Lei Jia, Zhang Hong, Yan Qiaojuan, Jiang Zhengqiang, Chang Chang
Key Laboratory of Food Bioengineering (China National Light Industry), College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China.
College of Engineering, China Agricultural University, Beijing, China.
Food Chem. 2025 Mar 1;467:142334. doi: 10.1016/j.foodchem.2024.142334. Epub 2024 Dec 3.
To mitigate postprandial hyperglycemia, α-amylase inhibitory peptides have been casually prepared by various pretreatments and proteolysis without exploring their impacting mechanisms and digestive stabilities. In this study, pea protein treated by pH 2 shifting followed by flavourzyme hydrolysis (PS-PF) expressed excellent protein recovery rate (40.06 %) and α-amylase inhibitory activity (IC of 6.75 mg/mL) after simulated gastrointestinal digestion. A moderate decrease of α-helix structure (by 10.80 %) but increases of β conformations (by ∼17.75 %) and small molecules (< 5 kDa, 94.73 %) on the pea protein were beneficial to enhance α-amylase inhibition of the digested PS-PF. 13 of potential α-amylase inhibitory peptides were identified from the digested PS-PF to inactivate α-amylase via hydrogen bonding, Pi-Alkyl, Pi-Pi and attractive interactions of phenylalanine, proline, leucine, arginine, glutamic acid and lysine. Overall, pH 2 shifting assisted flavourzyme hydrolysis could be a valuable strategy to enhance α-amylase inhibition of in vitro digested pea protein for diabetes mellitus.
