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<p>This work aimed to discover potential peptides with antidiabetic properties by inhibiting the enzymes <i>α</i>-amylase and <i>α</i>-glucosidase. After undergoing simulated gastrointestinal digestion (SGID), the protein digestion rate was determined to be 66.98%. SDS-PAGE analysis demonstrated that SGID effectively promoted the digestion of peanut protein, leading to the formation of smaller peptides. The digested protein exhibited significant inhibition of <i>α</i>-amylase and <i>α</i>-glucosidase. The inhibitory activity of both enzymes was higher in the FIII fraction (&lt; 3 kDa) obtained through ultrafiltration. This fraction was further purified using gel filtration chromatography to produce sub-fractions (SF). Among these SFs, FIII-SF5 exhibited the highest activity (<i>p</i> &lt; 0.05) in terms of inhibiting <i>α</i>-amylase (IC<sub>50</sub> of 9.48 mg/mL) and <i>α</i>-glucosidase (IC<sub>50</sub> of 7.52 mg/mL). It was subsequently purified using RP-HPLC to produce sub-sub-fractions (SSF), and FIII-SF5-SSF3 was identified as the most active (<i>p</i> &lt; 0.05) with IC<sub>50</sub> of 1.80 mg/mL for <i>α</i>-amylase and 1.23 mg/mL for <i>α</i>-glucosidase. LC–MS/MS was then utilized to determine the peptide sequences. In this study, two novel peptides, Asp-Asn-Leu-Pro (458.19 Da, IC<sub>50</sub> of 1.37 and 0.95 mg/mL) and Gln-Leu-Pro (357.18 Da, IC<sub>50</sub> of 1.96 and 1.57 mg/mL), were successfully discovered as <i>α</i>-amylase and <i>α</i>-glucosidase inhibitors. Additionally, both peptides demonstrated antiglycation activity, with IC<sub>50</sub> values of 280.46 and 110.39 μg/mL, respectively. These results indicate that peptides derived from peanut protein are promising natural components for diabetes management applications and could serve as a novel source of antidiabetic peptides, offering potential benefits in the functional and health food sector.</p>

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In vitro simulated gastrointestinal digestion and identification of novel antidiabetic peptides from isolated peanut protein

  • 期刊论文

  • 发表日期：

    2025年6月27日

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  • Wedad Q. AL-Bukhaiti,
  • Anwar Noman,
  • Sam Al-Dalali,
  • Hanxiang Li,
  • Sherif M. Abed,
  • Shulin Deng,
  • Liyun Zhao,
  • Sheng-Xiang Qiu

摘要

This work aimed to discover potential peptides with antidiabetic properties by inhibiting the enzymes α-amylase and α-glucosidase. After undergoing simulated gastrointestinal digestion (SGID), the protein digestion rate was determined to be 66.98%. SDS-PAGE analysis demonstrated that SGID effectively promoted the digestion of peanut protein, leading to the formation of smaller peptides. The digested protein exhibited significant inhibition of α-amylase and α-glucosidase. The inhibitory activity of both enzymes was higher in the FIII fraction (< 3 kDa) obtained through ultrafiltration. This fraction was further purified using gel filtration chromatography to produce sub-fractions (SF). Among these SFs, FIII-SF5 exhibited the highest activity (p < 0.05) in terms of inhibiting α-amylase (IC50 of 9.48 mg/mL) and α-glucosidase (IC50 of 7.52 mg/mL). It was subsequently purified using RP-HPLC to produce sub-sub-fractions (SSF), and FIII-SF5-SSF3 was identified as the most active (p < 0.05) with IC50 of 1.80 mg/mL for α-amylase and 1.23 mg/mL for α-glucosidase. LC–MS/MS was then utilized to determine the peptide sequences. In this study, two novel peptides, Asp-Asn-Leu-Pro (458.19 Da, IC50 of 1.37 and 0.95 mg/mL) and Gln-Leu-Pro (357.18 Da, IC50 of 1.96 and 1.57 mg/mL), were successfully discovered as α-amylase and α-glucosidase inhibitors. Additionally, both peptides demonstrated antiglycation activity, with IC50 values of 280.46 and 110.39 μg/mL, respectively. These results indicate that peptides derived from peanut protein are promising natural components for diabetes management applications and could serve as a novel source of antidiabetic peptides, offering potential benefits in the functional and health food sector.