Mesoporous MgFe2O4@HaP@APTES nanocomposite as scaffold for α-glucosidase coupling

Many natural products contain inhibitory ligands for α-glucosidase, and in recent years, many bioanalytical screening techniques have been developed to help identify and characterize these small molecules from plant extracts. Yet, except Fe3O4 magnetic beads, few other nanoparticles have been described as α-glucosidase immobilization scaffolds for bioanalytical assay development. In this study, we describe the coupling of α-glucosidase to an amino-functionalized magnesium ferrite and hydroxyapatite mesoporous nanocomposite (MgFe2O4@HaP@APTES). The bare nanocomposite was synthesized through the coprecipitation method in aqueous solution, and its structure was investigated by X-ray diffraction and FT-IR, white its textural and magnetic properties were analyzed by BET and VSM analyses, respectively. Amino-functionalization was performed using APTES, and α-glucosidase coupling was achieved through glutaraldehyde crosslinking. We demonstrate that both enzyme activity and magnetic properties are preserved after coupling, suggesting that the nanocomposite system is suitable for further inclusion into bioanalytical platforms for enzyme inhibitor screening. General scheme for obtaining the nanocomposite of MgFe2O4@HaP@APTES@alfa-glucosidase. [Display omitted] •α-Glucosidase was coupled to a mesoporous MgFe2O4@HaP@APTES nanocomposite.•Enzyme activity was preserved after coupling.•Enzyme-coupled nanocomposite magnetic properties were preserved.•Nanocomposite is an excellent addition to scaffolds used for direct enzyme immobilization.