Abstract
Objectives
To improve the potential value of feather, which is a valuable protein resource, we have separated and identified antioxidant peptide(s) from feather hydrolysate.
Results
Feather hydrolysate was prepared by fermentation with Bacillus subtilis S1–4. Antioxidative peptides were separated by sequential acid precipitation, cation exchange, and reversed-phase fast performance liquid chromatography. Finally, a peptide with antioxidative activity was identified as Ser-Asn-Leu-Cys-Arg-Pro-Cys-Gly by MALDI time-of-flight (TOF)/TOF analysis, and determined to represent a portion of feather keratin near its N-terminal. A synthesized peptide with the same sequence was used to characterize its antioxidative properties, including scavenging free radicals, reducing power, and Fe2+ chelation. In terms of the peptide’s amino acid composition, the antioxidative activity might be mainly attributed to Cys and other amino acid residues.
Conclusion
Feather keratin is a good source for the quantitative preparation of antioxidative peptides.
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Acknowledgments
This work is supported in part by the National Science Foundation of China under the Grant (311710204) and the Innovation Team by the Education Department of Sichuan Province under the Grant (13TD0043).
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Min-Yuan Wan and Ge Dong have contributed equally to this work.
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Wan, MY., Dong, G., Yang, BQ. et al. Identification and characterization of a novel antioxidant peptide from feather keratin hydrolysate. Biotechnol Lett 38, 643–649 (2016). https://doi.org/10.1007/s10529-015-2016-9
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DOI: https://doi.org/10.1007/s10529-015-2016-9