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.

Bibliographic Details

Main Authors:	Oliveira Henriques, Rosana, Bork, Jonathan Alexsander, Fernández-Lorente, Gloria, Guisán, José Manuel, Furigo Júnior, Agenor, Oliveira, Débora de, Pessela, Benevides C.
Other Authors:	Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil)
Format:	artículo biblioteca
Published:	Elsevier 2018
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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