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

• Autor(a) principal: Costa,V. M.
• Data de Publicação: 2016
• Outros Autores: Souza,M. C. M. de, Fechine,P. B. A., Macedo,A. C., Gonçalves,L. R. B.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Brazilian Journal of Chemical Engineering
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322016000300661
• topic: Isoniazid; Magnetic Nanoparticles; Nanobiocatalytic systems; Lipase; Tuberculostatic Drug

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.