Abstract
Papain-treated Black-bone silky fowl (BSF) muscle hydrolysate was subjected to 6 kDa cutoff membrane ultrafiltration, and the resulting BSF peptides (<6 kDa) were purified by two-step reverse-phase high-performance liquid chromatography. The molecular weight (MW) distribution and amino acid composition were investigated for characterization of the BSF peptides. The results showed that the major amino acids of BSF peptides were Glu, Tyr, Lys, Asp, Leu, Ala, Thr and Pro, and the MW was from 281 to 7,982 Da. BSF peptides exhibited a strong antioxidant capacity. At 10 mg/mL, they displayed more powerful \( {\text{O}}_{2}^{ \cdot - } \), DPPH· and ABTS·+ scavenging activity and reducing power than carnosine. The peptide fraction 8 with more hydrophilicity revealed stronger \( {\text{O}}_{2}^{ \cdot - } \) and ABTS·+ scavenging activity and reducing power than BSF peptides and carnosine. Besides, a peptide, separated from fraction 8 and showed the strongest antioxidant capacity, was purified and identified by LC-ESI-MS/MS to be Glu-Pro-Asp-Arg-Tyr (678 Da).
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Acknowledgments
This study was financially supported by the Open Project Program of State Key Laboratory of Food Science and Technology, Nanchang University (No. SKLF-KF-201206), the National Natural Science Foundation of China (No. 20862012), the Objective-Oriented Project of State Key Laboratory of Food Science and Technology (SKLF-MB-200806) and Cheung Kong Scholars Program and Innovative Research Team in University (No. IRT0540).
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Liu, J., Huang, Y., Tian, Y. et al. Purification and identification of novel antioxidative peptide released from Black-bone silky fowl (Gallus gallus domesticus Brisson). Eur Food Res Technol 237, 253–263 (2013). https://doi.org/10.1007/s00217-013-1987-9
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DOI: https://doi.org/10.1007/s00217-013-1987-9