Izvorni znanstveni članak
Purification and Characterization of Antioxidant Peptide from Sunflower Protein Hydrolysate
Jian Ren
; Food and Bioengineering College, Qiqihar University, Qiqihar 161006, Heilongjiang Province, PR China
Xi-Qun Zheng
; Key Laboratory of Processing Agricultural Products of Heilongjiang Province, Qiqihar University, Qiqihar 161006, Heilongjiang Province, PR China
Xiao-Lan Liu
; Food and Bioengineering College, Qiqihar University, Qiqihar 161006, Heilongjiang Province, PR China
Huan Liu
; Food and Bioengineering College, Qiqihar University, Qiqihar 161006, Heilongjiang Province, PR China
Sažetak
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.
Ključne riječi
antioxidant peptide; sunflower; protein hydrolysate; purification and characterization
Hrčak ID:
61723
URI
Datum izdavanja:
15.12.2010.
Posjeta: 2.748 *