Identification and Molecular Binding Mechanism of Novel α-Glucosidase Inhibitory Peptides from Hot-Pressed Peanut Meal Protein Hydrolysates

• Published in: Foods Vol. 12; no. 3; p. 663
• Main Authors: Yang, Xinyu, Wang, Dan, Dai, Yangyong, Zhao, Luping, Wang, Wentao, Ding, Xiuzhen
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.02.2023; MDPI
• Subjects: Acids; Cation exchange; Cation exchanging; Chromatography; Composition; Diabetes; Diabetes mellitus; Digestive system; Enzymes; Food science; Fractions; Gastrointestinal tract; Glucosidase; Health aspects; High performance liquid chromatography; hot-pressed peanut meal protein; Hydrogen bonding; Hydrolases; Hydrolysates; Hydrophobicity; Liquid chromatography; Meals; Molecular docking; molecular mechanism; Molecular weight; Natural products; Nitrogen; Nutritional aspects; Peanuts; Peptides; Protein hydrolysates; Proteins; stability; Substrate inhibition; Subtilisin; Testing; Ultrafiltration; α-Glucosidase; α-glucosidase inhibition; China; United States > US; α-glucosidase inhibition; molecular mechanism; molecular docking; hot-pressed peanut meal protein; stability
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods12030663

Hot-pressed peanut meal protein hydrolysates are rich in Arg residue, but there is a lack of research on their α-glucosidase inhibitory activity. In this study, different proteases were used to produce hot-pressed peanut meal protein hydrolysates (PMHs) to evaluate the α-glucosidase inhibitory activity. All PMHs showed good α-glucosidase inhibitory activity with the best inhibition effect coming from the dual enzyme system of Alcalase and Neutrase with an IC of 5.63 ± 0.19 mg/mL. The fractions with the highest inhibition effect were separated and purified using ultrafiltration and cation exchange chromatography. Four novel α-glucosidase inhibitory peptides (FYNPAAGR, PGVLPVAS, FFVPPSQQ, and FSYNPQAG) were identified by nano-HPLC-MS/MS and molecular docking. Molecular docking showed that peptides could occupy the active pocket of α-glucosidase through hydrogen bonding, hydrophobic interaction, salt bridges, and π-stacking, thus preventing the formation of complexes between α-glucosidase and the substrate. In addition, the α-glucosidase inhibitory activity of PMHs was stable against hot, pH treatment and in vitro gastrointestinal digestion. The study demonstrated that PMHs might be used as a natural anti-diabetic material with the potential to inhibit α-glucosidase.