Effect of Genistein on Starch Digestion In Vitro and Its Mechanism of Action

• Published in: Foods Vol. 13; no. 17; p. 2809
• Main Authors: Jia, Jianhui, Dou, Boxin, Gao, Man, Zhang, Chujia, Liu, Ying, Zhang, Na
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 04.09.2024
• Subjects: Amylases; Antidiabetics; Bonding agents; Carbohydrates; Cereals; Chemical bonds; Diabetes; Digestion; Digestive enzymes; Enzyme inhibitors; Enzyme kinetics; Enzymes; Fluorescence; Fluorescence spectroscopy; Food; Genistein; Glucose; Glucosidase; Hydrogen bonding; Hydrogen bonds; Hydrophobicity; Hypoglycemia; inhibition mechanism; Metabolic syndrome; Molecular docking; Molecular dynamics; Phytoestrogens; Polyphenols; Spectroscopy; Starch; starch digestion; Starches; α-Amylase; α-Glucosidase; China; starch digestion; inhibition mechanism; α-glucosidase; α-amylase; genistein
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods13172809

The digestive properties of starch are crucial in determining postprandial glycaemic excursions. Genistein, an active phytoestrogen, has the potential to influence starch digestion rates. We investigated the way genistein affected the digestive properties of starch in vitro. We performed enzyme kinetics, fluorescence spectroscopy, molecular docking, and molecular dynamics (MD) simulations for analysing the inhibitory properties of genistein on starch digestive enzymes as well as clarifying relevant mechanism of action. Our findings demonstrated that, following the addition of 10% genistein, the contents of slowly digestible and resistant starches increased by 30.34% and 7.18%, respectively. Genistein inhibited α-amylase and α-glucosidase, with half maximal inhibitory concentrations of 0.69 ± 0.06 and 0.11 ± 0.04 mg/mL, respectively. Genistein exhibits a reversible and non-competitive inhibiting effect on α-amylase, while its inhibition on α-glucosidase is a reversible mixed manner type. Fluorescence spectroscopy indicated that the presence of genistein caused declining fluorescence intensity of the two digestive enzymes. Molecular docking and MD simulations showed that genistein binds spontaneously to α-amylase via hydrogen bonds, hydrophobic interactions, and π-stacking, whereas it binds with α-glucosidase via hydrogen bonds and hydrophobic interactions. These findings suggest the potential for developing genistein as a pharmacologic agent for regulating glycaemic excursions.