Immobilization of α-amylase on mesoporous silica nanoparticles as a target fishing tool for rapid affinity recognition of an active component from Schisandra chinensis (Turcz.) Baill

α-Amylase inhibitors constitute a category of compounds capable of diminishing α-amylase activity and hold significant promise for the development of novel drugs. This study focused on assessing the potential of Schisandra chinensis Baill extract to inhibit α-amylase. However, sieving and segregating inhibitors from intricate mixtures presents an obstacle. Consequently, this study devised and refined a methodology centered on immobilized α-amylase to identify and isolate natural inhibitors from S. chinensis . The immobilized α-amylase, featuring a load capacity of 254.18 ± 1.20 μg/mg and a specific activity of 2.69 ± 0.01 U/mg, was achieved through meticulous optimization of preparation conditions. Subsequently, this immobilized enzyme was used to isolate bioactive compounds from S. chinensis extract. The results revealed the presence of an active compound with an IC 50 of 324.12 ± 11.23 μg/mL. This compound was isolated via magnetic immobilized enzyme-based ligand fishing, employing high-speed countercurrent chromatography , and was conclusively identified as 5-hydroxymethylfurfural. The molecular docking analyses revealed its ability to interact with the active pocket of α-amylase through multiple hydrogen bonds .