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<p>Peanut peptides have high biological activity but are easily hydrolyzed during gastrointestinal transit, which may potentially lead to reduced or lost bioactivity. An effective approach to address this issue is to introduce polyphenols and form peptide-polyphenols complexes via non-covalent. Here, selenium-enriched peanut peptides (SePPs) were prepared from selenium-enriched peanuts by protease hydrolysis through optimizing enzymatic hydrolysis conditions using response surface methodology, and fractionated into P1 (&lt; 3&#xa0;kDa), P2 (3–10&#xa0;kDa), and P3 (&gt; 10&#xa0;kDa) through ultrafiltration fractionation. Next, nine purified complexes were prepared between three peptides and polyphenols including ferulic acid (FA), tea polyphenols (TP), and proanthocyanins (PAC). The content of each free polyphenol was significantly reduced after complexation through HPLC detection. All complexes showed the hydrophobicity decrease, with P1-FA having the lowest value. Meanwhile, P1-FA had the smallest particle size (78.3 ± 2.1&#xa0;nm), excellent dispersibility (polydispersity index, PDI = 0.12 ± 0.01), and more stable structure. Then, antioxidant evaluation indicated the peptide-polyphenols complexes had lower IC50 values for hydroxyl free radical scavenging (2.02&#xa0;mg/mL), ABTS (1.72&#xa0;mg/mL), and DPPH (1.82&#xa0;mg/mL). The selenium content (mg/kg of dry complex solids) of P1-FA was determined to be 2.445&#xa0;mg/kg, which is 36.29% higher than the starting material. Furthermore, after in vitro simulated digestion, the complex P1-FA still maintained relatively high antioxidant activity, demonstrating its prominent in vitro gastrointestinal stability. In conclusion, FA interacts with small molecule peptide through hydrogen bonding networks and hydrophobic microenvironments, synergistically enhancing their stability and antioxidant activities, which provides the theoretical basis for the development of selenium-enriched functional food.</p>

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Preparation, characterization, and antioxidant activities of complexes formed by selenium-enriched peanut peptides and polyphenols

  • 期刊论文

  • 发表日期：

    2026年3月19日

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  • Yunfei Xu,
  • Jiale Niu,
  • Haowei Li,
  • Shihua Chen,
  • Yuansen Hu,
  • Si Chen,
  • Zhiyi Wang,
  • Kai Wang,
  • Yanjie Yi

摘要

Peanut peptides have high biological activity but are easily hydrolyzed during gastrointestinal transit, which may potentially lead to reduced or lost bioactivity. An effective approach to address this issue is to introduce polyphenols and form peptide-polyphenols complexes via non-covalent. Here, selenium-enriched peanut peptides (SePPs) were prepared from selenium-enriched peanuts by protease hydrolysis through optimizing enzymatic hydrolysis conditions using response surface methodology, and fractionated into P1 (< 3 kDa), P2 (3–10 kDa), and P3 (> 10 kDa) through ultrafiltration fractionation. Next, nine purified complexes were prepared between three peptides and polyphenols including ferulic acid (FA), tea polyphenols (TP), and proanthocyanins (PAC). The content of each free polyphenol was significantly reduced after complexation through HPLC detection. All complexes showed the hydrophobicity decrease, with P1-FA having the lowest value. Meanwhile, P1-FA had the smallest particle size (78.3 ± 2.1 nm), excellent dispersibility (polydispersity index, PDI = 0.12 ± 0.01), and more stable structure. Then, antioxidant evaluation indicated the peptide-polyphenols complexes had lower IC50 values for hydroxyl free radical scavenging (2.02 mg/mL), ABTS (1.72 mg/mL), and DPPH (1.82 mg/mL). The selenium content (mg/kg of dry complex solids) of P1-FA was determined to be 2.445 mg/kg, which is 36.29% higher than the starting material. Furthermore, after in vitro simulated digestion, the complex P1-FA still maintained relatively high antioxidant activity, demonstrating its prominent in vitro gastrointestinal stability. In conclusion, FA interacts with small molecule peptide through hydrogen bonding networks and hydrophobic microenvironments, synergistically enhancing their stability and antioxidant activities, which provides the theoretical basis for the development of selenium-enriched functional food.