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.
| Main Authors: | , , , , , , |
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| Other Authors: | |
| Format: | artículo biblioteca |
| Published: |
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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