Potential of lignin from Canna edulis ker residue in the inhibition of α-d-glucosidase: Kinetics and interaction mechanism merging with docking simulation

- Canna edulis ker residue is a suitable biomass for value added products.
- Structure of lignin extracted from Canna edulis ker residue was analyzed.
- Lignin showed higher α-D-glucosidase inhibition than acarbose.
- Inhibition mechanism of lignin on α-D-glucosidase was predicted by molecular docking.

In this study, we extracted lignin from Canna edulis ker residue. Its chemical structure, inhibitory activity on α-d-glucosidase, and kinetics as well as interaction mechanism were investigated by using spectrum analysis and docking simulation. The isolated lignin was composed by guaiacyl and syringal units, and exhibited stronger inhibition on α-d-glucosidase than acarbose with the half maximal inhibitory concentration at 5.3 ± 0.3 μM. It was a non-competitive inhibitior with Km and Ki values of 0.53 ± 0.02 mM and 0.92 ± 0.12 μM, respectively. It could quench the intrinsic fluorescence of α-d-glucosidase through a static quenching mode. The calculated values of enthalpy and entropy change were 20.8 ± 2.5 kJ mol−1 and 172.7 ± 0.8 J mol−1 K−1, respectively. There was a single binding site on α-d-glucosidase for lignin, and the binding distance was 3.2 nm. The molecular docking analysis exhibited that the hydrogen bonds, hydropholic interaction, and van der Waals forces were the main forces for lignin bind to α-d-glucosidase. This work provides a new insight into the interaction between the lignin and α-d-glucosidase, which might be beneficial to type 2 diabetes with the application of lignin in functional food and pharmacy fields.

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