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<p>Data on the isolation of antioxidant peptides from sheep brain albumin hydrolysate are presented. The sheep brain albumin hydrolysates were separated by anion-exchange chromatography over DEAE-650M. Five peaks for peptides with molecular mass &lt;20 kDa were obtained. The peptides contained large amounts of hydrophobic, hydrophilic, and acidic amino acids and large amounts of His, Gly, Glu, Phe, Val, Tyr, Asp, and Leu, which possessed the highest antioxidant activity. The removal of ABTS free radicals in NaCl (0.2 M) was 82.36 ± 1.16%; chelating ability for Cu ions, 57.93 ± 0.22%, chelating ability for Fe ions, 65.95 ± 1.00%. LC-MS/MS identified two spots in two-dimensional gel electrophoresis (2-DE). Spots 15 and 27 contained the 14,728 kDa hybrid protein ubiquitin with eL40 ribosomal protein, which consisted of 51.6% and 43%, respectively.</p>

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Isolation and Purification of Antioxidant Peptides from Fermented Hydrolysates of Sheep Brain Proteins

  • 期刊论文

  • 发表日期：

    2025年11月21日

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  • R. Kelaimu,
  • H. He,
  • N. Dongmulati,
  • Z. Yang,
  • Y. Ali,
  • Y. Gao,
  • A. Wali,
  • G. Mavlonov,
  • A. Yili,
  • H. A. Aisa

摘要

Data on the isolation of antioxidant peptides from sheep brain albumin hydrolysate are presented. The sheep brain albumin hydrolysates were separated by anion-exchange chromatography over DEAE-650M. Five peaks for peptides with molecular mass <20 kDa were obtained. The peptides contained large amounts of hydrophobic, hydrophilic, and acidic amino acids and large amounts of His, Gly, Glu, Phe, Val, Tyr, Asp, and Leu, which possessed the highest antioxidant activity. The removal of ABTS free radicals in NaCl (0.2 M) was 82.36 ± 1.16%; chelating ability for Cu ions, 57.93 ± 0.22%, chelating ability for Fe ions, 65.95 ± 1.00%. LC-MS/MS identified two spots in two-dimensional gel electrophoresis (2-DE). Spots 15 and 27 contained the 14,728 kDa hybrid protein ubiquitin with eL40 ribosomal protein, which consisted of 51.6% and 43%, respectively.