement in L-AI immobilization via multipoint covalent attachment approach. Synthetized derivatives were compared with commercial supports such as Eupergit® C250L and glyoxal-agarose. The best chitosan derivative for L-AI immobilization was achieved by reacting 4 % (w/v) d-fructose with 3 % (w/v) chitosan at 50 °C for 4 h. When compared to the free enzyme, the glutaraldehyde-activated chitosan biocatalyst showed an apparent activity of 88.4 U ggel −1 with a 211-fold stabilization factor while the glyoxal-agarose biocatalyst gave an apparent activity of 161.8 U ggel −1 with an 85-fold stabilization factor. Hence, chitosan derivatives were comparable to commercial resins, thus becoming a viable low-cost strategy to obtain high active L-AI insolubilized derivatives. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-10 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/73016 Manzo, Ricardo Martín; de Sousa, Marylane; Fenoglio, Cecilia Lorena; Gonçalves, Luciana Rocha Barro; Mammarella, Enrique José; Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach; Springer Heidelberg; Journal of Industrial Microbiology & Biotechnology; 42; 10; 10-2015; 1325-1340 1367-5435 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/73016 |
identifier_str_mv |
Manzo, Ricardo Martín; de Sousa, Marylane; Fenoglio, Cecilia Lorena; Gonçalves, Luciana Rocha Barro; Mammarella, Enrique José; Chemical improvement of chitosan-modified beads for the immobilization of Enterococcus faecium DBFIQ E36 l-arabinose isomerase through multipoint covalent attachment approach; Springer Heidelberg; Journal of Industrial Microbiology & Biotechnology; 42; 10; 10-2015; 1325-1340 1367-5435 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007%2Fs10295-015-1662-1 info:eu-repo/semantics/altIdentifier/doi/10.1007/s10295-015-1662-1 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Springer Heidelberg |
publisher.none.fl_str_mv |
Springer Heidelberg |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614051025387520 |
score |
13.070432 |