Effect of quercetin on the in vitro Tartary buckwheat starch digestibility

Abstract

Tartary buckwheat is one of the few pseudocereals with abundant flavonoids and starch. However, there are different views on the digestibility of Tartary buckwheat starch (TBS) because of its particle size and structure. In this study, fluorescence spectrum methods and enzymatic kinetics were used to investigate the interaction between TBS /two glycosidase (α-amylase and α-glucosidase) and quercetin to explore its digestive properties and provide a perspective regarding the application of TBS in functional starch products. The results showed that the interaction between TBS and quercetin was probably weak hydrophobic force and hydrogen bonding. The inhibitory effect of quercetin on α-amylase was better than that on α-glucosidase. The half inhibitory concentrations (IC50) of quercetin to α-amylase and α- glucosidase was (270 ± 3.31) and (544 ± 9.01) μg/mL, respectively. The intrinsic fluorescence of two enzymes was statically quenched by forming a complex with quercetin. Quercetin also increased the microenvironment hydrophilicity of tryptophan residues in glycosidase. In vitro digestion experiment demonstrated that quercetin and TBS co-gelatinized together was more effective to inhibit TBS hydrolysis than quercetin itself alone. In the first-order kinetic and LOS model, quercetin-starch gel structure and quercetin inhibitory activity against enzymes had synergistic effects of the TBS digestion.