Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization
This article describes a model for co-immobilization of multiple enzymes onto a magnetic support. Lipase from Thermomyces lanuginosus (TLL) and β-D-galactosidase from Kluyveromyces lactis (βGal) were selected for this study. TLL was immobilized onto hydrophobic magnetic nanoparticles from magnetite (FeO) by a physical adsorption mechanism and was modified by chemical amination of surface carboxylic groups with ethylenediamine using a 1-ethyl-3-(dimethylaminopropyl) carbodiimide coupling method. The enzymatic derivate containing the adsorbed lipase had a 5–fold factor hyperactivation after the immobilization, and the residual activity decreased by 40% after chemical amination. βGal was co-immobilized on the aminated derivate by ion exchange. The post-treatment of the co-immobilized derivate with each of the cross-linking agents (glutaraldehyde and aldehyde-dextran) was studied to improve the stability of the enzymes. The derivates showed a better thermal stability than the enzymes in their free form (50 °C for TLL and 30 °C for βGal), increasing their thermal stabilities, and allowing their use over a wide pH range and up to 50 °C for βGal and up to 70 °C after the cross-linking step.
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Elsevier
2018
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Subjects: | Enzyme co-immobilization, Magnetic nanoparticles, |
Online Access: | http://hdl.handle.net/10261/192169 http://dx.doi.org/10.13039/501100003593 |
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dig-cial-es-10261-1921692020-12-12T16:57:49Z Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization Oliveira Henriques, Rosana Bork, Jonathan Alexsander Fernández-Lorente, Gloria Guisán, José Manuel Furigo Júnior, Agenor Oliveira, Débora de Pessela, Benevides C. Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) Enzyme co-immobilization Magnetic nanoparticles This article describes a model for co-immobilization of multiple enzymes onto a magnetic support. Lipase from Thermomyces lanuginosus (TLL) and β-D-galactosidase from Kluyveromyces lactis (βGal) were selected for this study. TLL was immobilized onto hydrophobic magnetic nanoparticles from magnetite (FeO) by a physical adsorption mechanism and was modified by chemical amination of surface carboxylic groups with ethylenediamine using a 1-ethyl-3-(dimethylaminopropyl) carbodiimide coupling method. The enzymatic derivate containing the adsorbed lipase had a 5–fold factor hyperactivation after the immobilization, and the residual activity decreased by 40% after chemical amination. βGal was co-immobilized on the aminated derivate by ion exchange. The post-treatment of the co-immobilized derivate with each of the cross-linking agents (glutaraldehyde and aldehyde-dextran) was studied to improve the stability of the enzymes. The derivates showed a better thermal stability than the enzymes in their free form (50 °C for TLL and 30 °C for βGal), increasing their thermal stabilities, and allowing their use over a wide pH range and up to 50 °C for βGal and up to 70 °C after the cross-linking step. The authors thank CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico) for the Science without Borders SWE scholarship (200577/2014-0); the Instituto de Investigación en Ciencias de la Alimentación, CIAL-CSIC for helping to develop this research work; and Laboratório Central de Microscopia Eletrônica (LCME) at Federal University of Santa Catarina for the microscopy analysis. Peer Reviewed 2019-10-04T10:54:06Z 2019-10-04T10:54:06Z 2018 2019-10-04T10:54:07Z artículo http://purl.org/coar/resource_type/c_6501 doi: 10.1016/j.mcat.2018.04.022 issn: 2468-8231 Molecular Catalysis 453: 12-21 (2018) http://hdl.handle.net/10261/192169 10.1016/j.mcat.2018.04.022 http://dx.doi.org/10.13039/501100003593 Sí none Elsevier |
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Enzyme co-immobilization Magnetic nanoparticles Enzyme co-immobilization Magnetic nanoparticles Oliveira Henriques, Rosana Bork, Jonathan Alexsander Fernández-Lorente, Gloria Guisán, José Manuel Furigo Júnior, Agenor Oliveira, Débora de Pessela, Benevides C. Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization |
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This article describes a model for co-immobilization of multiple enzymes onto a magnetic support. Lipase from Thermomyces lanuginosus (TLL) and β-D-galactosidase from Kluyveromyces lactis (βGal) were selected for this study. TLL was immobilized onto hydrophobic magnetic nanoparticles from magnetite (FeO) by a physical adsorption mechanism and was modified by chemical amination of surface carboxylic groups with ethylenediamine using a 1-ethyl-3-(dimethylaminopropyl) carbodiimide coupling method. The enzymatic derivate containing the adsorbed lipase had a 5–fold factor hyperactivation after the immobilization, and the residual activity decreased by 40% after chemical amination. βGal was co-immobilized on the aminated derivate by ion exchange. The post-treatment of the co-immobilized derivate with each of the cross-linking agents (glutaraldehyde and aldehyde-dextran) was studied to improve the stability of the enzymes. The derivates showed a better thermal stability than the enzymes in their free form (50 °C for TLL and 30 °C for βGal), increasing their thermal stabilities, and allowing their use over a wide pH range and up to 50 °C for βGal and up to 70 °C after the cross-linking step. |
author2 |
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) |
author_facet |
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) Oliveira Henriques, Rosana Bork, Jonathan Alexsander Fernández-Lorente, Gloria Guisán, José Manuel Furigo Júnior, Agenor Oliveira, Débora de Pessela, Benevides C. |
format |
artículo |
topic_facet |
Enzyme co-immobilization Magnetic nanoparticles |
author |
Oliveira Henriques, Rosana Bork, Jonathan Alexsander Fernández-Lorente, Gloria Guisán, José Manuel Furigo Júnior, Agenor Oliveira, Débora de Pessela, Benevides C. |
author_sort |
Oliveira Henriques, Rosana |
title |
Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization |
title_short |
Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization |
title_full |
Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization |
title_fullStr |
Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization |
title_full_unstemmed |
Co-immobilization of lipases and β-D-galactosidase onto magnetic nanoparticle supports: Biochemical characterization |
title_sort |
co-immobilization of lipases and β-d-galactosidase onto magnetic nanoparticle supports: biochemical characterization |
publisher |
Elsevier |
publishDate |
2018 |
url |
http://hdl.handle.net/10261/192169 http://dx.doi.org/10.13039/501100003593 |
work_keys_str_mv |
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_version_ |
1777671333009686528 |