NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

AUTOR(ES)

Costa, V. M., Souza, M. C. M. de, Fechine, P. B. A., Macedo, A. C., Gonçalves, L. R. B.

FONTE

Braz. J. Chem. Eng.

DATA DE PUBLICAÇÃO

2016-09

RESUMO

Abstract Superparamagnetic nanomaterials have attracted interest in many areas due to the high saturation magnetization and surface area. For enzyme immobilization, these properties favor the enzyme-support contact during the immobilization reaction and easy separation from the reaction mixture by use of low-cost magnetic processes. Iron oxide magnetic nanoparticles (Fe3O4, MNPs), produced by the co-precipitation method, functionalized with 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GLU), were evaluated as a solid support for Candida antarctica lipase B (CALB) immobilization. The nanomagnetic derivative (11nm) obtained after CALB immobilization (MNPs/APTES/GLU/CALB) was evaluated as biocatalyst in isoniazide (INH) synthesis using ethyl isonicotinate (INE) and hydrazine hydrate (HID) as substrates, in 1,4-dioxane. The results showed that MNPs/APTES/CALB had a similar performance when compared to a commercial enzyme Novozym 435, showing significant advantages over other biocatalysts, such as Rhizhomucor miehei lipase (RML) and CALB immobilized on non-conventional, low-cost, chitosan-based supports.

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