Flexible processing technology of coix seed prolamins by combined heat-ultrasound: Effects on their enzymatic hydrolysis characteristics and the hypoglycemic activities of derived peptides

Li, Z.; Shu, Zhang; Bai, Lan; Tang, Huacheng; Zhang, Guifang; Zhang, Jiayu; Meng, Wei; Zhang, Dongjie

doi:10.1016/j.ultsonch.2023.106526

Cited by 5 publications

(2 citation statements)

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“…In addition, coix seed prolamins are rich in Pro, Leu, Ala, and other amino acids. Studies have shown that the inhibitory activity of α-glucosidase is enhanced when the proportion of these amino acids in the active peptide is high [12,13]. The sequence of coix seed prolamins also shows that some peptide fragments have the structural characteristics of α-glucosidase inhibitory peptides [12,13], which is a potential source of hypoglycemic peptides and needs to be developed and studied urgently.…”

Section: Introductionmentioning

confidence: 99%

“…Studies have shown that the inhibitory activity of α-glucosidase is enhanced when the proportion of these amino acids in the active peptide is high [12,13]. The sequence of coix seed prolamins also shows that some peptide fragments have the structural characteristics of α-glucosidase inhibitory peptides [12,13], which is a potential source of hypoglycemic peptides and needs to be developed and studied urgently. To date, the specific configuration and mode of action of α-glucosidase inhibitory peptides derived from coix seed prolamins have not been studied in depth.…”

Section: Introductionmentioning

confidence: 99%

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Screening and Activity Analysis of α-Glucosidase Inhibitory Peptides Derived from Coix Seed Prolamins Using Bioinformatics and Molecular Docking

Li,

Zhang,

Meng

et al. 2023

Foods

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Hydrolysates of coix seed prolamins (CHPs) have an excellent hypoglycemic effect and can effectively inhibit α-glucosidase, which is the therapeutic target enzyme for type 2 diabetes mellitus. However, its hypoglycemic components and molecular mechanisms remain unclear, and its stability in food processing needs to be explored. In this study, four potential α-glucosidase inhibitory peptides (LFPSNPLA, FPCNPLV, HLPFNPQ, LLPFYPN) were identified and screened from CHPs using LC-MS/MS and virtual screening techniques. The results of molecular docking showed that the four peptides mainly inhibited α-glucosidase activity through hydrogen bonding and hydrophobic interactions, with Pro and Leu in the peptides playing important roles. In addition, CHPs can maintain good activity under high temperatures (40~100 °C) and weakly acidic or weakly alkaline conditions (pH 6.0~8.0). The addition of glucose (at 100 °C) and NaCl increased the inhibitory activity of α-glucosidase in CHPs. The addition of metal ions significantly decreased the inhibitory activity of α-glucosidase by CHPs, and their effects varied in magnitude with Cu2+ having the largest effect followed by Zn2+, Fe3+, K+, Mg2+, and Ca2+. These results further highlight the potential of CHPs as a foodborne hypoglycemic ingredient, providing a theoretical basis for the application of CHPs in the healthy food industry.

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