Shiitake polysaccharides acted as a non-competitive inhibitor to α-glucosidase and inhibited glucose transport of digested starch from Caco-2 cells monolayer.

ABSTRACT

The inhibition mechanism of shitake mushroom polysaccharides (Lentinula edodes polysaccharides, LEP) against α-glucosidase was studied by enzyme kinetic assay, fluorescence quenching and molecular docking. The effect of LEP on glucose transport of digested starch was investigated via an in vitro digestion/Caco-2 transwell model. LEP exhibited a stronger inhibiting effect (IC50 = 0.66 mg/mL) than acarbose and presented a non-competitive inhibition mechanism. The interaction between LEP and α-glucosidase primarily involved electrostatic interaction and hydrogen bonding. Molecular docking modelling showed that the four structures of LEP were bound to the allosteric tunnel or adjacent pocket of α-glucosidase via electrostatic force and hydrogen bonds. The (1 â†’ 6)-linkages in LEP structures favoured its binding affinity to the α-glucosidase. The α-glucosidase inhibiting activity of LEP was also found to emanate from the reduction in glucose transport of digested starch as deducted from the in vitro digestion/Caco-2 transwell data. The release of glucose from digested starch cooked with LEP was significantly reduced (33.7%) compared to the digested starch without LEP. The findings from the current study suggest that LEP could be a promising ingredient to inhibit α-glucosidase activity as well as control the level of postprandial blood glucose when incorporated into starchy foods.