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- W2556404654 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." @default.
- W2556404654 created "2016-11-30" @default.
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- W2556404654 date "2016-09-01" @default.
- W2556404654 modified "2023-10-15" @default.
- W2556404654 title "NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY" @default.
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- W2556404654 doi "https://doi.org/10.1590/0104-6632.20160333s20150137" @default.
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