Work

Improving α-amylase inhibitory activity of simulated gastrointestinal digested pea protein by pH shifting assisted proteolysis

Year: 2024

Type: article

Abstract: 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 (PS2-PF) expressed excellent protein recovery rate (40.06%) and α-amylase inhibitory activity (IC50 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 PS2-PF. 13 of potential α-amylase inhibitory peptides were identified from the digested PS2-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.

Source: Food Chemistry

DOI: 10.1016/j.foodchem.2024.142334

Authors: Jia Lei, Hong Zhang, Qiaojuan Yan, Zhengqiang Jiang, Chang Chang

Institution: China Agricultural University

Language: English

Topic: Protein Hydrolysis and Bioactive Peptides

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $4,620