Purification and Characterization of Antioxidant Peptide from Sunflower Protein Hydrolysate 

Jian Ren1,2*, Xi-Qun Zheng1,2, Xiao-Lan Liu1,2 and Huan Liu1

1Food and Bioengineering College, Qiqihar University, Qiqihar 161006, Heilongjiang Province, PR China

2Key Laboratory of Processing Agricultural Products of Heilongjiang Province, Qiqihar University, Qiqihar 161006, Heilongjiang Province, PR China

Article history:

Received March 9, 2009
Accepted March 29, 2010

Key words:

antioxidant peptide, sunflower, protein hydrolysate, purification and characterization


Sunflower proteins were hydrolyzed with Flavourzyme for the production of antioxidant peptide. DEAE-Sepharose Fast Flow, Sephadex G-25 gel filtration chromatography and reversed-phase HPLC were consecutively employed to purify a novel sunflower antioxidant peptide, and the ability to inhibit the autoxidation of pyrogallol was expressed as the antioxidative activity of the peptide. The amino acid sequence was identified as Ala-Cys-Ala-His-Asp-Lys-Val by a Q-Tof2 mass spectrometer. This novel peptide exhibited a high antioxidative activity of 79.42 U/mL, which is expected to protect against oxidative damage in living systems in relation to aging and carcinogenesis. Higher antioxidative activities were presumed mainly due to the presence of hydrophobic amino acids in its sequence.


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