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<p>Selenium (Se)-enriched <i>Pleurotus ostreatus</i> has become one of the important sources to safely supply the body with organic selenium. However, the composition and immunomodulatory activities of Se-containing peptides in <i>P. ostreatus</i> (SPP) remain unclear. In this study, we isolated Se-containing protein with the Se content of 204.77 ± 0.002&#xa0;mg/kg from <i>P. ostreatus</i> and enzymatically hydrolyzed it to obtain protein hydrolysates. Among the hydrolysates catalyzed by six proteases, the alkaline protease showed the highest degree of hydrolysis and produced the strongest DPPH scavenging hydrolysates. Moreover, two major peptide fractions (SPP-1 and SPP-2) were obtained from filtered peptides. The RAW264.7 cell model was further employed for screening immunomodulatory Se-containing peptides. SPP-2 could significantly enhance the phagocytic capacity and promote the ROS, NO, TNF-α, IL-6 and IL-1β secretion of macrophages. 11 tetrapeptides with high stability (SeCLPR, LSeCPR, KLVSeM, SeCRPL, SeCRLP, SeCPLR, SeMQPR, SeCAPL, ASeCPL, KSeMPR and SeCDLF) were further identified from the SPP-2 fraction. The molecular docking results showed that these tetrapeptides exhibited strong affinity with different immune proteins. SeCLPR and KLVSeM were found to be two novel Se-containing peptides, which exhibited stronger immunological activities than SPP-2. These results indicated that Se-enriched <i>P. ostreatus</i> could be a promising source of immunomodulatory peptides.</p>

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Identification of selenopeptides from selenium-enriched Pleurotus ostreatus protein hydrolysates and their immune-enhancing effects in macrophages

  • 期刊论文

  • 发表日期：

    2026年4月1日

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  • Rumeng You,
  • Jie Xu,
  • Jinying Min,
  • Shi Wang,
  • Yili Hu,
  • Xiaoling Chen,
  • Mengmeng Ren,
  • Xiaolong Ma,
  • Shaopeng Zhang

摘要

Selenium (Se)-enriched Pleurotus ostreatus has become one of the important sources to safely supply the body with organic selenium. However, the composition and immunomodulatory activities of Se-containing peptides in P. ostreatus (SPP) remain unclear. In this study, we isolated Se-containing protein with the Se content of 204.77 ± 0.002 mg/kg from P. ostreatus and enzymatically hydrolyzed it to obtain protein hydrolysates. Among the hydrolysates catalyzed by six proteases, the alkaline protease showed the highest degree of hydrolysis and produced the strongest DPPH scavenging hydrolysates. Moreover, two major peptide fractions (SPP-1 and SPP-2) were obtained from filtered peptides. The RAW264.7 cell model was further employed for screening immunomodulatory Se-containing peptides. SPP-2 could significantly enhance the phagocytic capacity and promote the ROS, NO, TNF-α, IL-6 and IL-1β secretion of macrophages. 11 tetrapeptides with high stability (SeCLPR, LSeCPR, KLVSeM, SeCRPL, SeCRLP, SeCPLR, SeMQPR, SeCAPL, ASeCPL, KSeMPR and SeCDLF) were further identified from the SPP-2 fraction. The molecular docking results showed that these tetrapeptides exhibited strong affinity with different immune proteins. SeCLPR and KLVSeM were found to be two novel Se-containing peptides, which exhibited stronger immunological activities than SPP-2. These results indicated that Se-enriched P. ostreatus could be a promising source of immunomodulatory peptides.