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Purification and characterisation of a novel antioxidant peptide from porcine haemoglobin hydrolysate

Authors

  • Qian Sun,

    1. College of Food Science & Nutritional Engineering, China Agricultural University; Beijing Higher Institution Engineering Research Center of Animal Product. Beijing 100083, China
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  • Yongkang Luo,

    Corresponding author
    1. College of Food Science & Nutritional Engineering, China Agricultural University; Beijing Higher Institution Engineering Research Center of Animal Product. Beijing 100083, China
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  • Huixing Shen,

    1. College of Science, China Agricultural University, Beijing 100083, China
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  • Xue Li,

    1. College of Food Science & Nutritional Engineering, China Agricultural University; Beijing Higher Institution Engineering Research Center of Animal Product. Beijing 100083, China
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  • Lei Yao

    1. College of Food Science & Nutritional Engineering, China Agricultural University; Beijing Higher Institution Engineering Research Center of Animal Product. Beijing 100083, China
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Correspondent: Fax: +86 10 62737385;
e-mails: luoyongkang@263.net or luoyongkang@cau.edu.cn

Summary

Porcine haemoglobin, which is normally discarded as a by-product of meat industry, was hydrolysed using pepsin, AS1398 neutrase, trypsin, flavorzyme, papain and alcalase respectively. The peptic hydrolysate exhibited the highest antioxidant activities than those of other hydrolysates, which was separated using ultrafiltration membranes, and consecutively using chromatographic methods including ion-exchange chromatography on SP Sephadex C-25 column, gel filtration chromatography on Sephadex G-25 column and reversed-phase high performance liquid chromatography. Finally, a novel antioxidant peptide from porcine haemoglobin (APPH) was purified, and its sequence was identified to be ARRLGHDFNPDVQAA (1666 Da) using mass spectrometry. APPH exhibited significant higher lipid peroxidation inhibitory ability than that of α-tocopherol as positive control (< 0.05), and efficiently quenched hydroxyl radical (IC50 = 26.9 μm). APPH agrees with the 115–129 residues of the β-chain from porcine haemoglobin. These results indicate that APPH would be a beneficial ingredient for functional food and pharmaceuticals.

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