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<p>In the present investigation, a novel antioxidant peptide designated as LMPH-PII was isolated from loach mucus protein (LMP) hydrolysates prepared using Alcalase. The peptide was purified through a multi-step separation process, beginning with ultrafiltration using membranes with molecular weight cut-offs of 100, 10, and 3&#xa0;kDa, followed by gel filtration chromatography on Sephadex G-15, and finally completed with reversed-phase high-performance liquid chromatography (RP-HPLC). This procedure led to the successful acquisition of a highly active antioxidant peptide fraction (&lt; 3&#xa0;kDa). Matrix-assisted laser desorption ionization–time-of-flight mass spectrometry (MALDI-TOF-MS) was used for de novo sequencing, through which the amino acid sequence was further characterized. The peptide was identified to contain 12 amino acids, have a molecular mass of 1352.10 Da, and possess the amino acid sequence SLIGRTLVVHEK. The fractionated fraction (LMPH-PII) exhibited significant antioxidant activities, including DPPH radical scavenging (44.65 ± 0.23%), hydroxyl radical scavenging (34.12 ± 0.09%) and reducing power (0.124 ± 0.004) at 1&#xa0;mg/mL. The results demonstrated that antioxidant activity was significantly enhanced following isolation and fractionation. The peptide separated from the sample presents application potential as a functional component in food items and pharmaceutical formulations, thereby facilitating the utilization of underused loach mucus protein.</p>

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Fractionation, identification and antioxidant activity of a novel peptide from loach (Misgurnus anguillicaudatus) skin mucus protein hydrolysates

  • 期刊论文

  • 发表日期：

    2026年3月10日

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  • Li Li,
  • Na Cheng,
  • Shuwen Chen,
  • Jie Zheng,
  • Aijun Hu,
  • Xiaoyi Wang,
  • Hui Yu

摘要

In the present investigation, a novel antioxidant peptide designated as LMPH-PII was isolated from loach mucus protein (LMP) hydrolysates prepared using Alcalase. The peptide was purified through a multi-step separation process, beginning with ultrafiltration using membranes with molecular weight cut-offs of 100, 10, and 3 kDa, followed by gel filtration chromatography on Sephadex G-15, and finally completed with reversed-phase high-performance liquid chromatography (RP-HPLC). This procedure led to the successful acquisition of a highly active antioxidant peptide fraction (< 3 kDa). Matrix-assisted laser desorption ionization–time-of-flight mass spectrometry (MALDI-TOF-MS) was used for de novo sequencing, through which the amino acid sequence was further characterized. The peptide was identified to contain 12 amino acids, have a molecular mass of 1352.10 Da, and possess the amino acid sequence SLIGRTLVVHEK. The fractionated fraction (LMPH-PII) exhibited significant antioxidant activities, including DPPH radical scavenging (44.65 ± 0.23%), hydroxyl radical scavenging (34.12 ± 0.09%) and reducing power (0.124 ± 0.004) at 1 mg/mL. The results demonstrated that antioxidant activity was significantly enhanced following isolation and fractionation. The peptide separated from the sample presents application potential as a functional component in food items and pharmaceutical formulations, thereby facilitating the utilization of underused loach mucus protein.